data_1HL4
# 
_entry.id   1HL4 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.279 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   1HL4         
PDBE  EBI-12324    
WWPDB D_1290012324 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
_pdbx_database_related.details 
PDB 2WZ6 unspecified 'G93A SOD1 MUTANT COMPLEXED WITH QUINAZOLINE.' 
PDB 1OEZ unspecified 'ZN HIS46ARG MUTANT OF HUMAN CU, ZN SUPEROXIDE DISMUTASE' 
PDB 1PTZ unspecified 
'CRYSTAL STRUCTURE OF THE HUMAN CU, ZN SUPEROXIDE DISMUTASE,FAMILIAL AMYOTROPHIC LATERAL SCLEROSIS (FALS) MUTANT H43R' 
PDB 1AZV unspecified 'FAMILIAL ALS MUTANT G37R CUZNSOD (HUMAN)' 
PDB 2WYZ unspecified 'L38V SOD1 MUTANT COMPLEXED WITH UMP' 
PDB 1OZU unspecified 
'CRYSTAL STRUCTURE OF FAMILIAL ALS MUTANT S134N OF HUMAN CU,ZN SUPEROXIDE DISMUTASE ( CUZNSOD) TO 1.3A RESOLUTION' 
PDB 2VR6 unspecified 'CRYSTAL STRUCTURE OF G85R ALS MUTANT OF HUMAN CU,ZN SUPEROXIDE DISMUTASE (CUZNSOD) AT 1.3 A RESOLUTION' 
PDB 2C9V unspecified 'ATOMIC RESOLUTION STRUCTURE OF CU-ZN HUMAN SUPEROXIDE DISMUTASE' 
PDB 2WZ5 unspecified 'L38V SOD1 MUTANT COMPLEXED WITH L-METHIONINE .' 
PDB 2XJL unspecified 'MONOMERIC HUMAN CU,ZN SUPEROXIDE DISMUTASE WITHOUT CU LIGANDS' 
PDB 1PU0 unspecified 'STRUCTURE OF HUMAN CU,ZN SUPEROXIDE DISMUTASE' 
PDB 1FUN unspecified 
'SUPEROXIDE DISMUTASE MUTANT WITH LYS 136 REPLACED BY GLU, CYS 6 REPLACED BY ALA AND CYS 111 REPLACED BY SER (K136E, C6A, C111S)' 
PDB 2XJK unspecified 'MONOMERIC HUMAN CU,ZN SUPEROXIDE DISMUTASE' 
PDB 1SOS unspecified 'SUPEROXIDE DISMUTASE MUTANT WITH CYS 6 REPLACED BY ALA AND CYS 111 REPLACED BY SER (C6A, C111S)' 
PDB 1N19 unspecified 'STRUCTURE OF THE HSOD A4V MUTANT' 
PDB 1P1V unspecified 'CRYSTAL STRUCTURE OF FALS-ASSOCIATED HUMAN COPPER-ZINCSUPEROXIDE DISMUTASE (CUZNSOD) MUTANT D125H TO 1.4A' 
PDB 1L3N unspecified 'THE SOLUTION STRUCTURE OF REDUCED DIMERIC COPPER ZINC SOD:THE STRUCTURAL EFFECTS OF DIMERIZATION' 
PDB 2WKO unspecified 'STRUCTURE OF METAL LOADED PATHOGENIC SOD1 MUTANT G93A.' 
PDB 2WZ0 unspecified 'L38V SOD1 MUTANT COMPLEXED WITH ANILINE.' 
PDB 1UXL unspecified 'I113T MUTANT OF HUMAN SOD1' 
PDB 2AF2 unspecified 'SOLUTION STRUCTURE OF DISULFIDE REDUCED AND COPPER DEPLETEDHUMAN SUPEROXIDE DISMUTASE' 
PDB 2VR8 unspecified 'CRYSTAL STRUCTURE OF G85R ALS MUTANT OF HUMAN CU,ZN SUPEROXIDE DISMUTASE (CUZNSOD) AT 1.36 A RESOLUTION' 
PDB 1RK7 unspecified 'SOLUTION STRUCTURE OF APO CU,ZN SUPEROXIDE DISMUTASE: ROLEOF METAL IONS IN PROTEIN FOLDING' 
PDB 2VR7 unspecified 'CRYSTAL STRUCTURE OF G85R ALS MUTANT OF HUMAN CU,ZN SUPEROXIDE DISMUTASE (CUZNSOD) AT 1.58 A RESOLUTION' 
PDB 2V0A unspecified 'ATOMIC RESOLUTION CRYSTAL STRUCTURE OF HUMAN SUPEROXIDE DISMUTASE' 
PDB 1MFM unspecified 'MONOMERIC HUMAN SOD MUTANT F50E/G51E/E133Q AT ATOMIC RESOLUTION' 
PDB 2C9S unspecified '1.24 ANGSTROMS RESOLUTION STRUCTURE OF ZN- ZN HUMAN SUPEROXIDE DISMUTASE' 
PDB 4SOD unspecified 
;CU,ZN SUPEROXIDE DISMUTASE MUTANT WITH CYS 6 REPLACED BY ALA AND CYS 111 REPLACED BY SER (C6A,C111S) WITH AN 18-RESIDUE HEPARIN-BINDING PEPTIDE FUSED TO THE C- TERMINUS (THEORETICAL MODEL)
;
PDB 2WYT unspecified '1.0 A RESOLUTION STRUCTURE OF L38V SOD1 MUTANT' 
PDB 1DSW unspecified 
;THE SOLUTION STRUCTURE OF A MONOMERIC, REDUCED FORM OFHUMAN COPPER, ZINC SUPEROXIDE DISMUTASE BEARING THE SAMECHARGE AS THE NATIVE PROTEIN
;
PDB 1KMG unspecified 'THE SOLUTION STRUCTURE OF MONOMERIC COPPER- FREE SUPEROXIDEDISMUTASE' 
PDB 1OZT unspecified 
'CRYSTAL STRUCTURE OF APO-H46R FAMILIAL ALS MUTANT HUMAN CU,ZN SUPEROXIDE DISMUTASE ( CUZNSOD) TO 2.5A RESOLUTION' 
PDB 1N18 unspecified 'THERMOSTABLE MUTANT OF HUMAN SUPEROXIDE DISMUTASE, C6A,C111S' 
PDB 1BA9 unspecified 'THE SOLUTION STRUCTURE OF REDUCED MONOMERIC SUPEROXIDE DISMUTASE, NMR, 36 STRUCTURES' 
PDB 1HL5 unspecified 'THE STRUCTURE OF HOLO TYPE HUMAN CU, ZN SUPEROXIDE DISMUTASE' 
PDB 2C9U unspecified '1.24 ANGSTROMS RESOLUTION STRUCTURE OF AS- ISOLATED CU-ZN HUMAN SUPEROXIDE DISMUTASE' 
PDB 1UXM unspecified 'A4V MUTANT OF HUMAN SOD1' 
PDB 1SPD unspecified 'SUPEROXIDE DISMUTASE' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        1HL4 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.SG_entry                        . 
_pdbx_database_status.recvd_initial_deposition_date   2003-03-13 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Strange, R.W.'   1 
'Antonyuk, S.'    2 
'Hough, M.A.'     3 
'Doucette, P.'    4 
'Rodriguez, J.'   5 
'Hart, P.J.'      6 
'Hayward, L.J.'   7 
'Valentine, J.S.' 8 
'Hasnain, S.S.'   9 
# 
_citation.id                        primary 
_citation.title                     
;The Structure of Holo and Metal-Deficient Wild-Type Human Cu, Zn Superoxide Dismutase and its Relevance to Familial Amyotrophic Lateral Sclerosis
;
_citation.journal_abbrev            J.Mol.Biol. 
_citation.journal_volume            328 
_citation.page_first                877 
_citation.page_last                 ? 
_citation.year                      2003 
_citation.journal_id_ASTM           JMOBAK 
_citation.country                   UK 
_citation.journal_id_ISSN           0022-2836 
_citation.journal_id_CSD            0070 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   12729761 
_citation.pdbx_database_id_DOI      '10.1016/S0022-2836(03)00355-3' 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Strange, R.W.'   1 
primary 'Antonyuk, S.'    2 
primary 'Hough, M.A.'     3 
primary 'Doucette, P.'    4 
primary 'Rodriguez, J.'   5 
primary 'Hart, P.J.'      6 
primary 'Hayward, L.J.'   7 
primary 'Valentine, J.S.' 8 
primary 'Hasnain, S.S.'   9 
# 
_cell.entry_id           1HL4 
_cell.length_a           156.404 
_cell.length_b           34.978 
_cell.length_c           114.809 
_cell.angle_alpha        90.00 
_cell.angle_beta         112.26 
_cell.angle_gamma        90.00 
_cell.Z_PDB              16 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         1HL4 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
# 
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' 15853.599 4   1.15.1.1 ? ? ? 
2 non-polymer syn 'ZINC ION'             65.409    2   ?        ? ? ? 
3 water       nat water                  18.015    311 ?        ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   yes 
_entity_poly.pdbx_seq_one_letter_code       
;(ACE)ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPK
DEERHVGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;XATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEER
HVGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_entity_poly.pdbx_strand_id                 A,B,C,D 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   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  HIS 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 CYS 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 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               HUMAN 
_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      'HOMO SAPIENS' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'SACCHAROMYCES CEREVISIAE' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     4932 
_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               EG118 
_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               YEP351 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_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 PDB 1HL4       1 ? ? 1HL4   ? 
2 UNP SODC_HUMAN 1 ? ? 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 1HL4 A 1 ? 1   ? 1HL4   0 ? 0   ? 0 0   
2 2 1HL4 A 2 ? 154 ? P00441 2 ? 154 ? 1 153 
3 1 1HL4 B 1 ? 1   ? 1HL4   0 ? 0   ? 0 0   
4 2 1HL4 B 2 ? 154 ? P00441 2 ? 154 ? 1 153 
5 1 1HL4 C 1 ? 1   ? 1HL4   0 ? 0   ? 0 0   
6 2 1HL4 C 2 ? 154 ? P00441 2 ? 154 ? 1 153 
7 1 1HL4 D 1 ? 1   ? 1HL4   0 ? 0   ? 0 0   
8 2 1HL4 D 2 ? 154 ? P00441 2 ? 154 ? 1 153 
# 
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 
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 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
ZN  non-polymer         . 'ZINC ION'      ? 'Zn 2'           65.409  
# 
_exptl.entry_id          1HL4 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.4 
_exptl_crystal.density_percent_sol   45.4 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          ? 
_exptl_crystal_grow.temp            ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              8.00 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.pdbx_details    '0.2M NH4CL, 20%PEG2000, 10% ETHYLENE GLYCOL, 0.1 M MES PH 5.6' 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100.0 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   'ADSC CCD' 
_diffrn_detector.pdbx_collection_date   2002-01-15 
_diffrn_detector.details                MIRRORS 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    'SI 111' 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'SRS BEAMLINE PX14.2' 
_diffrn_source.pdbx_synchrotron_site       SRS 
_diffrn_source.pdbx_synchrotron_beamline   PX14.2 
_diffrn_source.pdbx_wavelength             0.97 
_diffrn_source.pdbx_wavelength_list        ? 
# 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.entry_id                     1HL4 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             50.000 
_reflns.d_resolution_high            1.800 
_reflns.number_obs                   265996 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         98.6 
_reflns.pdbx_Rmerge_I_obs            0.05200 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        20.0000 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              3.400 
# 
_reflns_shell.pdbx_diffrn_id         1 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.d_res_high             1.80 
_reflns_shell.d_res_low              1.86 
_reflns_shell.percent_possible_all   96.3 
_reflns_shell.Rmerge_I_obs           0.35000 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.meanI_over_sigI_obs    2.700 
_reflns_shell.pdbx_redundancy        3.00 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 1HL4 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               'LIKELY RESIDUAL' 
_refine.ls_number_reflns_obs                     47806 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             25.00 
_refine.ls_d_res_high                            1.82 
_refine.ls_percent_reflns_obs                    96.1 
_refine.ls_R_factor_obs                          0.234 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.232 
_refine.ls_R_factor_R_free                       0.283 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.100 
_refine.ls_number_reflns_R_free                  2545 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.951 
_refine.correlation_coeff_Fo_to_Fc_free          0.920 
_refine.B_iso_mean                               27.50 
_refine.aniso_B[1][1]                            -4.96000 
_refine.aniso_B[2][2]                            8.87000 
_refine.aniso_B[3][3]                            -5.95000 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -2.69000 
_refine.aniso_B[2][3]                            0.00000 
_refine.solvent_model_details                    'BABINET MODEL WITH MASK' 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.40 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  'DISORDERED REGIONS IN MONOMERS B AND D WERE REMOVED FROM THE STRUCTURE' 
_refine.pdbx_starting_model                      'PDB ENTRY 1SOS' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       0.164 
_refine.pdbx_overall_ESU_R_Free                  0.160 
_refine.overall_SU_ML                            0.144 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             4.695 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        3997 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         2 
_refine_hist.number_atoms_solvent             311 
_refine_hist.number_atoms_total               4310 
_refine_hist.d_res_high                       1.82 
_refine_hist.d_res_low                        25.00 
# 
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 
r_bond_refined_d             0.016  0.021  ? 4062 'X-RAY DIFFRACTION' ? 
r_bond_other_d               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.819  1.941  ? 5492 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       4.762  3.000  ? 549  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       21.915 15.000 ? 656  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.119  0.200  ? 623  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.007  0.020  ? 3090 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_refined                0.222  0.300  ? 1873 'X-RAY DIFFRACTION' ? 
r_nbd_other                  ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_refined              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_other                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined        0.193  0.500  ? 479  'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_other          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_refined          0.190  0.500  ? 6    'X-RAY DIFFRACTION' ? 
r_metal_ion_other            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined       0.185  0.300  ? 39   'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_other         ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined     0.334  0.500  ? 11   'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_other       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_refined ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_other   ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcbond_it                  1.198  1.500  ? 2714 'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcangle_it                 1.608  2.000  ? 4304 'X-RAY DIFFRACTION' ? 
r_mcangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scbond_it                  2.910  3.000  ? 1348 'X-RAY DIFFRACTION' ? 
r_scbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_it                 3.758  4.500  ? 1188 'X-RAY DIFFRACTION' ? 
r_scangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_long_range_B_other         ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_rigid_bond_restr           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_free            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_bonded          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       1.82 
_refine_ls_shell.d_res_low                        1.87 
_refine_ls_shell.number_reflns_R_work             2938 
_refine_ls_shell.R_factor_R_work                  0.3690 
_refine_ls_shell.percent_reflns_obs               ? 
_refine_ls_shell.R_factor_R_free                  0.3880 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             167 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
loop_
_struct_ncs_oper.id 
_struct_ncs_oper.code 
_struct_ncs_oper.details 
_struct_ncs_oper.matrix[1][1] 
_struct_ncs_oper.matrix[1][2] 
_struct_ncs_oper.matrix[1][3] 
_struct_ncs_oper.matrix[2][1] 
_struct_ncs_oper.matrix[2][2] 
_struct_ncs_oper.matrix[2][3] 
_struct_ncs_oper.matrix[3][1] 
_struct_ncs_oper.matrix[3][2] 
_struct_ncs_oper.matrix[3][3] 
_struct_ncs_oper.vector[1] 
_struct_ncs_oper.vector[2] 
_struct_ncs_oper.vector[3] 
1 given ? 0.763240  -0.016790 -0.645900 -0.025800 -0.999660 -0.004490 -0.645610 0.020090  -0.763410 19.85701 0.08071  53.73026 
2 given ? -0.969750 -0.244100 0.001570  -0.205170 0.811570  -0.547040 0.132260  -0.530820 -0.837100 17.90989 9.16435  51.25463 
3 given ? -0.834840 0.141310  0.532040  0.207630  -0.814280 0.542070  0.509830  0.563010  0.650450  0.75498  -9.10994 3.23855  
# 
_struct.entry_id                  1HL4 
_struct.title                     'The Structure of Apo Type Human Cu, Zn Superoxide Dismutase' 
_struct.pdbx_descriptor           'SUPEROXIDE DISMUTASE (E.C.1.15.1.1)' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        1HL4 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
_struct_keywords.text            'OXIDOREDUCTASE, HUMAN CU, ZN SUPEROXIDE DISMUTASE' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 1 ? 
E N N 2 ? 
F N N 2 ? 
G N N 3 ? 
H N N 3 ? 
I N N 3 ? 
J N N 3 ? 
# 
_struct_biol.id   1 
# 
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 GLU A 133 ? LYS A 137 ? GLU A 132 LYS A 136 5 ? 5 
HELX_P HELX_P3 3 GLY B 57  ? GLY B 62  ? GLY B 56  GLY B 61  5 ? 6 
HELX_P HELX_P4 4 GLU B 134 ? GLY B 139 ? GLU B 133 GLY B 138 1 ? 6 
HELX_P HELX_P5 5 ALA C 56  ? GLY C 62  ? ALA C 55  GLY C 61  5 ? 7 
HELX_P HELX_P6 6 SER C 108 ? HIS C 111 ? SER C 107 HIS C 110 5 ? 4 
HELX_P HELX_P7 7 ALA D 56  ? GLY D 62  ? ALA D 55  GLY D 61  5 ? 7 
# 
_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 ? ? ? ? ? ? ? 2.029 ? 
disulf2 disulf ? ? B CYS 58 SG ? ? ? 1_555 B CYS 147 SG  ? ? B CYS 57  B CYS 146 1_555 ? ? ? ? ? ? ? 2.069 ? 
disulf3 disulf ? ? C CYS 58 SG ? ? ? 1_555 C CYS 147 SG  ? ? C CYS 57  C CYS 146 1_555 ? ? ? ? ? ? ? 2.078 ? 
disulf4 disulf ? ? D CYS 58 SG ? ? ? 1_555 D CYS 147 SG  ? ? D CYS 57  D CYS 146 1_555 ? ? ? ? ? ? ? 2.051 ? 
metalc1 metalc ? ? E ZN  .  ZN ? ? ? 1_555 A HIS 72  ND1 ? ? A ZN  155 A HIS 71  1_555 ? ? ? ? ? ? ? 2.449 ? 
metalc2 metalc ? ? E ZN  .  ZN ? ? ? 1_555 A ASP 84  OD1 ? ? A ZN  155 A ASP 83  1_555 ? ? ? ? ? ? ? 2.083 ? 
metalc3 metalc ? ? E ZN  .  ZN ? ? ? 1_555 A HIS 64  ND1 ? ? A ZN  155 A HIS 63  1_555 ? ? ? ? ? ? ? 2.025 ? 
metalc4 metalc ? ? E ZN  .  ZN ? ? ? 1_555 A HIS 81  ND1 ? ? A ZN  155 A HIS 80  1_555 ? ? ? ? ? ? ? 1.913 ? 
covale1 covale ? ? B ACE 1  C  ? ? ? 1_555 B ALA 2   N   ? ? B ACE 0   B ALA 1   1_555 ? ? ? ? ? ? ? 1.334 ? 
metalc5 metalc ? ? F ZN  .  ZN ? ? ? 1_555 B ASP 84  OD1 ? ? B ZN  155 B ASP 83  1_555 ? ? ? ? ? ? ? 1.897 ? 
metalc6 metalc ? ? F ZN  .  ZN ? ? ? 1_555 B HIS 72  ND1 ? ? B ZN  155 B HIS 71  1_555 ? ? ? ? ? ? ? 2.172 ? 
metalc7 metalc ? ? F ZN  .  ZN ? ? ? 1_555 B HIS 81  ND1 ? ? B ZN  155 B HIS 80  1_555 ? ? ? ? ? ? ? 1.978 ? 
metalc8 metalc ? ? F ZN  .  ZN ? ? ? 1_555 B HIS 64  ND1 ? ? B ZN  155 B HIS 63  1_555 ? ? ? ? ? ? ? 1.971 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
covale ? ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA ? 11 ? 
BA ? 5  ? 
BB ? 4  ? 
CA ? 5  ? 
CB ? 4  ? 
DA ? 5  ? 
DB ? 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 
AA 1  2  ? anti-parallel 
AA 2  3  ? anti-parallel 
AA 3  4  ? anti-parallel 
AA 4  5  ? anti-parallel 
AA 5  6  ? anti-parallel 
AA 6  7  ? anti-parallel 
AA 7  8  ? anti-parallel 
AA 8  9  ? anti-parallel 
AA 9  10 ? anti-parallel 
AA 10 11 ? anti-parallel 
BA 1  2  ? anti-parallel 
BA 2  3  ? anti-parallel 
BA 3  4  ? anti-parallel 
BA 4  5  ? anti-parallel 
BB 1  2  ? anti-parallel 
BB 2  3  ? anti-parallel 
BB 3  4  ? anti-parallel 
CA 1  2  ? anti-parallel 
CA 2  3  ? anti-parallel 
CA 3  4  ? anti-parallel 
CA 4  5  ? anti-parallel 
CB 1  2  ? anti-parallel 
CB 2  3  ? anti-parallel 
CB 3  4  ? anti-parallel 
DA 1  2  ? anti-parallel 
DA 2  3  ? anti-parallel 
DA 3  4  ? anti-parallel 
DA 4  5  ? anti-parallel 
DB 1  2  ? anti-parallel 
DB 2  3  ? anti-parallel 
DB 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 
AA 1  THR A 3   ? GLY A 11  ? THR A 2   GLY A 10  
AA 2  GLN A 16  ? GLN A 23  ? GLN A 15  GLN A 22  
AA 3  VAL A 30  ? LYS A 37  ? VAL A 29  LYS A 36  
AA 4  ALA A 96  ? ASP A 102 ? ALA A 95  ASP A 101 
AA 5  ASP A 84  ? ALA A 90  ? ASP A 83  ALA A 89  
AA 6  GLY A 42  ? HIS A 49  ? GLY A 41  HIS A 48  
AA 7  THR A 117 ? HIS A 121 ? THR A 116 HIS A 120 
AA 8  ARG A 144 ? VAL A 149 ? ARG A 143 VAL A 148 
AA 9  THR A 3   ? GLY A 11  ? THR A 2   GLY A 10  
AA 10 GLN A 16  ? GLN A 23  ? GLN A 15  GLN A 22  
AA 11 THR A 3   ? GLY A 11  ? THR A 2   GLY A 10  
BA 1  ALA B 96  ? ASP B 102 ? ALA B 95  ASP B 101 
BA 2  VAL B 30  ? LYS B 37  ? VAL B 29  LYS B 36  
BA 3  GLN B 16  ? GLU B 22  ? GLN B 15  GLU B 21  
BA 4  LYS B 4   ? LYS B 10  ? LYS B 3   LYS B 9   
BA 5  GLY B 151 ? ILE B 152 ? GLY B 150 ILE B 151 
BB 1  ASP B 84  ? ALA B 90  ? ASP B 83  ALA B 89  
BB 2  GLY B 42  ? HIS B 49  ? GLY B 41  HIS B 48  
BB 3  THR B 117 ? HIS B 121 ? THR B 116 HIS B 120 
BB 4  ARG B 144 ? VAL B 149 ? ARG B 143 VAL B 148 
CA 1  ALA C 96  ? ASP C 102 ? ALA C 95  ASP C 101 
CA 2  VAL C 30  ? LYS C 37  ? VAL C 29  LYS C 36  
CA 3  GLN C 16  ? GLN C 23  ? GLN C 15  GLN C 22  
CA 4  LYS C 4   ? LEU C 9   ? LYS C 3   LEU C 8   
CA 5  GLY C 151 ? ILE C 152 ? GLY C 150 ILE C 151 
CB 1  ASP C 84  ? ALA C 90  ? ASP C 83  ALA C 89  
CB 2  GLY C 42  ? HIS C 49  ? GLY C 41  HIS C 48  
CB 3  THR C 117 ? HIS C 121 ? THR C 116 HIS C 120 
CB 4  ARG C 144 ? VAL C 149 ? ARG C 143 VAL C 148 
DA 1  ALA D 96  ? ASP D 102 ? ALA D 95  ASP D 101 
DA 2  VAL D 30  ? LYS D 37  ? VAL D 29  LYS D 36  
DA 3  GLN D 16  ? GLN D 23  ? GLN D 15  GLN D 22  
DA 4  LYS D 4   ? LYS D 10  ? LYS D 3   LYS D 9   
DA 5  GLY D 151 ? ILE D 152 ? GLY D 150 ILE D 151 
DB 1  ASP D 84  ? ALA D 90  ? ASP D 83  ALA D 89  
DB 2  GLY D 42  ? HIS D 49  ? GLY D 41  HIS D 48  
DB 3  THR D 117 ? HIS D 121 ? THR D 116 HIS D 120 
DB 4  ARG D 144 ? VAL D 149 ? ARG D 143 VAL D 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 
AA 1  2  N LEU A 9   ? N LEU A 8   O GLY A 17  ? O GLY A 16  
AA 2  3  N GLU A 22  ? N GLU A 21  O LYS A 31  ? O LYS A 30  
AA 3  4  N ILE A 36  ? N ILE A 35  O ALA A 96  ? O ALA A 95  
AA 4  5  N ASP A 97  ? N ASP A 96  O THR A 89  ? O THR A 88  
AA 5  6  N ALA A 90  ? N ALA A 89  O GLY A 42  ? O GLY A 41  
AA 6  7  N HIS A 49  ? N HIS A 48  O THR A 117 ? O THR A 116 
AA 7  8  O VAL A 120 ? O VAL A 119 N LEU A 145 ? N LEU A 144 
AA 8  9  N CYS A 147 ? N CYS A 146 O LYS A 10  ? O LYS A 9   
AA 9  10 N LEU A 9   ? N LEU A 8   O GLY A 17  ? O GLY A 16  
AA 10 11 N GLN A 23  ? N GLN A 22  O THR A 3   ? O THR A 2   
BA 1  2  N ASP B 102 ? N ASP B 101 O VAL B 30  ? O VAL B 29  
BA 2  3  N LYS B 37  ? N LYS B 36  O GLN B 16  ? O GLN B 15  
BA 3  4  N PHE B 21  ? N PHE B 20  O ALA B 5   ? O ALA B 4   
BA 4  5  N VAL B 6   ? N VAL B 5   O GLY B 151 ? O GLY B 150 
BB 1  2  N ALA B 90  ? N ALA B 89  O GLY B 42  ? O GLY B 41  
BB 2  3  N HIS B 49  ? N HIS B 48  O THR B 117 ? O THR B 116 
BB 3  4  O VAL B 120 ? O VAL B 119 N LEU B 145 ? N LEU B 144 
CA 1  2  N ASP C 102 ? N ASP C 101 O VAL C 30  ? O VAL C 29  
CA 2  3  N LYS C 37  ? N LYS C 36  O GLN C 16  ? O GLN C 15  
CA 3  4  N PHE C 21  ? N PHE C 20  O ALA C 5   ? O ALA C 4   
CA 4  5  N VAL C 6   ? N VAL C 5   O GLY C 151 ? O GLY C 150 
CB 1  2  N ALA C 90  ? N ALA C 89  O GLY C 42  ? O GLY C 41  
CB 2  3  N HIS C 49  ? N HIS C 48  O THR C 117 ? O THR C 116 
CB 3  4  O VAL C 120 ? O VAL C 119 N LEU C 145 ? N LEU C 144 
DA 1  2  N ASP D 102 ? N ASP D 101 O VAL D 30  ? O VAL D 29  
DA 2  3  N LYS D 37  ? N LYS D 36  O GLN D 16  ? O GLN D 15  
DA 3  4  N PHE D 21  ? N PHE D 20  O ALA D 5   ? O ALA D 4   
DA 4  5  N VAL D 6   ? N VAL D 5   O GLY D 151 ? O GLY D 150 
DB 1  2  N ALA D 90  ? N ALA D 89  O GLY D 42  ? O GLY D 41  
DB 2  3  N HIS D 49  ? N HIS D 48  O THR D 117 ? O THR D 116 
DB 3  4  O VAL D 120 ? O VAL D 119 N LEU D 145 ? N LEU D 144 
# 
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 ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN A 155' 
AC2 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN 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 4 HIS A 64 ? HIS A 63 . ? 1_555 ? 
2 AC1 4 HIS A 72 ? HIS A 71 . ? 1_555 ? 
3 AC1 4 HIS A 81 ? HIS A 80 . ? 1_555 ? 
4 AC1 4 ASP A 84 ? ASP A 83 . ? 1_555 ? 
5 AC2 4 HIS B 64 ? HIS B 63 . ? 1_555 ? 
6 AC2 4 HIS B 72 ? HIS B 71 . ? 1_555 ? 
7 AC2 4 HIS B 81 ? HIS B 80 . ? 1_555 ? 
8 AC2 4 ASP B 84 ? ASP B 83 . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          1HL4 
_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                    1HL4 
_atom_sites.fract_transf_matrix[1][1]   0.006394 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002617 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.028589 
_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]   0.009411 
_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   . ALA A 1 2   ? 3.406   -14.947 28.562  1.00 34.21 ? 1    ALA A N   1 
ATOM   2    C  CA  . ALA A 1 2   ? 2.272   -14.274 27.841  1.00 33.94 ? 1    ALA A CA  1 
ATOM   3    C  C   . ALA A 1 2   ? 1.494   -13.275 28.713  1.00 33.75 ? 1    ALA A C   1 
ATOM   4    O  O   . ALA A 1 2   ? 0.981   -13.618 29.796  1.00 34.77 ? 1    ALA A O   1 
ATOM   5    C  CB  . ALA A 1 2   ? 1.318   -15.323 27.256  1.00 34.07 ? 1    ALA A CB  1 
ATOM   6    N  N   . THR A 1 3   ? 1.379   -12.029 28.265  1.00 32.77 ? 2    THR A N   1 
ATOM   7    C  CA  . THR A 1 3   ? 0.607   -11.110 29.077  1.00 31.10 ? 2    THR A CA  1 
ATOM   8    C  C   . THR A 1 3   ? -0.882  -11.319 28.781  1.00 30.15 ? 2    THR A C   1 
ATOM   9    O  O   . THR A 1 3   ? -1.275  -11.789 27.694  1.00 30.45 ? 2    THR A O   1 
ATOM   10   C  CB  . THR A 1 3   ? 1.118   -9.640  28.962  1.00 30.69 ? 2    THR A CB  1 
ATOM   11   O  OG1 . THR A 1 3   ? 0.292   -8.754  29.740  1.00 34.66 ? 2    THR A OG1 1 
ATOM   12   C  CG2 . THR A 1 3   ? 0.946   -9.144  27.587  1.00 30.88 ? 2    THR A CG2 1 
ATOM   13   N  N   . LYS A 1 4   ? -1.687  -11.070 29.806  1.00 28.89 ? 3    LYS A N   1 
ATOM   14   C  CA  . LYS A 1 4   ? -3.131  -11.183 29.746  1.00 27.94 ? 3    LYS A CA  1 
ATOM   15   C  C   . LYS A 1 4   ? -3.845  -9.948  30.285  1.00 26.50 ? 3    LYS A C   1 
ATOM   16   O  O   . LYS A 1 4   ? -3.412  -9.331  31.259  1.00 27.79 ? 3    LYS A O   1 
ATOM   17   C  CB  . LYS A 1 4   ? -3.570  -12.366 30.575  1.00 27.46 ? 3    LYS A CB  1 
ATOM   18   C  CG  . LYS A 1 4   ? -4.121  -13.504 29.776  1.00 29.80 ? 3    LYS A CG  1 
ATOM   19   C  CD  . LYS A 1 4   ? -4.463  -14.650 30.726  1.00 31.55 ? 3    LYS A CD  1 
ATOM   20   C  CE  . LYS A 1 4   ? -5.929  -15.066 30.631  1.00 32.44 ? 3    LYS A CE  1 
ATOM   21   N  NZ  . LYS A 1 4   ? -6.340  -15.977 31.759  1.00 32.49 ? 3    LYS A NZ  1 
ATOM   22   N  N   . ALA A 1 5   ? -4.977  -9.645  29.666  1.00 25.71 ? 4    ALA A N   1 
ATOM   23   C  CA  . ALA A 1 5   ? -5.795  -8.520  30.044  1.00 24.70 ? 4    ALA A CA  1 
ATOM   24   C  C   . ALA A 1 5   ? -7.274  -8.922  30.078  1.00 24.28 ? 4    ALA A C   1 
ATOM   25   O  O   . ALA A 1 5   ? -7.688  -9.990  29.567  1.00 26.75 ? 4    ALA A O   1 
ATOM   26   C  CB  . ALA A 1 5   ? -5.536  -7.322  29.057  1.00 23.16 ? 4    ALA A CB  1 
ATOM   27   N  N   . VAL A 1 6   ? -8.075  -8.093  30.723  1.00 23.21 ? 5    VAL A N   1 
ATOM   28   C  CA  . VAL A 1 6   ? -9.487  -8.322  30.868  1.00 21.62 ? 5    VAL A CA  1 
ATOM   29   C  C   . VAL A 1 6   ? -10.185 -6.952  30.935  1.00 21.85 ? 5    VAL A C   1 
ATOM   30   O  O   . VAL A 1 6   ? -9.539  -5.953  31.310  1.00 24.43 ? 5    VAL A O   1 
ATOM   31   C  CB  . VAL A 1 6   ? -9.815  -9.249  32.079  1.00 19.58 ? 5    VAL A CB  1 
ATOM   32   C  CG1 . VAL A 1 6   ? -9.457  -8.585  33.404  1.00 21.22 ? 5    VAL A CG1 1 
ATOM   33   C  CG2 . VAL A 1 6   ? -11.285 -9.671  32.078  1.00 20.67 ? 5    VAL A CG2 1 
ATOM   34   N  N   . CYS A 1 7   ? -11.449 -6.923  30.517  1.00 22.61 ? 6    CYS A N   1 
ATOM   35   C  CA  . CYS A 1 7   ? -12.314 -5.755  30.544  1.00 22.45 ? 6    CYS A CA  1 
ATOM   36   C  C   . CYS A 1 7   ? -13.725 -6.144  30.972  1.00 22.10 ? 6    CYS A C   1 
ATOM   37   O  O   . CYS A 1 7   ? -14.306 -7.076  30.421  1.00 25.14 ? 6    CYS A O   1 
ATOM   38   C  CB  . CYS A 1 7   ? -12.436 -5.122  29.165  1.00 20.40 ? 6    CYS A CB  1 
ATOM   39   S  SG  . CYS A 1 7   ? -13.116 -3.435  29.247  1.00 28.75 ? 6    CYS A SG  1 
ATOM   40   N  N   . VAL A 1 8   ? -14.267 -5.422  31.936  1.00 22.54 ? 7    VAL A N   1 
ATOM   41   C  CA  . VAL A 1 8   ? -15.650 -5.579  32.329  1.00 22.26 ? 7    VAL A CA  1 
ATOM   42   C  C   . VAL A 1 8   ? -16.444 -4.456  31.667  1.00 21.80 ? 7    VAL A C   1 
ATOM   43   O  O   . VAL A 1 8   ? -16.156 -3.269  31.845  1.00 23.29 ? 7    VAL A O   1 
ATOM   44   C  CB  . VAL A 1 8   ? -15.857 -5.553  33.860  1.00 20.30 ? 7    VAL A CB  1 
ATOM   45   C  CG1 . VAL A 1 8   ? -17.345 -5.677  34.211  1.00 19.60 ? 7    VAL A CG1 1 
ATOM   46   C  CG2 . VAL A 1 8   ? -15.052 -6.715  34.618  1.00 21.46 ? 7    VAL A CG2 1 
ATOM   47   N  N   . LEU A 1 9   ? -17.430 -4.844  30.883  1.00 22.63 ? 8    LEU A N   1 
ATOM   48   C  CA  . LEU A 1 9   ? -18.277 -3.870  30.217  1.00 21.79 ? 8    LEU A CA  1 
ATOM   49   C  C   . LEU A 1 9   ? -19.532 -3.588  30.993  1.00 21.46 ? 8    LEU A C   1 
ATOM   50   O  O   . LEU A 1 9   ? -20.320 -4.505  31.305  1.00 23.71 ? 8    LEU A O   1 
ATOM   51   C  CB  . LEU A 1 9   ? -18.644 -4.369  28.824  1.00 20.25 ? 8    LEU A CB  1 
ATOM   52   C  CG  . LEU A 1 9   ? -17.777 -4.199  27.574  1.00 22.28 ? 8    LEU A CG  1 
ATOM   53   C  CD1 . LEU A 1 9   ? -16.502 -3.458  27.812  1.00 21.16 ? 8    LEU A CD1 1 
ATOM   54   C  CD2 . LEU A 1 9   ? -17.502 -5.544  26.938  1.00 24.50 ? 8    LEU A CD2 1 
ATOM   55   N  N   . LYS A 1 10  ? -19.763 -2.301  31.246  1.00 22.05 ? 9    LYS A N   1 
ATOM   56   C  CA  . LYS A 1 10  ? -20.978 -1.819  31.869  1.00 23.10 ? 9    LYS A CA  1 
ATOM   57   C  C   . LYS A 1 10  ? -21.345 -0.446  31.316  1.00 23.51 ? 9    LYS A C   1 
ATOM   58   O  O   . LYS A 1 10  ? -20.440 0.352   30.923  1.00 24.20 ? 9    LYS A O   1 
ATOM   59   C  CB  . LYS A 1 10  ? -20.753 -1.656  33.365  1.00 22.06 ? 9    LYS A CB  1 
ATOM   60   C  CG  . LYS A 1 10  ? -21.011 -2.903  34.153  1.00 23.44 ? 9    LYS A CG  1 
ATOM   61   C  CD  . LYS A 1 10  ? -20.205 -2.887  35.438  1.00 26.15 ? 9    LYS A CD  1 
ATOM   62   C  CE  . LYS A 1 10  ? -20.662 -4.046  36.357  1.00 30.06 ? 9    LYS A CE  1 
ATOM   63   N  NZ  . LYS A 1 10  ? -21.304 -5.130  35.543  1.00 34.94 ? 9    LYS A NZ  1 
ATOM   64   N  N   . GLY A 1 11  ? -22.653 -0.191  31.315  1.00 25.46 ? 10   GLY A N   1 
ATOM   65   C  CA  . GLY A 1 11  ? -23.203 1.096   30.926  1.00 26.63 ? 10   GLY A CA  1 
ATOM   66   C  C   . GLY A 1 11  ? -24.357 1.590   31.785  1.00 26.45 ? 10   GLY A C   1 
ATOM   67   O  O   . GLY A 1 11  ? -24.570 1.183   32.949  1.00 28.73 ? 10   GLY A O   1 
ATOM   68   N  N   . ASP A 1 12  ? -25.131 2.503   31.219  1.00 27.70 ? 11   ASP A N   1 
ATOM   69   C  CA  . ASP A 1 12  ? -26.287 3.007   31.919  1.00 27.38 ? 11   ASP A CA  1 
ATOM   70   C  C   . ASP A 1 12  ? -27.423 1.990   31.775  1.00 27.13 ? 11   ASP A C   1 
ATOM   71   O  O   . ASP A 1 12  ? -28.216 1.837   32.691  1.00 29.18 ? 11   ASP A O   1 
ATOM   72   C  CB  . ASP A 1 12  ? -26.731 4.365   31.360  1.00 28.18 ? 11   ASP A CB  1 
ATOM   73   C  CG  . ASP A 1 12  ? -25.769 5.509   31.710  1.00 30.96 ? 11   ASP A CG  1 
ATOM   74   O  OD1 . ASP A 1 12  ? -25.218 5.536   32.844  1.00 35.27 ? 11   ASP A OD1 1 
ATOM   75   O  OD2 . ASP A 1 12  ? -25.511 6.446   30.909  1.00 34.28 ? 11   ASP A OD2 1 
ATOM   76   N  N   . GLY A 1 13  ? -27.497 1.323   30.625  1.00 26.49 ? 12   GLY A N   1 
ATOM   77   C  CA  . GLY A 1 13  ? -28.545 0.368   30.318  1.00 25.44 ? 12   GLY A CA  1 
ATOM   78   C  C   . GLY A 1 13  ? -28.251 -1.011  30.875  1.00 23.82 ? 12   GLY A C   1 
ATOM   79   O  O   . GLY A 1 13  ? -27.548 -1.126  31.863  1.00 25.43 ? 12   GLY A O   1 
ATOM   80   N  N   . PRO A 1 14  ? -28.790 -2.047  30.249  1.00 23.66 ? 13   PRO A N   1 
ATOM   81   C  CA  . PRO A 1 14  ? -28.583 -3.424  30.710  1.00 23.31 ? 13   PRO A CA  1 
ATOM   82   C  C   . PRO A 1 14  ? -27.398 -4.162  30.063  1.00 23.79 ? 13   PRO A C   1 
ATOM   83   O  O   . PRO A 1 14  ? -27.248 -5.370  30.335  1.00 25.74 ? 13   PRO A O   1 
ATOM   84   C  CB  . PRO A 1 14  ? -29.880 -4.079  30.273  1.00 22.60 ? 13   PRO A CB  1 
ATOM   85   C  CG  . PRO A 1 14  ? -30.092 -3.483  28.888  1.00 22.43 ? 13   PRO A CG  1 
ATOM   86   C  CD  . PRO A 1 14  ? -29.670 -2.007  29.065  1.00 21.74 ? 13   PRO A CD  1 
ATOM   87   N  N   . VAL A 1 15  ? -26.638 -3.512  29.191  1.00 24.24 ? 14   VAL A N   1 
ATOM   88   C  CA  . VAL A 1 15  ? -25.487 -4.173  28.524  1.00 23.82 ? 14   VAL A CA  1 
ATOM   89   C  C   . VAL A 1 15  ? -24.371 -4.514  29.521  1.00 24.23 ? 14   VAL A C   1 
ATOM   90   O  O   . VAL A 1 15  ? -23.894 -3.663  30.263  1.00 26.32 ? 14   VAL A O   1 
ATOM   91   C  CB  . VAL A 1 15  ? -24.912 -3.386  27.322  1.00 23.30 ? 14   VAL A CB  1 
ATOM   92   C  CG1 . VAL A 1 15  ? -23.714 -4.141  26.708  1.00 19.98 ? 14   VAL A CG1 1 
ATOM   93   C  CG2 . VAL A 1 15  ? -25.959 -3.147  26.276  1.00 21.67 ? 14   VAL A CG2 1 
ATOM   94   N  N   . GLN A 1 16  ? -23.970 -5.779  29.575  1.00 24.38 ? 15   GLN A N   1 
ATOM   95   C  CA  . GLN A 1 16  ? -22.866 -6.176  30.438  1.00 24.39 ? 15   GLN A CA  1 
ATOM   96   C  C   . GLN A 1 16  ? -22.096 -7.341  29.838  1.00 24.67 ? 15   GLN A C   1 
ATOM   97   O  O   . GLN A 1 16  ? -22.665 -8.223  29.170  1.00 25.97 ? 15   GLN A O   1 
ATOM   98   C  CB  . GLN A 1 16  ? -23.258 -6.445  31.905  1.00 23.81 ? 15   GLN A CB  1 
ATOM   99   C  CG  . GLN A 1 16  ? -24.460 -7.350  32.195  1.00 25.22 ? 15   GLN A CG  1 
ATOM   100  C  CD  . GLN A 1 16  ? -24.726 -7.556  33.713  1.00 27.32 ? 15   GLN A CD  1 
ATOM   101  O  OE1 . GLN A 1 16  ? -23.851 -8.018  34.461  1.00 32.40 ? 15   GLN A OE1 1 
ATOM   102  N  NE2 . GLN A 1 16  ? -25.927 -7.211  34.160  1.00 29.86 ? 15   GLN A NE2 1 
ATOM   103  N  N   . GLY A 1 17  ? -20.795 -7.330  30.071  1.00 25.60 ? 16   GLY A N   1 
ATOM   104  C  CA  . GLY A 1 17  ? -19.983 -8.366  29.492  1.00 25.99 ? 16   GLY A CA  1 
ATOM   105  C  C   . GLY A 1 17  ? -18.585 -8.438  30.029  1.00 25.22 ? 16   GLY A C   1 
ATOM   106  O  O   . GLY A 1 17  ? -18.118 -7.540  30.698  1.00 28.16 ? 16   GLY A O   1 
ATOM   107  N  N   . ILE A 1 18  ? -17.924 -9.549  29.759  1.00 25.13 ? 17   ILE A N   1 
ATOM   108  C  CA  . ILE A 1 18  ? -16.531 -9.738  30.137  1.00 23.81 ? 17   ILE A CA  1 
ATOM   109  C  C   . ILE A 1 18  ? -15.768 -10.086 28.868  1.00 23.38 ? 17   ILE A C   1 
ATOM   110  O  O   . ILE A 1 18  ? -16.142 -10.989 28.113  1.00 24.46 ? 17   ILE A O   1 
ATOM   111  C  CB  . ILE A 1 18  ? -16.369 -10.828 31.225  1.00 22.33 ? 17   ILE A CB  1 
ATOM   112  C  CG1 . ILE A 1 18  ? -17.124 -10.404 32.492  1.00 23.86 ? 17   ILE A CG1 1 
ATOM   113  C  CG2 . ILE A 1 18  ? -14.930 -10.977 31.611  1.00 21.96 ? 17   ILE A CG2 1 
ATOM   114  C  CD1 . ILE A 1 18  ? -17.287 -11.531 33.489  1.00 26.98 ? 17   ILE A CD1 1 
ATOM   115  N  N   . ILE A 1 19  ? -14.700 -9.363  28.614  1.00 23.50 ? 18   ILE A N   1 
ATOM   116  C  CA  . ILE A 1 19  ? -13.895 -9.601  27.435  1.00 23.02 ? 18   ILE A CA  1 
ATOM   117  C  C   . ILE A 1 19  ? -12.461 -9.886  27.884  1.00 23.67 ? 18   ILE A C   1 
ATOM   118  O  O   . ILE A 1 19  ? -11.893 -9.159  28.708  1.00 25.41 ? 18   ILE A O   1 
ATOM   119  C  CB  . ILE A 1 19  ? -13.959 -8.392  26.430  1.00 21.70 ? 18   ILE A CB  1 
ATOM   120  C  CG1 . ILE A 1 19  ? -15.375 -8.112  25.887  1.00 20.45 ? 18   ILE A CG1 1 
ATOM   121  C  CG2 . ILE A 1 19  ? -13.037 -8.627  25.298  1.00 19.51 ? 18   ILE A CG2 1 
ATOM   122  C  CD1 . ILE A 1 19  ? -16.078 -9.257  25.080  1.00 23.23 ? 18   ILE A CD1 1 
ATOM   123  N  N   . ASN A 1 20  ? -11.891 -10.967 27.364  1.00 24.19 ? 19   ASN A N   1 
ATOM   124  C  CA  . ASN A 1 20  ? -10.547 -11.369 27.715  1.00 24.62 ? 19   ASN A CA  1 
ATOM   125  C  C   . ASN A 1 20  ? -9.581  -11.039 26.585  1.00 25.17 ? 19   ASN A C   1 
ATOM   126  O  O   . ASN A 1 20  ? -9.943  -11.038 25.403  1.00 27.11 ? 19   ASN A O   1 
ATOM   127  C  CB  . ASN A 1 20  ? -10.499 -12.881 28.037  1.00 23.11 ? 19   ASN A CB  1 
ATOM   128  C  CG  . ASN A 1 20  ? -11.474 -13.280 29.145  1.00 23.49 ? 19   ASN A CG  1 
ATOM   129  O  OD1 . ASN A 1 20  ? -12.532 -13.867 28.873  1.00 26.59 ? 19   ASN A OD1 1 
ATOM   130  N  ND2 . ASN A 1 20  ? -11.153 -12.927 30.397  1.00 24.78 ? 19   ASN A ND2 1 
ATOM   131  N  N   . PHE A 1 21  ? -8.356  -10.723 26.941  1.00 26.36 ? 20   PHE A N   1 
ATOM   132  C  CA  . PHE A 1 21  ? -7.338  -10.452 25.936  1.00 25.32 ? 20   PHE A CA  1 
ATOM   133  C  C   . PHE A 1 21  ? -6.138  -11.278 26.287  1.00 25.72 ? 20   PHE A C   1 
ATOM   134  O  O   . PHE A 1 21  ? -5.744  -11.339 27.440  1.00 26.29 ? 20   PHE A O   1 
ATOM   135  C  CB  . PHE A 1 21  ? -6.893  -8.987  25.958  1.00 25.34 ? 20   PHE A CB  1 
ATOM   136  C  CG  . PHE A 1 21  ? -7.952  -8.020  25.587  1.00 22.47 ? 20   PHE A CG  1 
ATOM   137  C  CD1 . PHE A 1 21  ? -8.853  -7.581  26.550  1.00 26.09 ? 20   PHE A CD1 1 
ATOM   138  C  CD2 . PHE A 1 21  ? -8.053  -7.532  24.295  1.00 23.52 ? 20   PHE A CD2 1 
ATOM   139  C  CE1 . PHE A 1 21  ? -9.876  -6.653  26.239  1.00 21.43 ? 20   PHE A CE1 1 
ATOM   140  C  CE2 . PHE A 1 21  ? -9.062  -6.614  23.966  1.00 20.99 ? 20   PHE A CE2 1 
ATOM   141  C  CZ  . PHE A 1 21  ? -9.988  -6.168  24.960  1.00 20.83 ? 20   PHE A CZ  1 
ATOM   142  N  N   . GLU A 1 22  ? -5.528  -11.885 25.284  1.00 26.99 ? 21   GLU A N   1 
ATOM   143  C  CA  . GLU A 1 22  ? -4.293  -12.628 25.493  1.00 28.01 ? 21   GLU A CA  1 
ATOM   144  C  C   . GLU A 1 22  ? -3.326  -12.556 24.320  1.00 27.52 ? 21   GLU A C   1 
ATOM   145  O  O   . GLU A 1 22  ? -3.708  -12.689 23.146  1.00 28.15 ? 21   GLU A O   1 
ATOM   146  C  CB  . GLU A 1 22  ? -4.558  -14.089 25.842  1.00 28.13 ? 21   GLU A CB  1 
ATOM   147  C  CG  . GLU A 1 22  ? -3.271  -14.833 26.073  1.00 31.26 ? 21   GLU A CG  1 
ATOM   148  C  CD  . GLU A 1 22  ? -3.487  -16.264 26.500  1.00 35.11 ? 21   GLU A CD  1 
ATOM   149  O  OE1 . GLU A 1 22  ? -3.640  -17.131 25.598  1.00 37.43 ? 21   GLU A OE1 1 
ATOM   150  O  OE2 . GLU A 1 22  ? -3.510  -16.503 27.731  1.00 35.74 ? 21   GLU A OE2 1 
ATOM   151  N  N   . GLN A 1 23  ? -2.060  -12.380 24.665  1.00 27.31 ? 22   GLN A N   1 
ATOM   152  C  CA  . GLN A 1 23  ? -0.983  -12.268 23.704  1.00 27.06 ? 22   GLN A CA  1 
ATOM   153  C  C   . GLN A 1 23  ? 0.214   -13.019 24.231  1.00 27.64 ? 22   GLN A C   1 
ATOM   154  O  O   . GLN A 1 23  ? 0.779   -12.675 25.272  1.00 28.22 ? 22   GLN A O   1 
ATOM   155  C  CB  . GLN A 1 23  ? -0.632  -10.802 23.517  1.00 26.54 ? 22   GLN A CB  1 
ATOM   156  C  CG  . GLN A 1 23  ? 0.372   -10.503 22.420  1.00 25.67 ? 22   GLN A CG  1 
ATOM   157  C  CD  . GLN A 1 23  ? 0.543   -9.002  22.233  1.00 23.84 ? 22   GLN A CD  1 
ATOM   158  O  OE1 . GLN A 1 23  ? 0.363   -8.253  23.181  1.00 26.64 ? 22   GLN A OE1 1 
ATOM   159  N  NE2 . GLN A 1 23  ? 0.878   -8.568  21.018  1.00 25.89 ? 22   GLN A NE2 1 
ATOM   160  N  N   . LYS A 1 24  ? 0.594   -14.058 23.508  1.00 28.58 ? 23   LYS A N   1 
ATOM   161  C  CA  . LYS A 1 24  ? 1.685   -14.916 23.912  1.00 28.97 ? 23   LYS A CA  1 
ATOM   162  C  C   . LYS A 1 24  ? 3.065   -14.277 23.682  1.00 29.65 ? 23   LYS A C   1 
ATOM   163  O  O   . LYS A 1 24  ? 3.957   -14.404 24.525  1.00 30.38 ? 23   LYS A O   1 
ATOM   164  C  CB  . LYS A 1 24  ? 1.594   -16.276 23.189  1.00 28.79 ? 23   LYS A CB  1 
ATOM   165  N  N   . GLU A 1 25  ? 3.235   -13.594 22.549  1.00 30.61 ? 24   GLU A N   1 
ATOM   166  C  CA  . GLU A 1 25  ? 4.511   -12.972 22.191  1.00 30.66 ? 24   GLU A CA  1 
ATOM   167  C  C   . GLU A 1 25  ? 4.282   -11.516 21.791  1.00 31.35 ? 24   GLU A C   1 
ATOM   168  O  O   . GLU A 1 25  ? 3.220   -11.167 21.265  1.00 31.45 ? 24   GLU A O   1 
ATOM   169  C  CB  . GLU A 1 25  ? 5.229   -13.755 21.076  1.00 30.72 ? 24   GLU A CB  1 
ATOM   170  C  CG  . GLU A 1 25  ? 5.866   -15.100 21.499  1.00 29.22 ? 24   GLU A CG  1 
ATOM   171  N  N   . SER A 1 26  ? 5.288   -10.677 22.018  1.00 31.94 ? 25   SER A N   1 
ATOM   172  C  CA  . SER A 1 26  ? 5.153   -9.237  21.802  1.00 32.83 ? 25   SER A CA  1 
ATOM   173  C  C   . SER A 1 26  ? 4.837   -8.825  20.362  1.00 32.95 ? 25   SER A C   1 
ATOM   174  O  O   . SER A 1 26  ? 4.345   -7.716  20.102  1.00 34.14 ? 25   SER A O   1 
ATOM   175  C  CB  . SER A 1 26  ? 6.409   -8.519  22.294  1.00 32.69 ? 25   SER A CB  1 
ATOM   176  O  OG  . SER A 1 26  ? 7.481   -8.663  21.377  1.00 33.78 ? 25   SER A OG  1 
ATOM   177  N  N   . ASN A 1 27  ? 5.127   -9.708  19.423  1.00 32.83 ? 26   ASN A N   1 
ATOM   178  C  CA  . ASN A 1 27  ? 4.809   -9.424  18.043  1.00 32.72 ? 26   ASN A CA  1 
ATOM   179  C  C   . ASN A 1 27  ? 3.725   -10.379 17.594  1.00 32.34 ? 26   ASN A C   1 
ATOM   180  O  O   . ASN A 1 27  ? 3.470   -10.539 16.395  1.00 33.15 ? 26   ASN A O   1 
ATOM   181  C  CB  . ASN A 1 27  ? 6.028   -9.615  17.170  1.00 32.77 ? 26   ASN A CB  1 
ATOM   182  C  CG  . ASN A 1 27  ? 6.523   -11.043 17.178  1.00 33.57 ? 26   ASN A CG  1 
ATOM   183  O  OD1 . ASN A 1 27  ? 6.649   -11.673 18.246  1.00 35.59 ? 26   ASN A OD1 1 
ATOM   184  N  ND2 . ASN A 1 27  ? 6.817   -11.570 15.991  1.00 34.54 ? 26   ASN A ND2 1 
ATOM   185  N  N   . GLY A 1 28  ? 3.098   -11.035 18.558  1.00 31.80 ? 27   GLY A N   1 
ATOM   186  C  CA  . GLY A 1 28  ? 2.064   -11.996 18.233  1.00 30.27 ? 27   GLY A CA  1 
ATOM   187  C  C   . GLY A 1 28  ? 0.736   -11.306 18.111  1.00 28.72 ? 27   GLY A C   1 
ATOM   188  O  O   . GLY A 1 28  ? 0.601   -10.108 18.385  1.00 29.30 ? 27   GLY A O   1 
ATOM   189  N  N   . PRO A 1 29  ? -0.251  -12.065 17.674  1.00 27.89 ? 28   PRO A N   1 
ATOM   190  C  CA  . PRO A 1 29  ? -1.616  -11.573 17.622  1.00 26.23 ? 28   PRO A CA  1 
ATOM   191  C  C   . PRO A 1 29  ? -2.247  -11.691 19.014  1.00 25.35 ? 28   PRO A C   1 
ATOM   192  O  O   . PRO A 1 29  ? -1.782  -12.449 19.879  1.00 26.04 ? 28   PRO A O   1 
ATOM   193  C  CB  . PRO A 1 29  ? -2.289  -12.528 16.634  1.00 26.24 ? 28   PRO A CB  1 
ATOM   194  C  CG  . PRO A 1 29  ? -1.589  -13.814 16.841  1.00 27.12 ? 28   PRO A CG  1 
ATOM   195  C  CD  . PRO A 1 29  ? -0.134  -13.461 17.200  1.00 27.49 ? 28   PRO A CD  1 
ATOM   196  N  N   . VAL A 1 30  ? -3.295  -10.913 19.219  1.00 24.88 ? 29   VAL A N   1 
ATOM   197  C  CA  . VAL A 1 30  ? -4.012  -10.887 20.474  1.00 24.07 ? 29   VAL A CA  1 
ATOM   198  C  C   . VAL A 1 30  ? -5.316  -11.637 20.325  1.00 24.15 ? 29   VAL A C   1 
ATOM   199  O  O   . VAL A 1 30  ? -6.143  -11.315 19.472  1.00 26.63 ? 29   VAL A O   1 
ATOM   200  C  CB  . VAL A 1 30  ? -4.328  -9.435  20.892  1.00 22.57 ? 29   VAL A CB  1 
ATOM   201  C  CG1 . VAL A 1 30  ? -4.991  -9.404  22.258  1.00 21.22 ? 29   VAL A CG1 1 
ATOM   202  C  CG2 . VAL A 1 30  ? -3.053  -8.599  20.900  1.00 22.52 ? 29   VAL A CG2 1 
ATOM   203  N  N   . LYS A 1 31  ? -5.512  -12.665 21.135  1.00 25.52 ? 30   LYS A N   1 
ATOM   204  C  CA  . LYS A 1 31  ? -6.811  -13.344 21.152  1.00 25.02 ? 30   LYS A CA  1 
ATOM   205  C  C   . LYS A 1 31  ? -7.723  -12.489 22.036  1.00 24.80 ? 30   LYS A C   1 
ATOM   206  O  O   . LYS A 1 31  ? -7.331  -12.091 23.137  1.00 27.57 ? 30   LYS A O   1 
ATOM   207  C  CB  . LYS A 1 31  ? -6.701  -14.701 21.853  1.00 24.17 ? 30   LYS A CB  1 
ATOM   208  N  N   . VAL A 1 32  ? -8.915  -12.169 21.557  1.00 24.87 ? 31   VAL A N   1 
ATOM   209  C  CA  . VAL A 1 32  ? -9.904  -11.558 22.417  1.00 23.85 ? 31   VAL A CA  1 
ATOM   210  C  C   . VAL A 1 32  ? -11.210 -12.293 22.373  1.00 24.20 ? 31   VAL A C   1 
ATOM   211  O  O   . VAL A 1 32  ? -11.719 -12.648 21.309  1.00 25.98 ? 31   VAL A O   1 
ATOM   212  C  CB  . VAL A 1 32  ? -10.000 -10.021 22.258  1.00 23.14 ? 31   VAL A CB  1 
ATOM   213  C  CG1 . VAL A 1 32  ? -9.137  -9.574  21.083  1.00 24.53 ? 31   VAL A CG1 1 
ATOM   214  C  CG2 . VAL A 1 32  ? -11.443 -9.506  22.234  1.00 21.37 ? 31   VAL A CG2 1 
ATOM   215  N  N   . TRP A 1 33  ? -11.763 -12.516 23.557  1.00 24.79 ? 32   TRP A N   1 
ATOM   216  C  CA  . TRP A 1 33  ? -12.909 -13.383 23.673  1.00 24.04 ? 32   TRP A CA  1 
ATOM   217  C  C   . TRP A 1 33  ? -13.683 -13.194 24.967  1.00 23.71 ? 32   TRP A C   1 
ATOM   218  O  O   . TRP A 1 33  ? -13.148 -12.734 25.977  1.00 24.60 ? 32   TRP A O   1 
ATOM   219  C  CB  . TRP A 1 33  ? -12.430 -14.848 23.573  1.00 23.55 ? 32   TRP A CB  1 
ATOM   220  C  CG  . TRP A 1 33  ? -11.840 -15.424 24.825  1.00 23.70 ? 32   TRP A CG  1 
ATOM   221  C  CD1 . TRP A 1 33  ? -12.464 -16.251 25.711  1.00 22.85 ? 32   TRP A CD1 1 
ATOM   222  C  CD2 . TRP A 1 33  ? -10.507 -15.265 25.301  1.00 21.56 ? 32   TRP A CD2 1 
ATOM   223  N  NE1 . TRP A 1 33  ? -11.608 -16.596 26.722  1.00 24.61 ? 32   TRP A NE1 1 
ATOM   224  C  CE2 . TRP A 1 33  ? -10.398 -15.997 26.496  1.00 22.20 ? 32   TRP A CE2 1 
ATOM   225  C  CE3 . TRP A 1 33  ? -9.387  -14.547 24.850  1.00 20.95 ? 32   TRP A CE3 1 
ATOM   226  C  CZ2 . TRP A 1 33  ? -9.232  -16.055 27.233  1.00 20.42 ? 32   TRP A CZ2 1 
ATOM   227  C  CZ3 . TRP A 1 33  ? -8.233  -14.601 25.592  1.00 17.59 ? 32   TRP A CZ3 1 
ATOM   228  C  CH2 . TRP A 1 33  ? -8.163  -15.349 26.770  1.00 21.50 ? 32   TRP A CH2 1 
ATOM   229  N  N   . GLY A 1 34  ? -14.953 -13.577 24.924  1.00 24.25 ? 33   GLY A N   1 
ATOM   230  C  CA  . GLY A 1 34  ? -15.809 -13.508 26.086  1.00 23.73 ? 33   GLY A CA  1 
ATOM   231  C  C   . GLY A 1 34  ? -17.220 -13.405 25.597  1.00 23.59 ? 33   GLY A C   1 
ATOM   232  O  O   . GLY A 1 34  ? -17.533 -13.874 24.516  1.00 25.18 ? 33   GLY A O   1 
ATOM   233  N  N   . SER A 1 35  ? -18.074 -12.785 26.397  1.00 24.93 ? 34   SER A N   1 
ATOM   234  C  CA  . SER A 1 35  ? -19.468 -12.635 26.050  1.00 25.22 ? 34   SER A CA  1 
ATOM   235  C  C   . SER A 1 35  ? -20.054 -11.301 26.515  1.00 25.06 ? 34   SER A C   1 
ATOM   236  O  O   . SER A 1 35  ? -19.607 -10.711 27.507  1.00 26.35 ? 34   SER A O   1 
ATOM   237  C  CB  . SER A 1 35  ? -20.280 -13.788 26.631  1.00 25.59 ? 34   SER A CB  1 
ATOM   238  O  OG  . SER A 1 35  ? -21.635 -13.757 26.186  1.00 29.94 ? 34   SER A OG  1 
ATOM   239  N  N   . ILE A 1 36  ? -21.058 -10.837 25.788  1.00 24.85 ? 35   ILE A N   1 
ATOM   240  C  CA  . ILE A 1 36  ? -21.775 -9.634  26.164  1.00 23.53 ? 35   ILE A CA  1 
ATOM   241  C  C   . ILE A 1 36  ? -23.310 -9.911  26.057  1.00 23.62 ? 35   ILE A C   1 
ATOM   242  O  O   . ILE A 1 36  ? -23.776 -10.416 25.036  1.00 25.03 ? 35   ILE A O   1 
ATOM   243  C  CB  . ILE A 1 36  ? -21.377 -8.496  25.227  1.00 22.39 ? 35   ILE A CB  1 
ATOM   244  C  CG1 . ILE A 1 36  ? -19.842 -8.379  25.067  1.00 22.38 ? 35   ILE A CG1 1 
ATOM   245  C  CG2 . ILE A 1 36  ? -22.115 -7.219  25.662  1.00 20.85 ? 35   ILE A CG2 1 
ATOM   246  C  CD1 . ILE A 1 36  ? -19.325 -7.208  24.162  1.00 22.17 ? 35   ILE A CD1 1 
ATOM   247  N  N   . LYS A 1 37  ? -24.081 -9.578  27.099  1.00 24.41 ? 36   LYS A N   1 
ATOM   248  C  CA  . LYS A 1 37  ? -25.536 -9.735  27.109  1.00 24.09 ? 36   LYS A CA  1 
ATOM   249  C  C   . LYS A 1 37  ? -26.230 -8.378  27.180  1.00 24.35 ? 36   LYS A C   1 
ATOM   250  O  O   . LYS A 1 37  ? -25.562 -7.350  27.325  1.00 25.00 ? 36   LYS A O   1 
ATOM   251  C  CB  . LYS A 1 37  ? -26.021 -10.698 28.205  1.00 23.77 ? 36   LYS A CB  1 
ATOM   252  C  CG  . LYS A 1 37  ? -25.714 -10.286 29.650  1.00 24.82 ? 36   LYS A CG  1 
ATOM   253  C  CD  . LYS A 1 37  ? -26.128 -11.392 30.632  1.00 22.40 ? 36   LYS A CD  1 
ATOM   254  C  CE  . LYS A 1 37  ? -25.770 -11.057 32.080  1.00 25.58 ? 36   LYS A CE  1 
ATOM   255  N  NZ  . LYS A 1 37  ? -26.106 -12.187 33.018  1.00 28.41 ? 36   LYS A NZ  1 
ATOM   256  N  N   . GLY A 1 38  ? -27.557 -8.373  27.044  1.00 25.12 ? 37   GLY A N   1 
ATOM   257  C  CA  . GLY A 1 38  ? -28.347 -7.139  27.037  1.00 25.54 ? 37   GLY A CA  1 
ATOM   258  C  C   . GLY A 1 38  ? -28.313 -6.280  25.767  1.00 24.99 ? 37   GLY A C   1 
ATOM   259  O  O   . GLY A 1 38  ? -28.640 -5.089  25.809  1.00 26.82 ? 37   GLY A O   1 
ATOM   260  N  N   . LEU A 1 39  ? -27.900 -6.871  24.652  1.00 24.99 ? 38   LEU A N   1 
ATOM   261  C  CA  . LEU A 1 39  ? -27.786 -6.200  23.355  1.00 24.51 ? 38   LEU A CA  1 
ATOM   262  C  C   . LEU A 1 39  ? -28.960 -6.454  22.421  1.00 25.56 ? 38   LEU A C   1 
ATOM   263  O  O   . LEU A 1 39  ? -29.575 -7.551  22.435  1.00 25.41 ? 38   LEU A O   1 
ATOM   264  C  CB  . LEU A 1 39  ? -26.566 -6.746  22.612  1.00 24.27 ? 38   LEU A CB  1 
ATOM   265  C  CG  . LEU A 1 39  ? -25.172 -6.134  22.537  1.00 24.24 ? 38   LEU A CG  1 
ATOM   266  C  CD1 . LEU A 1 39  ? -25.024 -4.866  23.301  1.00 26.40 ? 38   LEU A CD1 1 
ATOM   267  C  CD2 . LEU A 1 39  ? -24.187 -7.204  22.980  1.00 26.64 ? 38   LEU A CD2 1 
ATOM   268  N  N   . THR A 1 40  ? -29.278 -5.475  21.572  1.00 26.23 ? 39   THR A N   1 
ATOM   269  C  CA  . THR A 1 40  ? -30.276 -5.778  20.552  1.00 26.63 ? 39   THR A CA  1 
ATOM   270  C  C   . THR A 1 40  ? -29.662 -6.735  19.572  1.00 26.50 ? 39   THR A C   1 
ATOM   271  O  O   . THR A 1 40  ? -28.462 -6.622  19.241  1.00 27.32 ? 39   THR A O   1 
ATOM   272  C  CB  . THR A 1 40  ? -30.795 -4.562  19.759  1.00 26.29 ? 39   THR A CB  1 
ATOM   273  O  OG1 . THR A 1 40  ? -29.706 -3.924  19.083  1.00 28.19 ? 39   THR A OG1 1 
ATOM   274  C  CG2 . THR A 1 40  ? -31.367 -3.526  20.675  1.00 27.09 ? 39   THR A CG2 1 
ATOM   275  N  N   . GLU A 1 41  ? -30.493 -7.672  19.119  1.00 25.92 ? 40   GLU A N   1 
ATOM   276  C  CA  . GLU A 1 41  ? -30.121 -8.668  18.120  1.00 25.94 ? 40   GLU A CA  1 
ATOM   277  C  C   . GLU A 1 41  ? -29.483 -7.947  16.952  1.00 25.68 ? 40   GLU A C   1 
ATOM   278  O  O   . GLU A 1 41  ? -29.927 -6.859  16.552  1.00 26.43 ? 40   GLU A O   1 
ATOM   279  C  CB  . GLU A 1 41  ? -31.344 -9.489  17.653  1.00 25.83 ? 40   GLU A CB  1 
ATOM   280  C  CG  . GLU A 1 41  ? -31.011 -10.801 16.929  1.00 26.92 ? 40   GLU A CG  1 
ATOM   281  C  CD  . GLU A 1 41  ? -32.232 -11.519 16.326  1.00 27.24 ? 40   GLU A CD  1 
ATOM   282  O  OE1 . GLU A 1 41  ? -33.392 -11.281 16.740  1.00 28.50 ? 40   GLU A OE1 1 
ATOM   283  O  OE2 . GLU A 1 41  ? -32.041 -12.326 15.395  1.00 29.28 ? 40   GLU A OE2 1 
ATOM   284  N  N   . GLY A 1 42  ? -28.408 -8.528  16.440  1.00 25.08 ? 41   GLY A N   1 
ATOM   285  C  CA  . GLY A 1 42  ? -27.707 -7.910  15.330  1.00 24.95 ? 41   GLY A CA  1 
ATOM   286  C  C   . GLY A 1 42  ? -26.311 -7.398  15.670  1.00 24.26 ? 41   GLY A C   1 
ATOM   287  O  O   . GLY A 1 42  ? -25.734 -7.713  16.739  1.00 25.07 ? 41   GLY A O   1 
ATOM   288  N  N   . LEU A 1 43  ? -25.761 -6.619  14.735  1.00 24.31 ? 42   LEU A N   1 
ATOM   289  C  CA  . LEU A 1 43  ? -24.389 -6.115  14.820  1.00 22.38 ? 42   LEU A CA  1 
ATOM   290  C  C   . LEU A 1 43  ? -24.186 -4.885  15.690  1.00 21.66 ? 42   LEU A C   1 
ATOM   291  O  O   . LEU A 1 43  ? -25.050 -3.985  15.750  1.00 22.21 ? 42   LEU A O   1 
ATOM   292  C  CB  . LEU A 1 43  ? -23.817 -5.823  13.438  1.00 22.44 ? 42   LEU A CB  1 
ATOM   293  C  CG  . LEU A 1 43  ? -23.076 -6.865  12.602  1.00 22.04 ? 42   LEU A CG  1 
ATOM   294  C  CD1 . LEU A 1 43  ? -23.548 -8.217  12.994  1.00 23.42 ? 42   LEU A CD1 1 
ATOM   295  C  CD2 . LEU A 1 43  ? -23.383 -6.606  11.147  1.00 22.89 ? 42   LEU A CD2 1 
ATOM   296  N  N   . HIS A 1 44  ? -23.033 -4.878  16.339  1.00 22.11 ? 43   HIS A N   1 
ATOM   297  C  CA  . HIS A 1 44  ? -22.587 -3.825  17.287  1.00 20.82 ? 43   HIS A CA  1 
ATOM   298  C  C   . HIS A 1 44  ? -21.099 -3.514  17.115  1.00 21.92 ? 43   HIS A C   1 
ATOM   299  O  O   . HIS A 1 44  ? -20.210 -4.379  17.200  1.00 22.47 ? 43   HIS A O   1 
ATOM   300  C  CB  . HIS A 1 44  ? -22.876 -4.228  18.740  1.00 19.03 ? 43   HIS A CB  1 
ATOM   301  C  CG  . HIS A 1 44  ? -24.323 -4.465  19.039  1.00 20.10 ? 43   HIS A CG  1 
ATOM   302  N  ND1 . HIS A 1 44  ? -25.187 -3.445  19.358  1.00 21.06 ? 43   HIS A ND1 1 
ATOM   303  C  CD2 . HIS A 1 44  ? -25.074 -5.600  19.012  1.00 12.29 ? 43   HIS A CD2 1 
ATOM   304  C  CE1 . HIS A 1 44  ? -26.395 -3.939  19.547  1.00 20.16 ? 43   HIS A CE1 1 
ATOM   305  N  NE2 . HIS A 1 44  ? -26.352 -5.245  19.338  1.00 23.91 ? 43   HIS A NE2 1 
ATOM   306  N  N   . GLY A 1 45  ? -20.804 -2.242  16.871  1.00 23.86 ? 44   GLY A N   1 
ATOM   307  C  CA  . GLY A 1 45  ? -19.434 -1.805  16.812  1.00 23.64 ? 44   GLY A CA  1 
ATOM   308  C  C   . GLY A 1 45  ? -18.733 -2.175  18.108  1.00 22.99 ? 44   GLY A C   1 
ATOM   309  O  O   . GLY A 1 45  ? -19.317 -2.111  19.225  1.00 25.56 ? 44   GLY A O   1 
ATOM   310  N  N   . PHE A 1 46  ? -17.483 -2.573  17.963  1.00 23.22 ? 45   PHE A N   1 
ATOM   311  C  CA  . PHE A 1 46  ? -16.652 -3.047  19.061  1.00 21.15 ? 45   PHE A CA  1 
ATOM   312  C  C   . PHE A 1 46  ? -15.286 -2.412  18.861  1.00 22.95 ? 45   PHE A C   1 
ATOM   313  O  O   . PHE A 1 46  ? -14.468 -2.877  18.018  1.00 23.65 ? 45   PHE A O   1 
ATOM   314  C  CB  . PHE A 1 46  ? -16.613 -4.540  18.899  1.00 22.22 ? 45   PHE A CB  1 
ATOM   315  C  CG  . PHE A 1 46  ? -16.027 -5.281  20.031  1.00 20.28 ? 45   PHE A CG  1 
ATOM   316  C  CD1 . PHE A 1 46  ? -16.597 -5.262  21.286  1.00 25.94 ? 45   PHE A CD1 1 
ATOM   317  C  CD2 . PHE A 1 46  ? -14.917 -6.110  19.798  1.00 20.43 ? 45   PHE A CD2 1 
ATOM   318  C  CE1 . PHE A 1 46  ? -16.051 -6.008  22.333  1.00 25.76 ? 45   PHE A CE1 1 
ATOM   319  C  CE2 . PHE A 1 46  ? -14.350 -6.864  20.862  1.00 21.00 ? 45   PHE A CE2 1 
ATOM   320  C  CZ  . PHE A 1 46  ? -14.911 -6.815  22.120  1.00 22.74 ? 45   PHE A CZ  1 
ATOM   321  N  N   . HIS A 1 47  ? -15.052 -1.336  19.621  1.00 23.38 ? 46   HIS A N   1 
ATOM   322  C  CA  . HIS A 1 47  ? -13.908 -0.449  19.473  1.00 22.78 ? 46   HIS A CA  1 
ATOM   323  C  C   . HIS A 1 47  ? -13.120 -0.089  20.716  1.00 21.89 ? 46   HIS A C   1 
ATOM   324  O  O   . HIS A 1 47  ? -13.681 0.185   21.817  1.00 25.55 ? 46   HIS A O   1 
ATOM   325  C  CB  . HIS A 1 47  ? -14.373 0.888   18.919  1.00 22.83 ? 46   HIS A CB  1 
ATOM   326  C  CG  . HIS A 1 47  ? -15.176 0.786   17.667  1.00 22.80 ? 46   HIS A CG  1 
ATOM   327  N  ND1 . HIS A 1 47  ? -16.106 1.734   17.320  1.00 25.25 ? 46   HIS A ND1 1 
ATOM   328  C  CD2 . HIS A 1 47  ? -15.199 -0.147  16.686  1.00 23.80 ? 46   HIS A CD2 1 
ATOM   329  C  CE1 . HIS A 1 47  ? -16.676 1.388   16.181  1.00 26.67 ? 46   HIS A CE1 1 
ATOM   330  N  NE2 . HIS A 1 47  ? -16.137 0.252   15.773  1.00 29.84 ? 46   HIS A NE2 1 
ATOM   331  N  N   . VAL A 1 48  ? -11.818 0.044   20.531  1.00 23.36 ? 47   VAL A N   1 
ATOM   332  C  CA  . VAL A 1 48  ? -10.989 0.466   21.621  1.00 22.36 ? 47   VAL A CA  1 
ATOM   333  C  C   . VAL A 1 48  ? -10.825 1.957   21.480  1.00 20.74 ? 47   VAL A C   1 
ATOM   334  O  O   . VAL A 1 48  ? -10.324 2.428   20.469  1.00 24.72 ? 47   VAL A O   1 
ATOM   335  C  CB  . VAL A 1 48  ? -9.623  -0.170  21.593  1.00 20.62 ? 47   VAL A CB  1 
ATOM   336  C  CG1 . VAL A 1 48  ? -8.865  0.214   22.871  1.00 22.21 ? 47   VAL A CG1 1 
ATOM   337  C  CG2 . VAL A 1 48  ? -9.754  -1.712  21.483  1.00 21.98 ? 47   VAL A CG2 1 
ATOM   338  N  N   . HIS A 1 49  ? -11.270 2.669   22.494  1.00 22.93 ? 48   HIS A N   1 
ATOM   339  C  CA  . HIS A 1 49  ? -11.143 4.129   22.526  1.00 21.78 ? 48   HIS A CA  1 
ATOM   340  C  C   . HIS A 1 49  ? -9.908  4.507   23.306  1.00 21.10 ? 48   HIS A C   1 
ATOM   341  O  O   . HIS A 1 49  ? -9.397  3.730   24.134  1.00 24.32 ? 48   HIS A O   1 
ATOM   342  C  CB  . HIS A 1 49  ? -12.388 4.789   23.086  1.00 20.24 ? 48   HIS A CB  1 
ATOM   343  C  CG  . HIS A 1 49  ? -13.598 4.669   22.192  1.00 21.99 ? 48   HIS A CG  1 
ATOM   344  N  ND1 . HIS A 1 49  ? -14.263 5.760   21.675  1.00 22.72 ? 48   HIS A ND1 1 
ATOM   345  C  CD2 . HIS A 1 49  ? -14.249 3.575   21.728  1.00 21.42 ? 48   HIS A CD2 1 
ATOM   346  C  CE1 . HIS A 1 49  ? -15.291 5.343   20.950  1.00 23.86 ? 48   HIS A CE1 1 
ATOM   347  N  NE2 . HIS A 1 49  ? -15.308 4.019   20.968  1.00 22.95 ? 48   HIS A NE2 1 
ATOM   348  N  N   . GLU A 1 50  ? -9.430  5.715   23.011  1.00 23.30 ? 49   GLU A N   1 
ATOM   349  C  CA  . GLU A 1 50  ? -8.181  6.249   23.511  1.00 23.27 ? 49   GLU A CA  1 
ATOM   350  C  C   . GLU A 1 50  ? -7.963  6.297   25.023  1.00 22.05 ? 49   GLU A C   1 
ATOM   351  O  O   . GLU A 1 50  ? -6.909  5.933   25.468  1.00 22.81 ? 49   GLU A O   1 
ATOM   352  C  CB  . GLU A 1 50  ? -7.890  7.642   22.917  1.00 23.43 ? 49   GLU A CB  1 
ATOM   353  C  CG  . GLU A 1 50  ? -6.500  8.165   23.333  1.00 22.55 ? 49   GLU A CG  1 
ATOM   354  C  CD  . GLU A 1 50  ? -6.064  9.408   22.602  1.00 23.90 ? 49   GLU A CD  1 
ATOM   355  O  OE1 . GLU A 1 50  ? -6.895  10.016  21.884  1.00 27.83 ? 49   GLU A OE1 1 
ATOM   356  O  OE2 . GLU A 1 50  ? -4.875  9.754   22.722  1.00 27.36 ? 49   GLU A OE2 1 
ATOM   357  N  N   . PHE A 1 51  ? -8.910  6.806   25.788  1.00 22.81 ? 50   PHE A N   1 
ATOM   358  C  CA  . PHE A 1 51  ? -8.649  6.927   27.195  1.00 22.33 ? 50   PHE A CA  1 
ATOM   359  C  C   . PHE A 1 51  ? -9.357  5.970   28.095  1.00 22.58 ? 50   PHE A C   1 
ATOM   360  O  O   . PHE A 1 51  ? -10.532 5.656   27.897  1.00 25.24 ? 50   PHE A O   1 
ATOM   361  C  CB  . PHE A 1 51  ? -8.962  8.355   27.583  1.00 22.40 ? 50   PHE A CB  1 
ATOM   362  C  CG  . PHE A 1 51  ? -8.180  9.339   26.792  1.00 22.69 ? 50   PHE A CG  1 
ATOM   363  C  CD1 . PHE A 1 51  ? -6.817  9.471   26.983  1.00 24.30 ? 50   PHE A CD1 1 
ATOM   364  C  CD2 . PHE A 1 51  ? -8.789  10.116  25.791  1.00 26.40 ? 50   PHE A CD2 1 
ATOM   365  C  CE1 . PHE A 1 51  ? -6.071  10.399  26.217  1.00 24.35 ? 50   PHE A CE1 1 
ATOM   366  C  CE2 . PHE A 1 51  ? -8.051  11.050  25.041  1.00 24.06 ? 50   PHE A CE2 1 
ATOM   367  C  CZ  . PHE A 1 51  ? -6.696  11.179  25.234  1.00 24.04 ? 50   PHE A CZ  1 
ATOM   368  N  N   . GLY A 1 52  ? -8.636  5.482   29.106  1.00 22.88 ? 51   GLY A N   1 
ATOM   369  C  CA  . GLY A 1 52  ? -9.220  4.659   30.151  1.00 22.54 ? 51   GLY A CA  1 
ATOM   370  C  C   . GLY A 1 52  ? -9.853  5.539   31.229  1.00 22.80 ? 51   GLY A C   1 
ATOM   371  O  O   . GLY A 1 52  ? -9.551  5.403   32.399  1.00 23.59 ? 51   GLY A O   1 
ATOM   372  N  N   . ASP A 1 53  ? -10.646 6.527   30.800  1.00 24.16 ? 52   ASP A N   1 
ATOM   373  C  CA  . ASP A 1 53  ? -11.271 7.523   31.688  1.00 22.96 ? 52   ASP A CA  1 
ATOM   374  C  C   . ASP A 1 53  ? -12.804 7.412   31.704  1.00 21.37 ? 52   ASP A C   1 
ATOM   375  O  O   . ASP A 1 53  ? -13.507 7.818   30.770  1.00 22.24 ? 52   ASP A O   1 
ATOM   376  C  CB  . ASP A 1 53  ? -10.898 8.914   31.175  1.00 22.56 ? 52   ASP A CB  1 
ATOM   377  C  CG  . ASP A 1 53  ? -11.488 10.040  32.006  1.00 23.41 ? 52   ASP A CG  1 
ATOM   378  O  OD1 . ASP A 1 53  ? -12.523 9.837   32.673  1.00 26.61 ? 52   ASP A OD1 1 
ATOM   379  O  OD2 . ASP A 1 53  ? -10.966 11.197  32.064  1.00 26.94 ? 52   ASP A OD2 1 
ATOM   380  N  N   . ASN A 1 54  ? -13.341 6.872   32.779  1.00 22.60 ? 53   ASN A N   1 
ATOM   381  C  CA  . ASN A 1 54  ? -14.784 6.696   32.905  1.00 23.05 ? 53   ASN A CA  1 
ATOM   382  C  C   . ASN A 1 54  ? -15.443 7.771   33.759  1.00 22.61 ? 53   ASN A C   1 
ATOM   383  O  O   . ASN A 1 54  ? -16.552 7.594   34.232  1.00 24.21 ? 53   ASN A O   1 
ATOM   384  C  CB  . ASN A 1 54  ? -15.087 5.307   33.472  1.00 22.30 ? 53   ASN A CB  1 
ATOM   385  C  CG  . ASN A 1 54  ? -16.583 4.869   33.282  1.00 25.23 ? 53   ASN A CG  1 
ATOM   386  O  OD1 . ASN A 1 54  ? -17.101 4.819   32.164  1.00 31.35 ? 53   ASN A OD1 1 
ATOM   387  N  ND2 . ASN A 1 54  ? -17.247 4.507   34.382  1.00 30.84 ? 53   ASN A ND2 1 
ATOM   388  N  N   . THR A 1 55  ? -14.762 8.892   33.964  1.00 24.36 ? 54   THR A N   1 
ATOM   389  C  CA  . THR A 1 55  ? -15.297 9.888   34.895  1.00 24.57 ? 54   THR A CA  1 
ATOM   390  C  C   . THR A 1 55  ? -16.715 10.390  34.553  1.00 25.00 ? 54   THR A C   1 
ATOM   391  O  O   . THR A 1 55  ? -17.488 10.685  35.458  1.00 26.20 ? 54   THR A O   1 
ATOM   392  C  CB  . THR A 1 55  ? -14.330 11.090  35.134  1.00 23.96 ? 54   THR A CB  1 
ATOM   393  O  OG1 . THR A 1 55  ? -13.876 11.584  33.884  1.00 26.68 ? 54   THR A OG1 1 
ATOM   394  C  CG2 . THR A 1 55  ? -13.022 10.679  35.869  1.00 23.71 ? 54   THR A CG2 1 
ATOM   395  N  N   . ALA A 1 56  ? -17.068 10.471  33.274  1.00 26.55 ? 55   ALA A N   1 
ATOM   396  C  CA  . ALA A 1 56  ? -18.413 10.892  32.887  1.00 26.58 ? 55   ALA A CA  1 
ATOM   397  C  C   . ALA A 1 56  ? -19.100 9.778   32.133  1.00 26.49 ? 55   ALA A C   1 
ATOM   398  O  O   . ALA A 1 56  ? -19.894 10.018  31.236  1.00 27.96 ? 55   ALA A O   1 
ATOM   399  C  CB  . ALA A 1 56  ? -18.362 12.128  32.036  1.00 26.65 ? 55   ALA A CB  1 
ATOM   400  N  N   . GLY A 1 57  ? -18.806 8.541   32.507  1.00 26.63 ? 56   GLY A N   1 
ATOM   401  C  CA  . GLY A 1 57  ? -19.304 7.429   31.731  1.00 26.04 ? 56   GLY A CA  1 
ATOM   402  C  C   . GLY A 1 57  ? -18.395 7.195   30.514  1.00 26.37 ? 56   GLY A C   1 
ATOM   403  O  O   . GLY A 1 57  ? -17.262 7.758   30.435  1.00 27.33 ? 56   GLY A O   1 
ATOM   404  N  N   . CYS A 1 58  ? -18.903 6.398   29.569  1.00 25.26 ? 57   CYS A N   1 
ATOM   405  C  CA  . CYS A 1 58  ? -18.257 6.045   28.310  1.00 25.04 ? 57   CYS A CA  1 
ATOM   406  C  C   . CYS A 1 58  ? -17.854 7.254   27.442  1.00 24.39 ? 57   CYS A C   1 
ATOM   407  O  O   . CYS A 1 58  ? -16.850 7.202   26.741  1.00 25.55 ? 57   CYS A O   1 
ATOM   408  C  CB  . CYS A 1 58  ? -19.135 5.043   27.565  1.00 23.85 ? 57   CYS A CB  1 
ATOM   409  S  SG  . CYS A 1 58  ? -19.440 3.545   28.595  1.00 27.24 ? 57   CYS A SG  1 
ATOM   410  N  N   . THR A 1 59  ? -18.586 8.364   27.559  1.00 25.15 ? 58   THR A N   1 
ATOM   411  C  CA  . THR A 1 59  ? -18.149 9.544   26.843  1.00 25.16 ? 58   THR A CA  1 
ATOM   412  C  C   . THR A 1 59  ? -16.698 9.928   27.164  1.00 23.78 ? 58   THR A C   1 
ATOM   413  O  O   . THR A 1 59  ? -15.927 10.221  26.273  1.00 25.82 ? 58   THR A O   1 
ATOM   414  C  CB  . THR A 1 59  ? -19.049 10.732  27.164  1.00 24.59 ? 58   THR A CB  1 
ATOM   415  O  OG1 . THR A 1 59  ? -20.360 10.465  26.679  1.00 29.94 ? 58   THR A OG1 1 
ATOM   416  C  CG2 . THR A 1 59  ? -18.624 11.898  26.357  1.00 24.55 ? 58   THR A CG2 1 
ATOM   417  N  N   . SER A 1 60  ? -16.318 9.968   28.425  1.00 24.84 ? 59   SER A N   1 
ATOM   418  C  CA  . SER A 1 60  ? -14.956 10.340  28.716  1.00 24.14 ? 59   SER A CA  1 
ATOM   419  C  C   . SER A 1 60  ? -13.835 9.434   28.158  1.00 23.61 ? 59   SER A C   1 
ATOM   420  O  O   . SER A 1 60  ? -12.678 9.716   28.342  1.00 25.57 ? 59   SER A O   1 
ATOM   421  C  CB  . SER A 1 60  ? -14.766 10.694  30.205  1.00 23.36 ? 59   SER A CB  1 
ATOM   422  O  OG  . SER A 1 60  ? -15.550 9.932   31.080  1.00 27.46 ? 59   SER A OG  1 
ATOM   423  N  N   . ALA A 1 61  ? -14.159 8.349   27.482  1.00 23.70 ? 60   ALA A N   1 
ATOM   424  C  CA  . ALA A 1 61  ? -13.101 7.541   26.953  1.00 22.78 ? 60   ALA A CA  1 
ATOM   425  C  C   . ALA A 1 61  ? -12.515 8.198   25.710  1.00 22.46 ? 60   ALA A C   1 
ATOM   426  O  O   . ALA A 1 61  ? -11.434 7.839   25.241  1.00 23.84 ? 60   ALA A O   1 
ATOM   427  C  CB  . ALA A 1 61  ? -13.625 6.189   26.628  1.00 20.96 ? 60   ALA A CB  1 
ATOM   428  N  N   . GLY A 1 62  ? -13.260 9.161   25.176  1.00 23.61 ? 61   GLY A N   1 
ATOM   429  C  CA  . GLY A 1 62  ? -12.910 9.875   23.979  1.00 24.87 ? 61   GLY A CA  1 
ATOM   430  C  C   . GLY A 1 62  ? -13.023 9.131   22.674  1.00 23.61 ? 61   GLY A C   1 
ATOM   431  O  O   . GLY A 1 62  ? -13.799 8.169   22.521  1.00 26.82 ? 61   GLY A O   1 
ATOM   432  N  N   . PRO A 1 63  ? -12.173 9.531   21.751  1.00 24.10 ? 62   PRO A N   1 
ATOM   433  C  CA  . PRO A 1 63  ? -12.201 9.052   20.377  1.00 22.91 ? 62   PRO A CA  1 
ATOM   434  C  C   . PRO A 1 63  ? -11.627 7.650   20.263  1.00 22.31 ? 62   PRO A C   1 
ATOM   435  O  O   . PRO A 1 63  ? -11.196 7.087   21.259  1.00 23.53 ? 62   PRO A O   1 
ATOM   436  C  CB  . PRO A 1 63  ? -11.299 10.036  19.690  1.00 23.56 ? 62   PRO A CB  1 
ATOM   437  C  CG  . PRO A 1 63  ? -10.273 10.304  20.700  1.00 22.39 ? 62   PRO A CG  1 
ATOM   438  C  CD  . PRO A 1 63  ? -11.068 10.491  21.958  1.00 24.17 ? 62   PRO A CD  1 
ATOM   439  N  N   . HIS A 1 64  ? -11.580 7.152   19.053  1.00 24.47 ? 63   HIS A N   1 
ATOM   440  C  CA  . HIS A 1 64  ? -11.033 5.815   18.801  1.00 22.93 ? 63   HIS A CA  1 
ATOM   441  C  C   . HIS A 1 64  ? -9.539  5.865   19.097  1.00 22.25 ? 63   HIS A C   1 
ATOM   442  O  O   . HIS A 1 64  ? -8.891  6.887   18.894  1.00 23.00 ? 63   HIS A O   1 
ATOM   443  C  CB  . HIS A 1 64  ? -11.284 5.385   17.339  1.00 21.64 ? 63   HIS A CB  1 
ATOM   444  C  CG  . HIS A 1 64  ? -12.711 5.013   17.032  1.00 22.05 ? 63   HIS A CG  1 
ATOM   445  N  ND1 . HIS A 1 64  ? -13.114 4.609   15.788  1.00 27.88 ? 63   HIS A ND1 1 
ATOM   446  C  CD2 . HIS A 1 64  ? -13.816 4.938   17.823  1.00 22.80 ? 63   HIS A CD2 1 
ATOM   447  C  CE1 . HIS A 1 64  ? -14.411 4.355   15.799  1.00 26.37 ? 63   HIS A CE1 1 
ATOM   448  N  NE2 . HIS A 1 64  ? -14.862 4.540   17.025  1.00 26.34 ? 63   HIS A NE2 1 
ATOM   449  N  N   . PHE A 1 65  ? -8.981  4.794   19.639  1.00 22.80 ? 64   PHE A N   1 
ATOM   450  C  CA  . PHE A 1 65  ? -7.527  4.732   19.731  1.00 22.35 ? 64   PHE A CA  1 
ATOM   451  C  C   . PHE A 1 65  ? -6.874  4.781   18.306  1.00 22.37 ? 64   PHE A C   1 
ATOM   452  O  O   . PHE A 1 65  ? -6.843  3.810   17.548  1.00 26.32 ? 64   PHE A O   1 
ATOM   453  C  CB  . PHE A 1 65  ? -7.082  3.543   20.630  1.00 20.28 ? 64   PHE A CB  1 
ATOM   454  C  CG  . PHE A 1 65  ? -5.573  3.441   20.829  1.00 13.87 ? 64   PHE A CG  1 
ATOM   455  C  CD1 . PHE A 1 65  ? -4.790  4.562   21.118  1.00 12.31 ? 64   PHE A CD1 1 
ATOM   456  C  CD2 . PHE A 1 65  ? -4.941  2.208   20.813  1.00 15.76 ? 64   PHE A CD2 1 
ATOM   457  C  CE1 . PHE A 1 65  ? -3.471  4.491   21.308  1.00 13.04 ? 64   PHE A CE1 1 
ATOM   458  C  CE2 . PHE A 1 65  ? -3.569  2.110   21.030  1.00 13.28 ? 64   PHE A CE2 1 
ATOM   459  C  CZ  . PHE A 1 65  ? -2.808  3.249   21.287  1.00 17.72 ? 64   PHE A CZ  1 
ATOM   460  N  N   . ASN A 1 66  ? -6.339  5.921   17.912  1.00 22.25 ? 65   ASN A N   1 
ATOM   461  C  CA  . ASN A 1 66  ? -5.832  6.046   16.533  1.00 22.48 ? 65   ASN A CA  1 
ATOM   462  C  C   . ASN A 1 66  ? -4.505  6.782   16.503  1.00 22.67 ? 65   ASN A C   1 
ATOM   463  O  O   . ASN A 1 66  ? -4.423  7.916   16.021  1.00 24.14 ? 65   ASN A O   1 
ATOM   464  C  CB  . ASN A 1 66  ? -6.923  6.717   15.647  1.00 22.28 ? 65   ASN A CB  1 
ATOM   465  C  CG  . ASN A 1 66  ? -6.589  6.759   14.144  1.00 22.19 ? 65   ASN A CG  1 
ATOM   466  O  OD1 . ASN A 1 66  ? -5.849  5.930   13.579  1.00 27.60 ? 65   ASN A OD1 1 
ATOM   467  N  ND2 . ASN A 1 66  ? -7.143  7.757   13.491  1.00 26.07 ? 65   ASN A ND2 1 
ATOM   468  N  N   . PRO A 1 67  ? -3.453  6.161   17.040  1.00 24.27 ? 66   PRO A N   1 
ATOM   469  C  CA  . PRO A 1 67  ? -2.136  6.810   17.125  1.00 24.12 ? 66   PRO A CA  1 
ATOM   470  C  C   . PRO A 1 67  ? -1.446  6.976   15.780  1.00 24.54 ? 66   PRO A C   1 
ATOM   471  O  O   . PRO A 1 67  ? -0.548  7.786   15.715  1.00 25.91 ? 66   PRO A O   1 
ATOM   472  C  CB  . PRO A 1 67  ? -1.343  5.859   18.007  1.00 24.96 ? 66   PRO A CB  1 
ATOM   473  C  CG  . PRO A 1 67  ? -1.962  4.562   17.697  1.00 23.14 ? 66   PRO A CG  1 
ATOM   474  C  CD  . PRO A 1 67  ? -3.435  4.816   17.652  1.00 21.93 ? 66   PRO A CD  1 
ATOM   475  N  N   . LEU A 1 68  ? -1.857  6.244   14.744  1.00 24.67 ? 67   LEU A N   1 
ATOM   476  C  CA  . LEU A 1 68  ? -1.318  6.428   13.406  1.00 24.49 ? 67   LEU A CA  1 
ATOM   477  C  C   . LEU A 1 68  ? -2.154  7.378   12.532  1.00 25.03 ? 67   LEU A C   1 
ATOM   478  O  O   . LEU A 1 68  ? -1.890  7.491   11.335  1.00 25.63 ? 67   LEU A O   1 
ATOM   479  C  CB  . LEU A 1 68  ? -1.178  5.090   12.666  1.00 23.59 ? 67   LEU A CB  1 
ATOM   480  C  CG  . LEU A 1 68  ? -0.215  4.059   13.228  1.00 24.36 ? 67   LEU A CG  1 
ATOM   481  C  CD1 . LEU A 1 68  ? -0.112  2.882   12.259  1.00 23.30 ? 67   LEU A CD1 1 
ATOM   482  C  CD2 . LEU A 1 68  ? 1.134   4.719   13.426  1.00 25.74 ? 67   LEU A CD2 1 
ATOM   483  N  N   . SER A 1 69  ? -3.142  8.046   13.135  1.00 25.88 ? 68   SER A N   1 
ATOM   484  C  CA  . SER A 1 69  ? -4.021  8.981   12.432  1.00 26.43 ? 68   SER A CA  1 
ATOM   485  C  C   . SER A 1 69  ? -4.546  8.477   11.091  1.00 26.29 ? 68   SER A C   1 
ATOM   486  O  O   . SER A 1 69  ? -4.432  9.167   10.085  1.00 28.06 ? 68   SER A O   1 
ATOM   487  C  CB  . SER A 1 69  ? -3.304  10.328  12.195  1.00 25.88 ? 68   SER A CB  1 
ATOM   488  O  OG  . SER A 1 69  ? -2.915  10.897  13.437  1.00 29.38 ? 68   SER A OG  1 
ATOM   489  N  N   . ARG A 1 70  ? -5.062  7.260   11.047  1.00 26.31 ? 69   ARG A N   1 
ATOM   490  C  CA  . ARG A 1 70  ? -5.608  6.763   9.817   1.00 26.38 ? 69   ARG A CA  1 
ATOM   491  C  C   . ARG A 1 70  ? -7.118  6.896   9.785   1.00 25.65 ? 69   ARG A C   1 
ATOM   492  O  O   . ARG A 1 70  ? -7.734  7.398   10.721  1.00 25.09 ? 69   ARG A O   1 
ATOM   493  C  CB  . ARG A 1 70  ? -5.150  5.336   9.591   1.00 26.94 ? 69   ARG A CB  1 
ATOM   494  C  CG  . ARG A 1 70  ? -3.701  5.310   9.136   1.00 29.61 ? 69   ARG A CG  1 
ATOM   495  C  CD  . ARG A 1 70  ? -2.911  4.170   9.724   1.00 32.95 ? 69   ARG A CD  1 
ATOM   496  N  NE  . ARG A 1 70  ? -1.662  3.967   8.994   1.00 36.41 ? 69   ARG A NE  1 
ATOM   497  C  CZ  . ARG A 1 70  ? -1.296  2.803   8.476   1.00 38.19 ? 69   ARG A CZ  1 
ATOM   498  N  NH1 . ARG A 1 70  ? -2.084  1.737   8.607   1.00 40.67 ? 69   ARG A NH1 1 
ATOM   499  N  NH2 . ARG A 1 70  ? -0.141  2.698   7.833   1.00 40.64 ? 69   ARG A NH2 1 
ATOM   500  N  N   . LYS A 1 71  ? -7.696  6.515   8.660   1.00 25.76 ? 70   LYS A N   1 
ATOM   501  C  CA  . LYS A 1 71  ? -9.125  6.536   8.526   1.00 25.44 ? 70   LYS A CA  1 
ATOM   502  C  C   . LYS A 1 71  ? -9.634  5.280   9.168   1.00 25.32 ? 70   LYS A C   1 
ATOM   503  O  O   . LYS A 1 71  ? -8.912  4.274   9.286   1.00 26.77 ? 70   LYS A O   1 
ATOM   504  C  CB  . LYS A 1 71  ? -9.533  6.565   7.065   1.00 24.65 ? 70   LYS A CB  1 
ATOM   505  C  CG  . LYS A 1 71  ? -9.604  7.967   6.479   1.00 26.58 ? 70   LYS A CG  1 
ATOM   506  C  CD  . LYS A 1 71  ? -9.807  7.875   5.006   1.00 25.23 ? 70   LYS A CD  1 
ATOM   507  N  N   . HIS A 1 72  ? -10.878 5.339   9.585   1.00 25.41 ? 71   HIS A N   1 
ATOM   508  C  CA  . HIS A 1 72  ? -11.521 4.214   10.213  1.00 25.18 ? 71   HIS A CA  1 
ATOM   509  C  C   . HIS A 1 72  ? -11.810 3.117   9.204   1.00 25.46 ? 71   HIS A C   1 
ATOM   510  O  O   . HIS A 1 72  ? -12.203 3.383   8.087   1.00 27.26 ? 71   HIS A O   1 
ATOM   511  C  CB  . HIS A 1 72  ? -12.806 4.675   10.883  1.00 23.82 ? 71   HIS A CB  1 
ATOM   512  C  CG  . HIS A 1 72  ? -13.708 3.559   11.302  1.00 24.23 ? 71   HIS A CG  1 
ATOM   513  N  ND1 . HIS A 1 72  ? -13.451 2.765   12.393  1.00 26.42 ? 71   HIS A ND1 1 
ATOM   514  C  CD2 . HIS A 1 72  ? -14.875 3.118   10.783  1.00 25.03 ? 71   HIS A CD2 1 
ATOM   515  C  CE1 . HIS A 1 72  ? -14.423 1.883   12.528  1.00 19.82 ? 71   HIS A CE1 1 
ATOM   516  N  NE2 . HIS A 1 72  ? -15.288 2.067   11.554  1.00 26.41 ? 71   HIS A NE2 1 
ATOM   517  N  N   . GLY A 1 73  ? -11.615 1.869   9.600   1.00 27.31 ? 72   GLY A N   1 
ATOM   518  C  CA  . GLY A 1 73  ? -11.936 0.760   8.711   1.00 27.54 ? 72   GLY A CA  1 
ATOM   519  C  C   . GLY A 1 73  ? -12.367 -0.428  9.557   1.00 28.08 ? 72   GLY A C   1 
ATOM   520  O  O   . GLY A 1 73  ? -12.594 -0.310  10.767  1.00 28.22 ? 72   GLY A O   1 
ATOM   521  N  N   . GLY A 1 74  ? -12.491 -1.578  8.904   1.00 28.49 ? 73   GLY A N   1 
ATOM   522  C  CA  . GLY A 1 74  ? -12.735 -2.819  9.592   1.00 27.76 ? 73   GLY A CA  1 
ATOM   523  C  C   . GLY A 1 74  ? -11.378 -3.395  9.963   1.00 27.31 ? 73   GLY A C   1 
ATOM   524  O  O   . GLY A 1 74  ? -10.351 -2.974  9.437   1.00 27.62 ? 73   GLY A O   1 
ATOM   525  N  N   . PRO A 1 75  ? -11.379 -4.378  10.846  1.00 27.28 ? 74   PRO A N   1 
ATOM   526  C  CA  . PRO A 1 75  ? -10.144 -4.989  11.344  1.00 27.69 ? 74   PRO A CA  1 
ATOM   527  C  C   . PRO A 1 75  ? -9.243  -5.550  10.235  1.00 28.32 ? 74   PRO A C   1 
ATOM   528  O  O   . PRO A 1 75  ? -8.015  -5.459  10.344  1.00 29.50 ? 74   PRO A O   1 
ATOM   529  C  CB  . PRO A 1 75  ? -10.631 -6.138  12.259  1.00 28.18 ? 74   PRO A CB  1 
ATOM   530  C  CG  . PRO A 1 75  ? -12.123 -6.021  12.355  1.00 26.35 ? 74   PRO A CG  1 
ATOM   531  C  CD  . PRO A 1 75  ? -12.603 -4.979  11.393  1.00 26.36 ? 74   PRO A CD  1 
ATOM   532  N  N   . LYS A 1 76  ? -9.836  -6.122  9.191   1.00 28.59 ? 75   LYS A N   1 
ATOM   533  C  CA  . LYS A 1 76  ? -9.065  -6.712  8.098   1.00 28.78 ? 75   LYS A CA  1 
ATOM   534  C  C   . LYS A 1 76  ? -8.465  -5.646  7.149   1.00 28.12 ? 75   LYS A C   1 
ATOM   535  O  O   . LYS A 1 76  ? -7.605  -5.938  6.340   1.00 28.97 ? 75   LYS A O   1 
ATOM   536  C  CB  . LYS A 1 76  ? -9.933  -7.700  7.304   1.00 28.96 ? 75   LYS A CB  1 
ATOM   537  C  CG  . LYS A 1 76  ? -10.429 -8.947  8.065   1.00 29.50 ? 75   LYS A CG  1 
ATOM   538  C  CD  . LYS A 1 76  ? -11.026 -9.961  7.089   1.00 32.37 ? 75   LYS A CD  1 
ATOM   539  C  CE  . LYS A 1 76  ? -11.761 -11.097 7.811   1.00 34.23 ? 75   LYS A CE  1 
ATOM   540  N  NZ  . LYS A 1 76  ? -11.513 -12.436 7.158   1.00 36.31 ? 75   LYS A NZ  1 
ATOM   541  N  N   . ASP A 1 77  ? -8.914  -4.403  7.279   1.00 28.50 ? 76   ASP A N   1 
ATOM   542  C  CA  . ASP A 1 77  ? -8.483  -3.364  6.369   1.00 27.82 ? 76   ASP A CA  1 
ATOM   543  C  C   . ASP A 1 77  ? -7.106  -2.862  6.719   1.00 27.90 ? 76   ASP A C   1 
ATOM   544  O  O   . ASP A 1 77  ? -6.777  -2.739  7.895   1.00 27.35 ? 76   ASP A O   1 
ATOM   545  C  CB  . ASP A 1 77  ? -9.473  -2.198  6.408   1.00 28.05 ? 76   ASP A CB  1 
ATOM   546  C  CG  . ASP A 1 77  ? -10.818 -2.564  5.837   1.00 28.00 ? 76   ASP A CG  1 
ATOM   547  O  OD1 . ASP A 1 77  ? -10.874 -3.426  4.944   1.00 33.10 ? 76   ASP A OD1 1 
ATOM   548  O  OD2 . ASP A 1 77  ? -11.879 -2.039  6.190   1.00 31.11 ? 76   ASP A OD2 1 
ATOM   549  N  N   . GLU A 1 78  ? -6.309  -2.575  5.695   1.00 28.18 ? 77   GLU A N   1 
ATOM   550  C  CA  . GLU A 1 78  ? -4.990  -1.994  5.901   1.00 28.72 ? 77   GLU A CA  1 
ATOM   551  C  C   . GLU A 1 78  ? -5.181  -0.633  6.514   1.00 28.71 ? 77   GLU A C   1 
ATOM   552  O  O   . GLU A 1 78  ? -4.449  -0.228  7.419   1.00 29.46 ? 77   GLU A O   1 
ATOM   553  C  CB  . GLU A 1 78  ? -4.242  -1.821  4.583   1.00 28.97 ? 77   GLU A CB  1 
ATOM   554  C  CG  . GLU A 1 78  ? -2.804  -1.353  4.782   1.00 30.96 ? 77   GLU A CG  1 
ATOM   555  C  CD  . GLU A 1 78  ? -1.976  -2.384  5.532   1.00 34.39 ? 77   GLU A CD  1 
ATOM   556  O  OE1 . GLU A 1 78  ? -1.915  -3.542  5.031   1.00 38.35 ? 77   GLU A OE1 1 
ATOM   557  O  OE2 . GLU A 1 78  ? -1.399  -2.055  6.610   1.00 35.38 ? 77   GLU A OE2 1 
ATOM   558  N  N   . GLU A 1 79  ? -6.163  0.088   5.994   1.00 28.78 ? 78   GLU A N   1 
ATOM   559  C  CA  . GLU A 1 79  ? -6.473  1.419   6.504   1.00 28.49 ? 78   GLU A CA  1 
ATOM   560  C  C   . GLU A 1 79  ? -7.513  1.301   7.612   1.00 26.99 ? 78   GLU A C   1 
ATOM   561  O  O   . GLU A 1 79  ? -8.681  1.006   7.348   1.00 28.25 ? 78   GLU A O   1 
ATOM   562  C  CB  . GLU A 1 79  ? -6.963  2.314   5.378   1.00 28.31 ? 78   GLU A CB  1 
ATOM   563  C  CG  . GLU A 1 79  ? -7.088  3.770   5.781   1.00 30.84 ? 78   GLU A CG  1 
ATOM   564  C  CD  . GLU A 1 79  ? -5.750  4.474   5.861   1.00 34.36 ? 78   GLU A CD  1 
ATOM   565  O  OE1 . GLU A 1 79  ? -4.729  3.900   5.408   1.00 36.24 ? 78   GLU A OE1 1 
ATOM   566  O  OE2 . GLU A 1 79  ? -5.729  5.621   6.372   1.00 35.82 ? 78   GLU A OE2 1 
ATOM   567  N  N   . ARG A 1 80  ? -7.072  1.493   8.851   1.00 26.07 ? 79   ARG A N   1 
ATOM   568  C  CA  . ARG A 1 80  ? -7.914  1.381   10.044  1.00 25.16 ? 79   ARG A CA  1 
ATOM   569  C  C   . ARG A 1 80  ? -7.259  1.996   11.260  1.00 24.88 ? 79   ARG A C   1 
ATOM   570  O  O   . ARG A 1 80  ? -6.029  2.223   11.310  1.00 26.54 ? 79   ARG A O   1 
ATOM   571  C  CB  . ARG A 1 80  ? -8.196  -0.080  10.402  1.00 23.74 ? 79   ARG A CB  1 
ATOM   572  C  CG  . ARG A 1 80  ? -6.927  -0.832  10.788  1.00 23.73 ? 79   ARG A CG  1 
ATOM   573  C  CD  . ARG A 1 80  ? -7.149  -2.223  11.366  1.00 22.39 ? 79   ARG A CD  1 
ATOM   574  N  NE  . ARG A 1 80  ? -7.200  -2.261  12.836  1.00 26.83 ? 79   ARG A NE  1 
ATOM   575  C  CZ  . ARG A 1 80  ? -7.159  -3.399  13.529  1.00 24.09 ? 79   ARG A CZ  1 
ATOM   576  N  NH1 . ARG A 1 80  ? -7.122  -4.562  12.891  1.00 24.17 ? 79   ARG A NH1 1 
ATOM   577  N  NH2 . ARG A 1 80  ? -7.173  -3.382  14.849  1.00 27.22 ? 79   ARG A NH2 1 
ATOM   578  N  N   . HIS A 1 81  ? -8.088  2.224   12.265  1.00 25.49 ? 80   HIS A N   1 
ATOM   579  C  CA  . HIS A 1 81  ? -7.604  2.667   13.555  1.00 25.36 ? 80   HIS A CA  1 
ATOM   580  C  C   . HIS A 1 81  ? -7.045  1.448   14.246  1.00 24.83 ? 80   HIS A C   1 
ATOM   581  O  O   . HIS A 1 81  ? -7.480  0.326   13.990  1.00 25.74 ? 80   HIS A O   1 
ATOM   582  C  CB  . HIS A 1 81  ? -8.721  3.257   14.415  1.00 24.33 ? 80   HIS A CB  1 
ATOM   583  C  CG  . HIS A 1 81  ? -9.416  4.425   13.785  1.00 24.59 ? 80   HIS A CG  1 
ATOM   584  N  ND1 . HIS A 1 81  ? -10.699 4.783   14.122  1.00 25.70 ? 80   HIS A ND1 1 
ATOM   585  C  CD2 . HIS A 1 81  ? -9.033  5.276   12.806  1.00 23.09 ? 80   HIS A CD2 1 
ATOM   586  C  CE1 . HIS A 1 81  ? -11.057 5.844   13.425  1.00 20.94 ? 80   HIS A CE1 1 
ATOM   587  N  NE2 . HIS A 1 81  ? -10.071 6.148   12.598  1.00 26.50 ? 80   HIS A NE2 1 
ATOM   588  N  N   . VAL A 1 82  ? -6.082  1.677   15.123  1.00 25.42 ? 81   VAL A N   1 
ATOM   589  C  CA  . VAL A 1 82  ? -5.601  0.597   15.974  1.00 25.19 ? 81   VAL A CA  1 
ATOM   590  C  C   . VAL A 1 82  ? -6.805  -0.003  16.698  1.00 25.36 ? 81   VAL A C   1 
ATOM   591  O  O   . VAL A 1 82  ? -6.953  -1.219  16.780  1.00 26.42 ? 81   VAL A O   1 
ATOM   592  C  CB  . VAL A 1 82  ? -4.499  1.077   16.963  1.00 24.43 ? 81   VAL A CB  1 
ATOM   593  C  CG1 . VAL A 1 82  ? -4.203  -0.003  18.019  1.00 23.69 ? 81   VAL A CG1 1 
ATOM   594  C  CG2 . VAL A 1 82  ? -3.200  1.433   16.217  1.00 24.93 ? 81   VAL A CG2 1 
ATOM   595  N  N   . GLY A 1 83  ? -7.707  0.860   17.164  1.00 25.49 ? 82   GLY A N   1 
ATOM   596  C  CA  . GLY A 1 83  ? -8.869  0.437   17.915  1.00 25.12 ? 82   GLY A CA  1 
ATOM   597  C  C   . GLY A 1 83  ? -9.997  -0.226  17.153  1.00 23.41 ? 82   GLY A C   1 
ATOM   598  O  O   . GLY A 1 83  ? -10.969 -0.541  17.782  1.00 27.50 ? 82   GLY A O   1 
ATOM   599  N  N   . ASP A 1 84  ? -9.840  -0.440  15.851  1.00 23.15 ? 83   ASP A N   1 
ATOM   600  C  CA  . ASP A 1 84  ? -10.897 -0.936  14.979  1.00 20.82 ? 83   ASP A CA  1 
ATOM   601  C  C   . ASP A 1 84  ? -11.068 -2.472  15.024  1.00 20.96 ? 83   ASP A C   1 
ATOM   602  O  O   . ASP A 1 84  ? -10.479 -3.195  14.222  1.00 23.38 ? 83   ASP A O   1 
ATOM   603  C  CB  . ASP A 1 84  ? -10.618 -0.516  13.567  1.00 21.25 ? 83   ASP A CB  1 
ATOM   604  C  CG  . ASP A 1 84  ? -11.006 0.944   13.284  1.00 18.70 ? 83   ASP A CG  1 
ATOM   605  O  OD1 . ASP A 1 84  ? -11.651 1.572   14.144  1.00 25.43 ? 83   ASP A OD1 1 
ATOM   606  O  OD2 . ASP A 1 84  ? -10.732 1.517   12.224  1.00 25.57 ? 83   ASP A OD2 1 
ATOM   607  N  N   . LEU A 1 85  ? -11.916 -2.952  15.909  1.00 21.50 ? 84   LEU A N   1 
ATOM   608  C  CA  . LEU A 1 85  ? -12.102 -4.393  16.063  1.00 20.67 ? 84   LEU A CA  1 
ATOM   609  C  C   . LEU A 1 85  ? -13.416 -4.829  15.405  1.00 21.86 ? 84   LEU A C   1 
ATOM   610  O  O   . LEU A 1 85  ? -13.858 -5.986  15.518  1.00 24.95 ? 84   LEU A O   1 
ATOM   611  C  CB  . LEU A 1 85  ? -11.980 -4.785  17.524  1.00 20.35 ? 84   LEU A CB  1 
ATOM   612  C  CG  . LEU A 1 85  ? -10.613 -4.526  18.124  1.00 18.72 ? 84   LEU A CG  1 
ATOM   613  C  CD1 . LEU A 1 85  ? -10.684 -4.810  19.604  1.00 23.34 ? 84   LEU A CD1 1 
ATOM   614  C  CD2 . LEU A 1 85  ? -9.498  -5.274  17.390  1.00 21.10 ? 84   LEU A CD2 1 
ATOM   615  N  N   . GLY A 1 86  ? -14.034 -3.909  14.673  1.00 22.79 ? 85   GLY A N   1 
ATOM   616  C  CA  . GLY A 1 86  ? -15.224 -4.240  13.898  1.00 23.91 ? 85   GLY A CA  1 
ATOM   617  C  C   . GLY A 1 86  ? -16.546 -4.365  14.626  1.00 23.25 ? 85   GLY A C   1 
ATOM   618  O  O   . GLY A 1 86  ? -16.982 -3.454  15.317  1.00 25.91 ? 85   GLY A O   1 
ATOM   619  N  N   . ASN A 1 87  ? -17.180 -5.521  14.488  1.00 23.97 ? 86   ASN A N   1 
ATOM   620  C  CA  . ASN A 1 87  ? -18.495 -5.761  15.042  1.00 23.58 ? 86   ASN A CA  1 
ATOM   621  C  C   . ASN A 1 87  ? -18.585 -7.065  15.762  1.00 23.13 ? 86   ASN A C   1 
ATOM   622  O  O   . ASN A 1 87  ? -17.849 -8.009  15.465  1.00 24.91 ? 86   ASN A O   1 
ATOM   623  C  CB  . ASN A 1 87  ? -19.526 -5.850  13.936  1.00 22.56 ? 86   ASN A CB  1 
ATOM   624  C  CG  . ASN A 1 87  ? -19.830 -4.528  13.310  1.00 24.28 ? 86   ASN A CG  1 
ATOM   625  O  OD1 . ASN A 1 87  ? -20.266 -3.583  13.978  1.00 23.29 ? 86   ASN A OD1 1 
ATOM   626  N  ND2 . ASN A 1 87  ? -19.604 -4.446  12.009  1.00 26.26 ? 86   ASN A ND2 1 
ATOM   627  N  N   . VAL A 1 88  ? -19.512 -7.118  16.699  1.00 24.84 ? 87   VAL A N   1 
ATOM   628  C  CA  . VAL A 1 88  ? -19.805 -8.370  17.373  1.00 24.09 ? 87   VAL A CA  1 
ATOM   629  C  C   . VAL A 1 88  ? -21.251 -8.734  17.097  1.00 24.04 ? 87   VAL A C   1 
ATOM   630  O  O   . VAL A 1 88  ? -22.087 -7.868  16.839  1.00 25.82 ? 87   VAL A O   1 
ATOM   631  C  CB  . VAL A 1 88  ? -19.530 -8.311  18.891  1.00 22.76 ? 87   VAL A CB  1 
ATOM   632  C  CG1 . VAL A 1 88  ? -18.022 -8.183  19.163  1.00 24.39 ? 87   VAL A CG1 1 
ATOM   633  C  CG2 . VAL A 1 88  ? -20.350 -7.185  19.576  1.00 23.49 ? 87   VAL A CG2 1 
ATOM   634  N  N   . THR A 1 89  ? -21.580 -10.016 17.133  1.00 25.13 ? 88   THR A N   1 
ATOM   635  C  CA  . THR A 1 89  ? -22.969 -10.384 16.845  1.00 25.52 ? 88   THR A CA  1 
ATOM   636  C  C   . THR A 1 89  ? -23.805 -10.842 18.040  1.00 24.86 ? 88   THR A C   1 
ATOM   637  O  O   . THR A 1 89  ? -23.434 -11.749 18.774  1.00 26.40 ? 88   THR A O   1 
ATOM   638  C  CB  . THR A 1 89  ? -23.042 -11.415 15.720  1.00 25.20 ? 88   THR A CB  1 
ATOM   639  O  OG1 . THR A 1 89  ? -22.320 -10.913 14.598  1.00 28.47 ? 88   THR A OG1 1 
ATOM   640  C  CG2 . THR A 1 89  ? -24.477 -11.506 15.195  1.00 23.28 ? 88   THR A CG2 1 
ATOM   641  N  N   . ALA A 1 90  ? -24.930 -10.187 18.253  1.00 25.45 ? 89   ALA A N   1 
ATOM   642  C  CA  . ALA A 1 90  ? -25.833 -10.578 19.324  1.00 25.57 ? 89   ALA A CA  1 
ATOM   643  C  C   . ALA A 1 90  ? -26.913 -11.466 18.737  1.00 26.03 ? 89   ALA A C   1 
ATOM   644  O  O   . ALA A 1 90  ? -27.481 -11.144 17.692  1.00 26.89 ? 89   ALA A O   1 
ATOM   645  C  CB  . ALA A 1 90  ? -26.465 -9.358  19.974  1.00 25.40 ? 89   ALA A CB  1 
ATOM   646  N  N   . ASP A 1 91  ? -27.189 -12.575 19.412  1.00 26.70 ? 90   ASP A N   1 
ATOM   647  C  CA  . ASP A 1 91  ? -28.242 -13.497 18.992  1.00 27.08 ? 90   ASP A CA  1 
ATOM   648  C  C   . ASP A 1 91  ? -29.623 -12.959 19.412  1.00 26.94 ? 90   ASP A C   1 
ATOM   649  O  O   . ASP A 1 91  ? -29.723 -11.825 19.888  1.00 28.19 ? 90   ASP A O   1 
ATOM   650  C  CB  . ASP A 1 91  ? -27.970 -14.914 19.527  1.00 26.79 ? 90   ASP A CB  1 
ATOM   651  C  CG  . ASP A 1 91  ? -28.066 -15.020 21.059  1.00 28.04 ? 90   ASP A CG  1 
ATOM   652  O  OD1 . ASP A 1 91  ? -28.589 -14.096 21.740  1.00 27.22 ? 90   ASP A OD1 1 
ATOM   653  O  OD2 . ASP A 1 91  ? -27.662 -16.036 21.684  1.00 30.04 ? 90   ASP A OD2 1 
ATOM   654  N  N   . LYS A 1 92  ? -30.664 -13.769 19.276  1.00 27.00 ? 91   LYS A N   1 
ATOM   655  C  CA  . LYS A 1 92  ? -32.028 -13.326 19.552  1.00 25.76 ? 91   LYS A CA  1 
ATOM   656  C  C   . LYS A 1 92  ? -32.332 -13.162 21.037  1.00 24.99 ? 91   LYS A C   1 
ATOM   657  O  O   . LYS A 1 92  ? -33.331 -12.554 21.392  1.00 24.82 ? 91   LYS A O   1 
ATOM   658  C  CB  . LYS A 1 92  ? -33.048 -14.253 18.875  1.00 26.51 ? 91   LYS A CB  1 
ATOM   659  C  CG  . LYS A 1 92  ? -33.072 -15.674 19.426  1.00 25.97 ? 91   LYS A CG  1 
ATOM   660  C  CD  . LYS A 1 92  ? -33.073 -16.692 18.297  1.00 29.95 ? 91   LYS A CD  1 
ATOM   661  C  CE  . LYS A 1 92  ? -33.008 -18.125 18.826  1.00 31.46 ? 91   LYS A CE  1 
ATOM   662  N  NZ  . LYS A 1 92  ? -33.948 -18.355 19.974  1.00 32.75 ? 91   LYS A NZ  1 
ATOM   663  N  N   . ASP A 1 93  ? -31.482 -13.714 21.894  1.00 24.90 ? 92   ASP A N   1 
ATOM   664  C  CA  . ASP A 1 93  ? -31.583 -13.512 23.332  1.00 24.95 ? 92   ASP A CA  1 
ATOM   665  C  C   . ASP A 1 93  ? -30.679 -12.388 23.854  1.00 24.74 ? 92   ASP A C   1 
ATOM   666  O  O   . ASP A 1 93  ? -30.450 -12.289 25.054  1.00 25.52 ? 92   ASP A O   1 
ATOM   667  C  CB  . ASP A 1 93  ? -31.257 -14.792 24.083  1.00 24.89 ? 92   ASP A CB  1 
ATOM   668  C  CG  . ASP A 1 93  ? -32.042 -15.979 23.573  1.00 26.28 ? 92   ASP A CG  1 
ATOM   669  O  OD1 . ASP A 1 93  ? -33.307 -15.949 23.606  1.00 24.06 ? 92   ASP A OD1 1 
ATOM   670  O  OD2 . ASP A 1 93  ? -31.472 -16.995 23.104  1.00 30.70 ? 92   ASP A OD2 1 
ATOM   671  N  N   . GLY A 1 94  ? -30.162 -11.545 22.958  1.00 24.95 ? 93   GLY A N   1 
ATOM   672  C  CA  . GLY A 1 94  ? -29.306 -10.417 23.322  1.00 23.88 ? 93   GLY A CA  1 
ATOM   673  C  C   . GLY A 1 94  ? -27.845 -10.682 23.661  1.00 23.49 ? 93   GLY A C   1 
ATOM   674  O  O   . GLY A 1 94  ? -27.104 -9.808  24.172  1.00 24.95 ? 93   GLY A O   1 
ATOM   675  N  N   . VAL A 1 95  ? -27.417 -11.890 23.334  1.00 23.51 ? 94   VAL A N   1 
ATOM   676  C  CA  . VAL A 1 95  ? -26.102 -12.386 23.691  1.00 23.09 ? 94   VAL A CA  1 
ATOM   677  C  C   . VAL A 1 95  ? -25.124 -12.420 22.521  1.00 23.31 ? 94   VAL A C   1 
ATOM   678  O  O   . VAL A 1 95  ? -25.385 -13.002 21.451  1.00 24.29 ? 94   VAL A O   1 
ATOM   679  C  CB  . VAL A 1 95  ? -26.222 -13.796 24.315  1.00 21.57 ? 94   VAL A CB  1 
ATOM   680  C  CG1 . VAL A 1 95  ? -24.846 -14.362 24.686  1.00 22.56 ? 94   VAL A CG1 1 
ATOM   681  C  CG2 . VAL A 1 95  ? -27.103 -13.727 25.549  1.00 21.94 ? 94   VAL A CG2 1 
ATOM   682  N  N   . ALA A 1 96  ? -23.995 -11.777 22.745  1.00 25.14 ? 95   ALA A N   1 
ATOM   683  C  CA  . ALA A 1 96  ? -22.933 -11.715 21.771  1.00 25.65 ? 95   ALA A CA  1 
ATOM   684  C  C   . ALA A 1 96  ? -21.714 -12.447 22.282  1.00 26.21 ? 95   ALA A C   1 
ATOM   685  O  O   . ALA A 1 96  ? -21.038 -12.003 23.222  1.00 27.18 ? 95   ALA A O   1 
ATOM   686  C  CB  . ALA A 1 96  ? -22.601 -10.264 21.400  1.00 24.07 ? 95   ALA A CB  1 
ATOM   687  N  N   . ASP A 1 97  ? -21.477 -13.619 21.696  1.00 27.45 ? 96   ASP A N   1 
ATOM   688  C  CA  . ASP A 1 97  ? -20.225 -14.333 21.912  1.00 28.42 ? 96   ASP A CA  1 
ATOM   689  C  C   . ASP A 1 97  ? -19.091 -13.696 21.071  1.00 27.62 ? 96   ASP A C   1 
ATOM   690  O  O   . ASP A 1 97  ? -19.233 -13.477 19.870  1.00 28.99 ? 96   ASP A O   1 
ATOM   691  C  CB  . ASP A 1 97  ? -20.377 -15.808 21.555  1.00 29.19 ? 96   ASP A CB  1 
ATOM   692  C  CG  . ASP A 1 97  ? -20.204 -16.731 22.768  1.00 33.61 ? 96   ASP A CG  1 
ATOM   693  O  OD1 . ASP A 1 97  ? -21.097 -16.755 23.678  1.00 35.39 ? 96   ASP A OD1 1 
ATOM   694  O  OD2 . ASP A 1 97  ? -19.184 -17.458 22.897  1.00 37.52 ? 96   ASP A OD2 1 
ATOM   695  N  N   . VAL A 1 98  ? -17.971 -13.389 21.710  1.00 28.01 ? 97   VAL A N   1 
ATOM   696  C  CA  . VAL A 1 98  ? -16.852 -12.793 21.004  1.00 27.85 ? 97   VAL A CA  1 
ATOM   697  C  C   . VAL A 1 98  ? -15.686 -13.759 20.948  1.00 28.00 ? 97   VAL A C   1 
ATOM   698  O  O   . VAL A 1 98  ? -15.342 -14.335 21.957  1.00 29.23 ? 97   VAL A O   1 
ATOM   699  C  CB  . VAL A 1 98  ? -16.355 -11.580 21.752  1.00 27.53 ? 97   VAL A CB  1 
ATOM   700  C  CG1 . VAL A 1 98  ? -15.131 -10.979 21.042  1.00 27.77 ? 97   VAL A CG1 1 
ATOM   701  C  CG2 . VAL A 1 98  ? -17.469 -10.590 21.978  1.00 26.97 ? 97   VAL A CG2 1 
ATOM   702  N  N   . SER A 1 99  ? -15.113 -13.953 19.761  1.00 28.36 ? 98   SER A N   1 
ATOM   703  C  CA  . SER A 1 99  ? -13.886 -14.734 19.563  1.00 28.64 ? 98   SER A CA  1 
ATOM   704  C  C   . SER A 1 99  ? -13.146 -14.166 18.356  1.00 28.97 ? 98   SER A C   1 
ATOM   705  O  O   . SER A 1 99  ? -13.499 -14.429 17.196  1.00 30.18 ? 98   SER A O   1 
ATOM   706  C  CB  . SER A 1 99  ? -14.153 -16.214 19.348  1.00 28.48 ? 98   SER A CB  1 
ATOM   707  O  OG  . SER A 1 99  ? -12.937 -16.947 19.489  1.00 30.37 ? 98   SER A OG  1 
ATOM   708  N  N   . ILE A 1 100 ? -12.093 -13.417 18.638  1.00 29.19 ? 99   ILE A N   1 
ATOM   709  C  CA  . ILE A 1 100 ? -11.401 -12.659 17.631  1.00 27.87 ? 99   ILE A CA  1 
ATOM   710  C  C   . ILE A 1 100 ? -9.930  -12.858 17.796  1.00 27.36 ? 99   ILE A C   1 
ATOM   711  O  O   . ILE A 1 100 ? -9.429  -13.098 18.894  1.00 28.34 ? 99   ILE A O   1 
ATOM   712  C  CB  . ILE A 1 100 ? -11.664 -11.151 17.876  1.00 28.12 ? 99   ILE A CB  1 
ATOM   713  C  CG1 . ILE A 1 100 ? -13.148 -10.797 17.693  1.00 29.38 ? 99   ILE A CG1 1 
ATOM   714  C  CG2 . ILE A 1 100 ? -10.809 -10.342 16.954  1.00 28.69 ? 99   ILE A CG2 1 
ATOM   715  C  CD1 . ILE A 1 100 ? -13.485 -9.370  18.067  1.00 26.20 ? 99   ILE A CD1 1 
ATOM   716  N  N   . GLU A 1 101 ? -9.221  -12.743 16.692  1.00 26.79 ? 100  GLU A N   1 
ATOM   717  C  CA  . GLU A 1 101 ? -7.797  -12.659 16.757  1.00 25.47 ? 100  GLU A CA  1 
ATOM   718  C  C   . GLU A 1 101 ? -7.445  -11.381 16.007  1.00 25.37 ? 100  GLU A C   1 
ATOM   719  O  O   . GLU A 1 101 ? -7.982  -11.143 14.934  1.00 26.38 ? 100  GLU A O   1 
ATOM   720  C  CB  . GLU A 1 101 ? -7.187  -13.881 16.120  1.00 25.23 ? 100  GLU A CB  1 
ATOM   721  C  CG  . GLU A 1 101 ? -5.674  -13.923 16.194  1.00 25.09 ? 100  GLU A CG  1 
ATOM   722  C  CD  . GLU A 1 101 ? -5.180  -15.314 15.948  1.00 26.53 ? 100  GLU A CD  1 
ATOM   723  O  OE1 . GLU A 1 101 ? -5.259  -16.111 16.906  1.00 29.32 ? 100  GLU A OE1 1 
ATOM   724  O  OE2 . GLU A 1 101 ? -4.742  -15.604 14.805  1.00 28.02 ? 100  GLU A OE2 1 
ATOM   725  N  N   . ASP A 1 102 ? -6.576  -10.549 16.582  1.00 26.33 ? 101  ASP A N   1 
ATOM   726  C  CA  . ASP A 1 102 ? -6.142  -9.291  15.949  1.00 25.98 ? 101  ASP A CA  1 
ATOM   727  C  C   . ASP A 1 102 ? -4.636  -9.084  16.079  1.00 26.72 ? 101  ASP A C   1 
ATOM   728  O  O   . ASP A 1 102 ? -4.044  -9.349  17.146  1.00 27.07 ? 101  ASP A O   1 
ATOM   729  C  CB  . ASP A 1 102 ? -6.860  -8.084  16.571  1.00 25.42 ? 101  ASP A CB  1 
ATOM   730  C  CG  . ASP A 1 102 ? -6.831  -6.859  15.656  1.00 25.02 ? 101  ASP A CG  1 
ATOM   731  O  OD1 . ASP A 1 102 ? -7.566  -6.854  14.649  1.00 29.92 ? 101  ASP A OD1 1 
ATOM   732  O  OD2 . ASP A 1 102 ? -6.106  -5.860  15.849  1.00 28.11 ? 101  ASP A OD2 1 
ATOM   733  N  N   . SER A 1 103 ? -4.018  -8.550  15.032  1.00 27.55 ? 102  SER A N   1 
ATOM   734  C  CA  . SER A 1 103 ? -2.566  -8.356  15.049  1.00 28.19 ? 102  SER A CA  1 
ATOM   735  C  C   . SER A 1 103 ? -2.143  -6.898  14.938  1.00 27.19 ? 102  SER A C   1 
ATOM   736  O  O   . SER A 1 103 ? -0.990  -6.587  14.590  1.00 28.32 ? 102  SER A O   1 
ATOM   737  C  CB  . SER A 1 103 ? -1.921  -9.150  13.934  1.00 28.23 ? 102  SER A CB  1 
ATOM   738  O  OG  . SER A 1 103 ? -2.348  -10.496 13.984  1.00 32.25 ? 102  SER A OG  1 
ATOM   739  N  N   . VAL A 1 104 ? -3.086  -6.010  15.196  1.00 27.23 ? 103  VAL A N   1 
ATOM   740  C  CA  . VAL A 1 104 ? -2.804  -4.595  15.146  1.00 25.88 ? 103  VAL A CA  1 
ATOM   741  C  C   . VAL A 1 104 ? -2.794  -4.067  16.579  1.00 26.26 ? 103  VAL A C   1 
ATOM   742  O  O   . VAL A 1 104 ? -1.945  -3.248  16.970  1.00 27.38 ? 103  VAL A O   1 
ATOM   743  C  CB  . VAL A 1 104 ? -3.834  -3.880  14.279  1.00 25.05 ? 103  VAL A CB  1 
ATOM   744  C  CG1 . VAL A 1 104 ? -3.617  -2.368  14.357  1.00 26.21 ? 103  VAL A CG1 1 
ATOM   745  C  CG2 . VAL A 1 104 ? -3.753  -4.372  12.826  1.00 26.13 ? 103  VAL A CG2 1 
ATOM   746  N  N   . ILE A 1 105 ? -3.753  -4.527  17.362  1.00 26.10 ? 104  ILE A N   1 
ATOM   747  C  CA  . ILE A 1 105 ? -3.757  -4.211  18.765  1.00 25.04 ? 104  ILE A CA  1 
ATOM   748  C  C   . ILE A 1 105 ? -2.598  -4.941  19.390  1.00 24.66 ? 104  ILE A C   1 
ATOM   749  O  O   . ILE A 1 105 ? -2.070  -5.884  18.810  1.00 25.36 ? 104  ILE A O   1 
ATOM   750  C  CB  . ILE A 1 105 ? -5.114  -4.555  19.487  1.00 24.43 ? 104  ILE A CB  1 
ATOM   751  C  CG1 . ILE A 1 105 ? -5.512  -6.029  19.323  1.00 21.52 ? 104  ILE A CG1 1 
ATOM   752  C  CG2 . ILE A 1 105 ? -6.190  -3.644  19.026  1.00 24.06 ? 104  ILE A CG2 1 
ATOM   753  C  CD1 . ILE A 1 105 ? -6.654  -6.465  20.267  1.00 26.29 ? 104  ILE A CD1 1 
ATOM   754  N  N   . SER A 1 106 ? -2.210  -4.477  20.568  1.00 24.41 ? 105  SER A N   1 
ATOM   755  C  CA  . SER A 1 106 ? -1.184  -5.091  21.383  1.00 24.31 ? 105  SER A CA  1 
ATOM   756  C  C   . SER A 1 106 ? -1.427  -4.880  22.881  1.00 23.43 ? 105  SER A C   1 
ATOM   757  O  O   . SER A 1 106 ? -2.167  -3.963  23.290  1.00 26.89 ? 105  SER A O   1 
ATOM   758  C  CB  . SER A 1 106 ? 0.200   -4.541  20.986  1.00 21.60 ? 105  SER A CB  1 
ATOM   759  O  OG  . SER A 1 106 ? 1.230   -5.473  21.271  1.00 27.33 ? 105  SER A OG  1 
ATOM   760  N  N   . LEU A 1 107 ? -0.793  -5.729  23.698  1.00 25.36 ? 106  LEU A N   1 
ATOM   761  C  CA  . LEU A 1 107 ? -0.817  -5.603  25.157  1.00 24.69 ? 106  LEU A CA  1 
ATOM   762  C  C   . LEU A 1 107 ? 0.513   -5.024  25.632  1.00 26.03 ? 106  LEU A C   1 
ATOM   763  O  O   . LEU A 1 107 ? 0.787   -4.967  26.833  1.00 27.27 ? 106  LEU A O   1 
ATOM   764  C  CB  . LEU A 1 107 ? -1.088  -6.951  25.830  1.00 24.34 ? 106  LEU A CB  1 
ATOM   765  C  CG  . LEU A 1 107 ? -2.435  -7.587  25.481  1.00 21.85 ? 106  LEU A CG  1 
ATOM   766  C  CD1 . LEU A 1 107 ? -2.789  -8.863  26.306  1.00 23.43 ? 106  LEU A CD1 1 
ATOM   767  C  CD2 . LEU A 1 107 ? -3.569  -6.532  25.564  1.00 24.07 ? 106  LEU A CD2 1 
ATOM   768  N  N   . SER A 1 108 ? 1.319   -4.556  24.695  1.00 27.27 ? 107  SER A N   1 
ATOM   769  C  CA  . SER A 1 108 ? 2.612   -3.934  24.998  1.00 29.14 ? 107  SER A CA  1 
ATOM   770  C  C   . SER A 1 108 ? 3.036   -3.049  23.825  1.00 29.56 ? 107  SER A C   1 
ATOM   771  O  O   . SER A 1 108 ? 2.537   -3.239  22.714  1.00 31.28 ? 107  SER A O   1 
ATOM   772  C  CB  . SER A 1 108 ? 3.697   -4.997  25.279  1.00 29.29 ? 107  SER A CB  1 
ATOM   773  O  OG  . SER A 1 108 ? 3.665   -6.091  24.356  1.00 31.56 ? 107  SER A OG  1 
ATOM   774  N  N   . GLY A 1 109 ? 3.947   -2.099  24.058  1.00 29.61 ? 108  GLY A N   1 
ATOM   775  C  CA  . GLY A 1 109 ? 4.453   -1.226  22.999  1.00 28.83 ? 108  GLY A CA  1 
ATOM   776  C  C   . GLY A 1 109 ? 3.627   0.012   22.658  1.00 28.48 ? 108  GLY A C   1 
ATOM   777  O  O   . GLY A 1 109 ? 2.778   0.432   23.444  1.00 29.81 ? 108  GLY A O   1 
ATOM   778  N  N   . ASP A 1 110 ? 3.852   0.585   21.476  1.00 28.26 ? 109  ASP A N   1 
ATOM   779  C  CA  . ASP A 1 110 ? 3.121   1.792   21.077  1.00 27.54 ? 109  ASP A CA  1 
ATOM   780  C  C   . ASP A 1 110 ? 1.626   1.532   20.808  1.00 26.47 ? 109  ASP A C   1 
ATOM   781  O  O   . ASP A 1 110 ? 0.807   2.439   20.911  1.00 27.24 ? 109  ASP A O   1 
ATOM   782  C  CB  . ASP A 1 110 ? 3.719   2.472   19.829  1.00 27.91 ? 109  ASP A CB  1 
ATOM   783  C  CG  . ASP A 1 110 ? 5.233   2.424   19.763  1.00 29.72 ? 109  ASP A CG  1 
ATOM   784  O  OD1 . ASP A 1 110 ? 5.751   2.390   18.617  1.00 33.39 ? 109  ASP A OD1 1 
ATOM   785  O  OD2 . ASP A 1 110 ? 5.999   2.451   20.752  1.00 34.66 ? 109  ASP A OD2 1 
ATOM   786  N  N   . HIS A 1 111 ? 1.262   0.307   20.441  1.00 25.65 ? 110  HIS A N   1 
ATOM   787  C  CA  . HIS A 1 111 ? -0.141  -0.019  20.204  1.00 24.84 ? 110  HIS A CA  1 
ATOM   788  C  C   . HIS A 1 111 ? -0.866  -0.611  21.435  1.00 23.67 ? 110  HIS A C   1 
ATOM   789  O  O   . HIS A 1 111 ? -2.032  -1.043  21.341  1.00 25.04 ? 110  HIS A O   1 
ATOM   790  C  CB  . HIS A 1 111 ? -0.260  -0.986  19.018  1.00 24.19 ? 110  HIS A CB  1 
ATOM   791  C  CG  . HIS A 1 111 ? 0.131   -0.399  17.698  1.00 24.93 ? 110  HIS A CG  1 
ATOM   792  N  ND1 . HIS A 1 111 ? 0.115   -1.136  16.534  1.00 25.31 ? 110  HIS A ND1 1 
ATOM   793  C  CD2 . HIS A 1 111 ? 0.551   0.845   17.352  1.00 24.95 ? 110  HIS A CD2 1 
ATOM   794  C  CE1 . HIS A 1 111 ? 0.508   -0.378  15.530  1.00 25.71 ? 110  HIS A CE1 1 
ATOM   795  N  NE2 . HIS A 1 111 ? 0.780   0.828   15.998  1.00 29.22 ? 110  HIS A NE2 1 
ATOM   796  N  N   . CYS A 1 112 ? -0.191  -0.645  22.582  1.00 23.62 ? 111  CYS A N   1 
ATOM   797  C  CA  . CYS A 1 112 ? -0.771  -1.206  23.796  1.00 23.49 ? 111  CYS A CA  1 
ATOM   798  C  C   . CYS A 1 112 ? -2.161  -0.649  24.173  1.00 22.66 ? 111  CYS A C   1 
ATOM   799  O  O   . CYS A 1 112 ? -2.387  0.550   24.256  1.00 24.69 ? 111  CYS A O   1 
ATOM   800  C  CB  . CYS A 1 112 ? 0.214   -1.140  24.973  1.00 21.43 ? 111  CYS A CB  1 
ATOM   801  S  SG  . CYS A 1 112 ? -0.402  -1.748  26.533  1.00 26.63 ? 111  CYS A SG  1 
ATOM   802  N  N   . ILE A 1 113 ? -3.096  -1.535  24.421  1.00 23.00 ? 112  ILE A N   1 
ATOM   803  C  CA  . ILE A 1 113 ? -4.412  -1.111  24.834  1.00 21.55 ? 112  ILE A CA  1 
ATOM   804  C  C   . ILE A 1 113 ? -4.704  -1.169  26.331  1.00 22.01 ? 112  ILE A C   1 
ATOM   805  O  O   . ILE A 1 113 ? -5.805  -0.806  26.755  1.00 24.25 ? 112  ILE A O   1 
ATOM   806  C  CB  . ILE A 1 113 ? -5.476  -1.794  24.010  1.00 18.70 ? 112  ILE A CB  1 
ATOM   807  C  CG1 . ILE A 1 113 ? -5.477  -3.343  24.193  1.00 17.52 ? 112  ILE A CG1 1 
ATOM   808  C  CG2 . ILE A 1 113 ? -5.328  -1.392  22.541  1.00 22.61 ? 112  ILE A CG2 1 
ATOM   809  C  CD1 . ILE A 1 113 ? -6.606  -3.954  23.311  1.00 20.01 ? 112  ILE A CD1 1 
ATOM   810  N  N   . ILE A 1 114 ? -3.734  -1.644  27.128  1.00 22.74 ? 113  ILE A N   1 
ATOM   811  C  CA  . ILE A 1 114 ? -3.936  -1.751  28.573  1.00 21.46 ? 113  ILE A CA  1 
ATOM   812  C  C   . ILE A 1 114 ? -4.112  -0.319  29.033  1.00 21.10 ? 113  ILE A C   1 
ATOM   813  O  O   . ILE A 1 114 ? -3.262  0.522   28.709  1.00 22.90 ? 113  ILE A O   1 
ATOM   814  C  CB  . ILE A 1 114 ? -2.700  -2.296  29.262  1.00 19.75 ? 113  ILE A CB  1 
ATOM   815  C  CG1 . ILE A 1 114 ? -2.472  -3.786  28.928  1.00 20.96 ? 113  ILE A CG1 1 
ATOM   816  C  CG2 . ILE A 1 114 ? -2.789  -2.085  30.778  1.00 21.67 ? 113  ILE A CG2 1 
ATOM   817  C  CD1 . ILE A 1 114 ? -3.732  -4.394  28.559  1.00 20.68 ? 113  ILE A CD1 1 
ATOM   818  N  N   . GLY A 1 115 ? -5.183  -0.072  29.771  1.00 24.33 ? 114  GLY A N   1 
ATOM   819  C  CA  . GLY A 1 115 ? -5.460  1.247   30.338  1.00 22.92 ? 114  GLY A CA  1 
ATOM   820  C  C   . GLY A 1 115 ? -6.307  2.094   29.436  1.00 20.84 ? 114  GLY A C   1 
ATOM   821  O  O   . GLY A 1 115 ? -6.572  3.264   29.723  1.00 22.72 ? 114  GLY A O   1 
ATOM   822  N  N   . ARG A 1 116 ? -6.650  1.572   28.273  1.00 21.48 ? 115  ARG A N   1 
ATOM   823  C  CA  . ARG A 1 116 ? -7.510  2.273   27.389  1.00 19.34 ? 115  ARG A CA  1 
ATOM   824  C  C   . ARG A 1 116 ? -8.919  1.708   27.628  1.00 20.68 ? 115  ARG A C   1 
ATOM   825  O  O   . ARG A 1 116 ? -9.125  0.944   28.565  1.00 24.04 ? 115  ARG A O   1 
ATOM   826  C  CB  . ARG A 1 116 ? -6.974  2.166   25.955  1.00 17.42 ? 115  ARG A CB  1 
ATOM   827  C  CG  . ARG A 1 116 ? -5.521  2.728   25.848  1.00 13.08 ? 115  ARG A CG  1 
ATOM   828  C  CD  . ARG A 1 116 ? -5.069  3.120   24.414  1.00 13.57 ? 115  ARG A CD  1 
ATOM   829  N  NE  . ARG A 1 116 ? -3.663  3.413   24.438  1.00 17.26 ? 115  ARG A NE  1 
ATOM   830  C  CZ  . ARG A 1 116 ? -3.209  4.643   24.621  1.00 12.44 ? 115  ARG A CZ  1 
ATOM   831  N  NH1 . ARG A 1 116 ? -4.109  5.599   24.782  1.00 23.05 ? 115  ARG A NH1 1 
ATOM   832  N  NH2 . ARG A 1 116 ? -1.912  4.918   24.612  1.00 18.57 ? 115  ARG A NH2 1 
ATOM   833  N  N   . THR A 1 117 ? -9.905  2.131   26.851  1.00 20.49 ? 116  THR A N   1 
ATOM   834  C  CA  . THR A 1 117 ? -11.288 1.719   27.046  1.00 20.85 ? 116  THR A CA  1 
ATOM   835  C  C   . THR A 1 117 ? -11.911 0.930   25.858  1.00 20.03 ? 116  THR A C   1 
ATOM   836  O  O   . THR A 1 117 ? -11.824 1.306   24.652  1.00 24.44 ? 116  THR A O   1 
ATOM   837  C  CB  . THR A 1 117 ? -12.131 2.979   27.459  1.00 15.86 ? 116  THR A CB  1 
ATOM   838  O  OG1 . THR A 1 117 ? -11.818 3.346   28.793  1.00 21.86 ? 116  THR A OG1 1 
ATOM   839  C  CG2 . THR A 1 117 ? -13.666 2.681   27.500  1.00 15.85 ? 116  THR A CG2 1 
ATOM   840  N  N   . LEU A 1 118 ? -12.373 -0.270  26.170  1.00 21.76 ? 117  LEU A N   1 
ATOM   841  C  CA  . LEU A 1 118 ? -13.154 -1.057  25.229  1.00 20.85 ? 117  LEU A CA  1 
ATOM   842  C  C   . LEU A 1 118 ? -14.627 -0.668  25.271  1.00 21.38 ? 117  LEU A C   1 
ATOM   843  O  O   . LEU A 1 118 ? -15.221 -0.613  26.360  1.00 24.49 ? 117  LEU A O   1 
ATOM   844  C  CB  . LEU A 1 118 ? -12.994 -2.542  25.569  1.00 19.69 ? 117  LEU A CB  1 
ATOM   845  C  CG  . LEU A 1 118 ? -13.644 -3.466  24.528  1.00 17.55 ? 117  LEU A CG  1 
ATOM   846  C  CD1 . LEU A 1 118 ? -12.945 -3.446  23.195  1.00 22.97 ? 117  LEU A CD1 1 
ATOM   847  C  CD2 . LEU A 1 118 ? -13.584 -4.933  25.084  1.00 19.21 ? 117  LEU A CD2 1 
ATOM   848  N  N   . VAL A 1 119 ? -15.205 -0.352  24.111  1.00 21.95 ? 118  VAL A N   1 
ATOM   849  C  CA  . VAL A 1 119 ? -16.583 0.098   24.006  1.00 20.88 ? 118  VAL A CA  1 
ATOM   850  C  C   . VAL A 1 119 ? -17.393 -0.741  23.015  1.00 20.60 ? 118  VAL A C   1 
ATOM   851  O  O   . VAL A 1 119 ? -16.940 -1.090  21.858  1.00 23.38 ? 118  VAL A O   1 
ATOM   852  C  CB  . VAL A 1 119 ? -16.677 1.623   23.538  1.00 20.43 ? 118  VAL A CB  1 
ATOM   853  C  CG1 . VAL A 1 119 ? -18.158 2.091   23.412  1.00 19.48 ? 118  VAL A CG1 1 
ATOM   854  C  CG2 . VAL A 1 119 ? -15.825 2.538   24.375  1.00 20.15 ? 118  VAL A CG2 1 
ATOM   855  N  N   . VAL A 1 120 ? -18.567 -1.146  23.480  1.00 21.26 ? 119  VAL A N   1 
ATOM   856  C  CA  . VAL A 1 120 ? -19.554 -1.776  22.626  1.00 20.75 ? 119  VAL A CA  1 
ATOM   857  C  C   . VAL A 1 120 ? -20.648 -0.773  22.288  1.00 19.36 ? 119  VAL A C   1 
ATOM   858  O  O   . VAL A 1 120 ? -21.337 -0.204  23.192  1.00 23.09 ? 119  VAL A O   1 
ATOM   859  C  CB  . VAL A 1 120 ? -20.158 -3.005  23.244  1.00 19.63 ? 119  VAL A CB  1 
ATOM   860  C  CG1 . VAL A 1 120 ? -21.035 -2.639  24.527  1.00 18.70 ? 119  VAL A CG1 1 
ATOM   861  C  CG2 . VAL A 1 120 ? -20.973 -3.765  22.170  1.00 21.02 ? 119  VAL A CG2 1 
ATOM   862  N  N   . HIS A 1 121 ? -20.827 -0.585  20.994  1.00 21.21 ? 120  HIS A N   1 
ATOM   863  C  CA  . HIS A 1 121 ? -21.742 0.416   20.436  1.00 20.48 ? 120  HIS A CA  1 
ATOM   864  C  C   . HIS A 1 121 ? -23.219 0.064   20.149  1.00 22.40 ? 120  HIS A C   1 
ATOM   865  O  O   . HIS A 1 121 ? -23.638 -1.098  20.104  1.00 23.50 ? 120  HIS A O   1 
ATOM   866  C  CB  . HIS A 1 121 ? -21.100 1.030   19.199  1.00 18.58 ? 120  HIS A CB  1 
ATOM   867  C  CG  . HIS A 1 121 ? -19.986 1.973   19.509  1.00 18.71 ? 120  HIS A CG  1 
ATOM   868  N  ND1 . HIS A 1 121 ? -20.189 3.325   19.641  1.00 25.80 ? 120  HIS A ND1 1 
ATOM   869  C  CD2 . HIS A 1 121 ? -18.687 1.752   19.833  1.00 16.97 ? 120  HIS A CD2 1 
ATOM   870  C  CE1 . HIS A 1 121 ? -19.047 3.899   19.972  1.00 17.57 ? 120  HIS A CE1 1 
ATOM   871  N  NE2 . HIS A 1 121 ? -18.107 2.976   20.039  1.00 23.49 ? 120  HIS A NE2 1 
ATOM   872  N  N   . GLU A 1 122 ? -23.991 1.125   19.969  1.00 24.34 ? 121  GLU A N   1 
ATOM   873  C  CA  . GLU A 1 122 ? -25.410 1.076   19.701  1.00 23.68 ? 121  GLU A CA  1 
ATOM   874  C  C   . GLU A 1 122 ? -25.783 0.383   18.392  1.00 24.30 ? 121  GLU A C   1 
ATOM   875  O  O   . GLU A 1 122 ? -26.697 -0.439  18.381  1.00 26.26 ? 121  GLU A O   1 
ATOM   876  C  CB  . GLU A 1 122 ? -25.967 2.509   19.674  1.00 24.98 ? 121  GLU A CB  1 
ATOM   877  C  CG  . GLU A 1 122 ? -27.465 2.578   19.384  1.00 25.47 ? 121  GLU A CG  1 
ATOM   878  C  CD  . GLU A 1 122 ? -27.911 3.917   18.830  1.00 30.50 ? 121  GLU A CD  1 
ATOM   879  O  OE1 . GLU A 1 122 ? -29.014 3.956   18.225  1.00 35.38 ? 121  GLU A OE1 1 
ATOM   880  O  OE2 . GLU A 1 122 ? -27.166 4.925   18.960  1.00 31.89 ? 121  GLU A OE2 1 
ATOM   881  N  N   . LYS A 1 123 ? -25.109 0.740   17.298  1.00 25.23 ? 122  LYS A N   1 
ATOM   882  C  CA  . LYS A 1 123 ? -25.438 0.244   15.940  1.00 25.46 ? 122  LYS A CA  1 
ATOM   883  C  C   . LYS A 1 123 ? -24.262 -0.521  15.338  1.00 25.08 ? 122  LYS A C   1 
ATOM   884  O  O   . LYS A 1 123 ? -23.184 -0.614  15.958  1.00 27.21 ? 122  LYS A O   1 
ATOM   885  C  CB  . LYS A 1 123 ? -25.709 1.411   14.989  1.00 25.96 ? 122  LYS A CB  1 
ATOM   886  C  CG  . LYS A 1 123 ? -26.739 2.446   15.447  1.00 29.01 ? 122  LYS A CG  1 
ATOM   887  C  CD  . LYS A 1 123 ? -26.994 3.446   14.303  1.00 31.16 ? 122  LYS A CD  1 
ATOM   888  C  CE  . LYS A 1 123 ? -28.493 3.745   14.112  1.00 34.38 ? 122  LYS A CE  1 
ATOM   889  N  NZ  . LYS A 1 123 ? -28.850 4.297   12.737  1.00 36.03 ? 122  LYS A NZ  1 
ATOM   890  N  N   . ALA A 1 124 ? -24.453 -1.030  14.122  1.00 25.92 ? 123  ALA A N   1 
ATOM   891  C  CA  . ALA A 1 124 ? -23.388 -1.685  13.389  1.00 24.30 ? 123  ALA A CA  1 
ATOM   892  C  C   . ALA A 1 124 ? -22.313 -0.676  12.982  1.00 24.30 ? 123  ALA A C   1 
ATOM   893  O  O   . ALA A 1 124 ? -22.569 0.516   12.761  1.00 25.30 ? 123  ALA A O   1 
ATOM   894  C  CB  . ALA A 1 124 ? -23.919 -2.414  12.171  1.00 25.16 ? 123  ALA A CB  1 
ATOM   895  N  N   . ASP A 1 125 ? -21.089 -1.138  13.041  1.00 24.24 ? 124  ASP A N   1 
ATOM   896  C  CA  . ASP A 1 125 ? -19.990 -0.383  12.486  1.00 24.03 ? 124  ASP A CA  1 
ATOM   897  C  C   . ASP A 1 125 ? -20.012 -0.647  10.973  1.00 23.56 ? 124  ASP A C   1 
ATOM   898  O  O   . ASP A 1 125 ? -19.930 -1.796  10.512  1.00 24.87 ? 124  ASP A O   1 
ATOM   899  C  CB  . ASP A 1 125 ? -18.725 -0.857  13.199  1.00 24.15 ? 124  ASP A CB  1 
ATOM   900  C  CG  . ASP A 1 125 ? -17.451 -0.283  12.635  1.00 24.23 ? 124  ASP A CG  1 
ATOM   901  O  OD1 . ASP A 1 125 ? -17.449 0.435   11.619  1.00 27.74 ? 124  ASP A OD1 1 
ATOM   902  O  OD2 . ASP A 1 125 ? -16.362 -0.531  13.213  1.00 28.70 ? 124  ASP A OD2 1 
ATOM   903  N  N   . ASP A 1 126 ? -20.115 0.413   10.166  1.00 23.36 ? 125  ASP A N   1 
ATOM   904  C  CA  . ASP A 1 126 ? -20.175 0.226   8.710   1.00 23.08 ? 125  ASP A CA  1 
ATOM   905  C  C   . ASP A 1 126 ? -18.830 -0.035  8.018   1.00 22.80 ? 125  ASP A C   1 
ATOM   906  O  O   . ASP A 1 126 ? -18.777 -0.113  6.806   1.00 24.14 ? 125  ASP A O   1 
ATOM   907  C  CB  . ASP A 1 126 ? -21.005 1.295   7.997   1.00 22.04 ? 125  ASP A CB  1 
ATOM   908  C  CG  . ASP A 1 126 ? -20.402 2.667   8.083   1.00 20.48 ? 125  ASP A CG  1 
ATOM   909  O  OD1 . ASP A 1 126 ? -19.168 2.798   8.146   1.00 25.34 ? 125  ASP A OD1 1 
ATOM   910  O  OD2 . ASP A 1 126 ? -21.112 3.687   8.085   1.00 24.46 ? 125  ASP A OD2 1 
ATOM   911  N  N   . LEU A 1 127 ? -17.783 -0.182  8.840   1.00 24.82 ? 126  LEU A N   1 
ATOM   912  C  CA  . LEU A 1 127 ? -16.412 -0.475  8.448   1.00 24.17 ? 126  LEU A CA  1 
ATOM   913  C  C   . LEU A 1 127 ? -15.867 0.528   7.444   1.00 24.50 ? 126  LEU A C   1 
ATOM   914  O  O   . LEU A 1 127 ? -15.025 0.215   6.608   1.00 25.60 ? 126  LEU A O   1 
ATOM   915  C  CB  . LEU A 1 127 ? -16.312 -1.916  7.950   1.00 23.57 ? 126  LEU A CB  1 
ATOM   916  C  CG  . LEU A 1 127 ? -17.046 -2.866  8.912   1.00 23.72 ? 126  LEU A CG  1 
ATOM   917  C  CD1 . LEU A 1 127 ? -17.246 -4.267  8.314   1.00 24.52 ? 126  LEU A CD1 1 
ATOM   918  C  CD2 . LEU A 1 127 ? -16.322 -2.975  10.240  1.00 20.96 ? 126  LEU A CD2 1 
ATOM   919  N  N   . GLY A 1 128 ? -16.360 1.754   7.531   1.00 24.57 ? 127  GLY A N   1 
ATOM   920  C  CA  . GLY A 1 128 ? -15.968 2.769   6.587   1.00 23.67 ? 127  GLY A CA  1 
ATOM   921  C  C   . GLY A 1 128 ? -16.526 2.559   5.182   1.00 22.84 ? 127  GLY A C   1 
ATOM   922  O  O   . GLY A 1 128 ? -16.010 3.086   4.222   1.00 24.00 ? 127  GLY A O   1 
ATOM   923  N  N   . LYS A 1 129 ? -17.582 1.770   5.056   1.00 24.08 ? 128  LYS A N   1 
ATOM   924  C  CA  . LYS A 1 129 ? -18.217 1.548   3.767   1.00 23.41 ? 128  LYS A CA  1 
ATOM   925  C  C   . LYS A 1 129 ? -19.607 2.096   3.733   1.00 23.27 ? 128  LYS A C   1 
ATOM   926  O  O   . LYS A 1 129 ? -20.398 1.667   2.926   1.00 23.87 ? 128  LYS A O   1 
ATOM   927  C  CB  . LYS A 1 129 ? -18.283 0.054   3.422   1.00 23.17 ? 128  LYS A CB  1 
ATOM   928  C  CG  . LYS A 1 129 ? -17.270 -0.349  2.386   1.00 25.66 ? 128  LYS A CG  1 
ATOM   929  C  CD  . LYS A 1 129 ? -15.926 -0.641  2.990   1.00 28.58 ? 128  LYS A CD  1 
ATOM   930  C  CE  . LYS A 1 129 ? -14.821 -0.048  2.121   1.00 28.62 ? 128  LYS A CE  1 
ATOM   931  N  NZ  . LYS A 1 129 ? -13.673 -0.961  1.771   1.00 30.31 ? 128  LYS A NZ  1 
ATOM   932  N  N   . GLY A 1 130 ? -19.904 3.044   4.616   1.00 23.45 ? 129  GLY A N   1 
ATOM   933  C  CA  . GLY A 1 130 ? -21.233 3.633   4.688   1.00 22.64 ? 129  GLY A CA  1 
ATOM   934  C  C   . GLY A 1 130 ? -21.527 4.783   3.730   1.00 23.74 ? 129  GLY A C   1 
ATOM   935  O  O   . GLY A 1 130 ? -22.672 5.222   3.621   1.00 23.96 ? 129  GLY A O   1 
ATOM   936  N  N   . GLY A 1 131 ? -20.502 5.297   3.057   1.00 24.25 ? 130  GLY A N   1 
ATOM   937  C  CA  . GLY A 1 131 ? -20.709 6.312   2.048   1.00 24.81 ? 130  GLY A CA  1 
ATOM   938  C  C   . GLY A 1 131 ? -20.953 7.730   2.520   1.00 25.45 ? 130  GLY A C   1 
ATOM   939  O  O   . GLY A 1 131 ? -21.506 8.532   1.777   1.00 26.36 ? 130  GLY A O   1 
ATOM   940  N  N   . ASN A 1 132 ? -20.558 8.029   3.755   1.00 26.60 ? 131  ASN A N   1 
ATOM   941  C  CA  . ASN A 1 132 ? -20.647 9.393   4.295   1.00 26.83 ? 131  ASN A CA  1 
ATOM   942  C  C   . ASN A 1 132 ? -19.367 9.770   5.040   1.00 26.71 ? 131  ASN A C   1 
ATOM   943  O  O   . ASN A 1 132 ? -18.472 8.931   5.210   1.00 26.74 ? 131  ASN A O   1 
ATOM   944  C  CB  . ASN A 1 132 ? -21.929 9.632   5.126   1.00 26.63 ? 131  ASN A CB  1 
ATOM   945  C  CG  . ASN A 1 132 ? -22.186 8.553   6.183   1.00 28.54 ? 131  ASN A CG  1 
ATOM   946  O  OD1 . ASN A 1 132 ? -21.266 8.000   6.775   1.00 30.22 ? 131  ASN A OD1 1 
ATOM   947  N  ND2 . ASN A 1 132 ? -23.462 8.278   6.444   1.00 29.86 ? 131  ASN A ND2 1 
ATOM   948  N  N   . GLU A 1 133 ? -19.260 11.038  5.444   1.00 27.02 ? 132  GLU A N   1 
ATOM   949  C  CA  . GLU A 1 133 ? -18.066 11.548  6.137   1.00 26.03 ? 132  GLU A CA  1 
ATOM   950  C  C   . GLU A 1 133 ? -17.891 10.829  7.463   1.00 25.58 ? 132  GLU A C   1 
ATOM   951  O  O   . GLU A 1 133 ? -16.796 10.370  7.806   1.00 26.11 ? 132  GLU A O   1 
ATOM   952  C  CB  . GLU A 1 133 ? -18.161 13.105  6.271   1.00 25.42 ? 132  GLU A CB  1 
ATOM   953  N  N   . GLU A 1 134 ? -18.991 10.661  8.189   1.00 25.30 ? 133  GLU A N   1 
ATOM   954  C  CA  . GLU A 1 134 ? -18.954 10.027  9.487   1.00 25.80 ? 133  GLU A CA  1 
ATOM   955  C  C   . GLU A 1 134 ? -18.490 8.557   9.418   1.00 24.77 ? 133  GLU A C   1 
ATOM   956  O  O   . GLU A 1 134 ? -17.917 8.053   10.373  1.00 26.05 ? 133  GLU A O   1 
ATOM   957  C  CB  . GLU A 1 134 ? -20.337 10.115  10.150  1.00 24.89 ? 133  GLU A CB  1 
ATOM   958  C  CG  . GLU A 1 134 ? -20.379 9.630   11.578  1.00 28.56 ? 133  GLU A CG  1 
ATOM   959  C  CD  . GLU A 1 134 ? -19.476 10.439  12.481  1.00 29.73 ? 133  GLU A CD  1 
ATOM   960  O  OE1 . GLU A 1 134 ? -19.500 11.687  12.412  1.00 31.95 ? 133  GLU A OE1 1 
ATOM   961  O  OE2 . GLU A 1 134 ? -18.733 9.821   13.247  1.00 33.98 ? 133  GLU A OE2 1 
ATOM   962  N  N   . SER A 1 135 ? -18.736 7.898   8.294   1.00 25.00 ? 134  SER A N   1 
ATOM   963  C  CA  . SER A 1 135 ? -18.366 6.487   8.105   1.00 24.55 ? 134  SER A CA  1 
ATOM   964  C  C   . SER A 1 135 ? -16.862 6.300   8.211   1.00 24.75 ? 134  SER A C   1 
ATOM   965  O  O   . SER A 1 135 ? -16.373 5.288   8.727   1.00 24.92 ? 134  SER A O   1 
ATOM   966  C  CB  . SER A 1 135 ? -18.882 5.981   6.742   1.00 23.90 ? 134  SER A CB  1 
ATOM   967  O  OG  . SER A 1 135 ? -18.428 4.670   6.395   1.00 25.01 ? 134  SER A OG  1 
ATOM   968  N  N   . THR A 1 136 ? -16.139 7.324   7.783   1.00 24.81 ? 135  THR A N   1 
ATOM   969  C  CA  . THR A 1 136 ? -14.683 7.312   7.725   1.00 25.55 ? 135  THR A CA  1 
ATOM   970  C  C   . THR A 1 136 ? -13.990 7.777   9.031   1.00 25.81 ? 135  THR A C   1 
ATOM   971  O  O   . THR A 1 136 ? -12.748 7.860   9.116   1.00 25.93 ? 135  THR A O   1 
ATOM   972  C  CB  . THR A 1 136 ? -14.270 8.121   6.493   1.00 24.95 ? 135  THR A CB  1 
ATOM   973  O  OG1 . THR A 1 136 ? -13.209 7.455   5.813   1.00 28.41 ? 135  THR A OG1 1 
ATOM   974  C  CG2 . THR A 1 136 ? -13.712 9.480   6.847   1.00 24.90 ? 135  THR A CG2 1 
ATOM   975  N  N   . LYS A 1 137 ? -14.822 8.068   10.029  1.00 27.33 ? 136  LYS A N   1 
ATOM   976  C  CA  . LYS A 1 137 ? -14.403 8.451   11.372  1.00 28.18 ? 136  LYS A CA  1 
ATOM   977  C  C   . LYS A 1 137 ? -14.782 7.387   12.410  1.00 28.97 ? 136  LYS A C   1 
ATOM   978  O  O   . LYS A 1 137 ? -13.921 6.935   13.161  1.00 29.88 ? 136  LYS A O   1 
ATOM   979  C  CB  . LYS A 1 137 ? -14.998 9.798   11.789  1.00 28.63 ? 136  LYS A CB  1 
ATOM   980  C  CG  . LYS A 1 137 ? -14.799 10.924  10.783  1.00 28.74 ? 136  LYS A CG  1 
ATOM   981  C  CD  . LYS A 1 137 ? -15.844 11.983  11.066  1.00 29.00 ? 136  LYS A CD  1 
ATOM   982  C  CE  . LYS A 1 137 ? -15.535 13.385  10.514  1.00 27.57 ? 136  LYS A CE  1 
ATOM   983  N  N   . THR A 1 138 ? -16.049 6.975   12.464  1.00 29.81 ? 137  THR A N   1 
ATOM   984  C  CA  . THR A 1 138 ? -16.474 6.036   13.488  1.00 29.51 ? 137  THR A CA  1 
ATOM   985  C  C   . THR A 1 138 ? -17.220 4.814   12.981  1.00 29.23 ? 137  THR A C   1 
ATOM   986  O  O   . THR A 1 138 ? -17.542 3.916   13.764  1.00 30.17 ? 137  THR A O   1 
ATOM   987  C  CB  . THR A 1 138 ? -17.376 6.767   14.498  1.00 30.21 ? 137  THR A CB  1 
ATOM   988  O  OG1 . THR A 1 138 ? -18.608 7.150   13.854  1.00 31.21 ? 137  THR A OG1 1 
ATOM   989  C  CG2 . THR A 1 138 ? -16.740 8.127   14.884  1.00 29.75 ? 137  THR A CG2 1 
ATOM   990  N  N   . GLY A 1 139 ? -17.528 4.792   11.687  1.00 27.33 ? 138  GLY A N   1 
ATOM   991  C  CA  . GLY A 1 139 ? -18.291 3.706   11.101  1.00 25.69 ? 138  GLY A CA  1 
ATOM   992  C  C   . GLY A 1 139 ? -19.779 3.750   11.415  1.00 25.13 ? 138  GLY A C   1 
ATOM   993  O  O   . GLY A 1 139 ? -20.502 2.755   11.253  1.00 24.97 ? 138  GLY A O   1 
ATOM   994  N  N   . ASN A 1 140 ? -20.220 4.913   11.870  1.00 24.84 ? 139  ASN A N   1 
ATOM   995  C  CA  . ASN A 1 140 ? -21.592 5.142   12.264  1.00 24.56 ? 139  ASN A CA  1 
ATOM   996  C  C   . ASN A 1 140 ? -22.121 4.134   13.283  1.00 23.86 ? 139  ASN A C   1 
ATOM   997  O  O   . ASN A 1 140 ? -23.280 3.733   13.213  1.00 25.38 ? 139  ASN A O   1 
ATOM   998  C  CB  . ASN A 1 140 ? -22.499 5.192   11.032  1.00 24.91 ? 139  ASN A CB  1 
ATOM   999  C  CG  . ASN A 1 140 ? -22.304 6.441   10.199  1.00 24.93 ? 139  ASN A CG  1 
ATOM   1000 O  OD1 . ASN A 1 140 ? -22.865 7.499   10.499  1.00 29.90 ? 139  ASN A OD1 1 
ATOM   1001 N  ND2 . ASN A 1 140 ? -21.555 6.316   9.120   1.00 22.98 ? 139  ASN A ND2 1 
ATOM   1002 N  N   . ALA A 1 141 ? -21.283 3.735   14.229  1.00 24.33 ? 140  ALA A N   1 
ATOM   1003 C  CA  . ALA A 1 141 ? -21.691 2.765   15.238  1.00 23.82 ? 140  ALA A CA  1 
ATOM   1004 C  C   . ALA A 1 141 ? -22.601 3.392   16.324  1.00 23.25 ? 140  ALA A C   1 
ATOM   1005 O  O   . ALA A 1 141 ? -23.182 2.710   17.166  1.00 23.61 ? 140  ALA A O   1 
ATOM   1006 C  CB  . ALA A 1 141 ? -20.468 2.089   15.850  1.00 24.13 ? 140  ALA A CB  1 
ATOM   1007 N  N   . GLY A 1 142 ? -22.740 4.713   16.265  1.00 24.41 ? 141  GLY A N   1 
ATOM   1008 C  CA  . GLY A 1 142 ? -23.593 5.430   17.183  1.00 24.22 ? 141  GLY A CA  1 
ATOM   1009 C  C   . GLY A 1 142 ? -23.172 5.397   18.637  1.00 24.12 ? 141  GLY A C   1 
ATOM   1010 O  O   . GLY A 1 142 ? -21.982 5.421   18.953  1.00 24.91 ? 141  GLY A O   1 
ATOM   1011 N  N   . SER A 1 143 ? -24.176 5.347   19.506  1.00 24.89 ? 142  SER A N   1 
ATOM   1012 C  CA  . SER A 1 143 ? -24.043 5.342   20.970  1.00 25.64 ? 142  SER A CA  1 
ATOM   1013 C  C   . SER A 1 143 ? -23.083 4.368   21.648  1.00 24.62 ? 142  SER A C   1 
ATOM   1014 O  O   . SER A 1 143 ? -22.881 3.219   21.227  1.00 26.44 ? 142  SER A O   1 
ATOM   1015 C  CB  . SER A 1 143 ? -25.405 5.070   21.592  1.00 24.93 ? 142  SER A CB  1 
ATOM   1016 O  OG  . SER A 1 143 ? -25.791 6.218   22.237  1.00 30.44 ? 142  SER A OG  1 
ATOM   1017 N  N   . ARG A 1 144 ? -22.562 4.811   22.764  1.00 25.02 ? 143  ARG A N   1 
ATOM   1018 C  CA  . ARG A 1 144 ? -21.743 3.929   23.567  1.00 23.16 ? 143  ARG A CA  1 
ATOM   1019 C  C   . ARG A 1 144 ? -22.654 3.176   24.537  1.00 22.95 ? 143  ARG A C   1 
ATOM   1020 O  O   . ARG A 1 144 ? -23.087 3.717   25.547  1.00 24.71 ? 143  ARG A O   1 
ATOM   1021 C  CB  . ARG A 1 144 ? -20.669 4.741   24.283  1.00 22.53 ? 143  ARG A CB  1 
ATOM   1022 C  CG  . ARG A 1 144 ? -20.047 5.805   23.379  1.00 21.03 ? 143  ARG A CG  1 
ATOM   1023 C  CD  . ARG A 1 144 ? -18.758 6.422   23.889  1.00 15.21 ? 143  ARG A CD  1 
ATOM   1024 N  NE  . ARG A 1 144 ? -18.108 7.160   22.820  1.00 20.53 ? 143  ARG A NE  1 
ATOM   1025 C  CZ  . ARG A 1 144 ? -16.913 7.742   22.870  1.00 16.23 ? 143  ARG A CZ  1 
ATOM   1026 N  NH1 . ARG A 1 144 ? -16.133 7.678   23.967  1.00 20.84 ? 143  ARG A NH1 1 
ATOM   1027 N  NH2 . ARG A 1 144 ? -16.475 8.413   21.778  1.00 20.24 ? 143  ARG A NH2 1 
ATOM   1028 N  N   . LEU A 1 145 ? -22.913 1.892   24.291  1.00 24.39 ? 144  LEU A N   1 
ATOM   1029 C  CA  . LEU A 1 145 ? -23.802 1.188   25.191  1.00 23.11 ? 144  LEU A CA  1 
ATOM   1030 C  C   . LEU A 1 145 ? -23.196 0.822   26.542  1.00 22.50 ? 144  LEU A C   1 
ATOM   1031 O  O   . LEU A 1 145 ? -23.880 0.994   27.570  1.00 24.25 ? 144  LEU A O   1 
ATOM   1032 C  CB  . LEU A 1 145 ? -24.406 -0.052  24.551  1.00 23.18 ? 144  LEU A CB  1 
ATOM   1033 C  CG  . LEU A 1 145 ? -25.213 0.160   23.268  1.00 22.21 ? 144  LEU A CG  1 
ATOM   1034 C  CD1 . LEU A 1 145 ? -25.803 -1.156  22.826  1.00 21.28 ? 144  LEU A CD1 1 
ATOM   1035 C  CD2 . LEU A 1 145 ? -26.311 1.191   23.411  1.00 23.40 ? 144  LEU A CD2 1 
ATOM   1036 N  N   . ALA A 1 146 ? -21.953 0.329   26.517  1.00 21.83 ? 145  ALA A N   1 
ATOM   1037 C  CA  . ALA A 1 146 ? -21.187 -0.092  27.670  1.00 19.62 ? 145  ALA A CA  1 
ATOM   1038 C  C   . ALA A 1 146 ? -19.704 0.016   27.322  1.00 18.82 ? 145  ALA A C   1 
ATOM   1039 O  O   . ALA A 1 146 ? -19.326 -0.126  26.137  1.00 21.81 ? 145  ALA A O   1 
ATOM   1040 C  CB  . ALA A 1 146 ? -21.550 -1.600  28.089  1.00 15.14 ? 145  ALA A CB  1 
ATOM   1041 N  N   . CYS A 1 147 ? -18.883 0.232   28.355  1.00 20.62 ? 146  CYS A N   1 
ATOM   1042 C  CA  . CYS A 1 147 ? -17.429 0.275   28.355  1.00 20.81 ? 146  CYS A CA  1 
ATOM   1043 C  C   . CYS A 1 147 ? -16.807 -0.221  29.638  1.00 20.33 ? 146  CYS A C   1 
ATOM   1044 O  O   . CYS A 1 147 ? -17.460 -0.312  30.678  1.00 21.96 ? 146  CYS A O   1 
ATOM   1045 C  CB  . CYS A 1 147 ? -16.934 1.718   28.133  1.00 17.02 ? 146  CYS A CB  1 
ATOM   1046 S  SG  . CYS A 1 147 ? -17.683 2.843   29.327  1.00 27.22 ? 146  CYS A SG  1 
ATOM   1047 N  N   . GLY A 1 148 ? -15.489 -0.436  29.558  1.00 21.57 ? 147  GLY A N   1 
ATOM   1048 C  CA  . GLY A 1 148 ? -14.621 -0.779  30.675  1.00 19.43 ? 147  GLY A CA  1 
ATOM   1049 C  C   . GLY A 1 148 ? -13.178 -0.474  30.291  1.00 18.61 ? 147  GLY A C   1 
ATOM   1050 O  O   . GLY A 1 148 ? -12.790 -0.533  29.109  1.00 21.75 ? 147  GLY A O   1 
ATOM   1051 N  N   . VAL A 1 149 ? -12.359 -0.207  31.297  1.00 20.19 ? 148  VAL A N   1 
ATOM   1052 C  CA  . VAL A 1 149 ? -10.934 0.020   31.139  1.00 18.86 ? 148  VAL A CA  1 
ATOM   1053 C  C   . VAL A 1 149 ? -10.360 -1.383  31.023  1.00 17.49 ? 148  VAL A C   1 
ATOM   1054 O  O   . VAL A 1 149 ? -10.781 -2.286  31.755  1.00 23.61 ? 148  VAL A O   1 
ATOM   1055 C  CB  . VAL A 1 149 ? -10.366 0.764   32.366  1.00 16.96 ? 148  VAL A CB  1 
ATOM   1056 C  CG1 . VAL A 1 149 ? -8.862  0.919   32.315  1.00 15.72 ? 148  VAL A CG1 1 
ATOM   1057 C  CG2 . VAL A 1 149 ? -11.056 2.196   32.499  1.00 19.66 ? 148  VAL A CG2 1 
ATOM   1058 N  N   . ILE A 1 150 ? -9.479  -1.541  30.075  1.00 19.92 ? 149  ILE A N   1 
ATOM   1059 C  CA  . ILE A 1 150 ? -8.738  -2.761  29.868  1.00 19.16 ? 149  ILE A CA  1 
ATOM   1060 C  C   . ILE A 1 150 ? -7.630  -2.810  30.946  1.00 18.75 ? 149  ILE A C   1 
ATOM   1061 O  O   . ILE A 1 150 ? -6.680  -1.986  30.957  1.00 24.89 ? 149  ILE A O   1 
ATOM   1062 C  CB  . ILE A 1 150 ? -8.199  -2.820  28.466  1.00 16.87 ? 149  ILE A CB  1 
ATOM   1063 C  CG1 . ILE A 1 150 ? -9.310  -2.609  27.399  1.00 17.70 ? 149  ILE A CG1 1 
ATOM   1064 C  CG2 . ILE A 1 150 ? -7.472  -4.203  28.255  1.00 17.55 ? 149  ILE A CG2 1 
ATOM   1065 C  CD1 . ILE A 1 150 ? -8.747  -2.498  26.064  1.00 17.18 ? 149  ILE A CD1 1 
ATOM   1066 N  N   . GLY A 1 151 ? -7.711  -3.790  31.844  1.00 19.61 ? 150  GLY A N   1 
ATOM   1067 C  CA  . GLY A 1 151 ? -6.803  -3.912  32.967  1.00 18.48 ? 150  GLY A CA  1 
ATOM   1068 C  C   . GLY A 1 151 ? -5.978  -5.164  32.851  1.00 19.57 ? 150  GLY A C   1 
ATOM   1069 O  O   . GLY A 1 151 ? -6.367  -6.088  32.144  1.00 22.56 ? 150  GLY A O   1 
ATOM   1070 N  N   . ILE A 1 152 ? -4.844  -5.181  33.537  1.00 21.97 ? 151  ILE A N   1 
ATOM   1071 C  CA  . ILE A 1 152 ? -3.942  -6.326  33.544  1.00 20.88 ? 151  ILE A CA  1 
ATOM   1072 C  C   . ILE A 1 152 ? -4.599  -7.506  34.251  1.00 21.44 ? 151  ILE A C   1 
ATOM   1073 O  O   . ILE A 1 152 ? -5.227  -7.362  35.291  1.00 21.94 ? 151  ILE A O   1 
ATOM   1074 C  CB  . ILE A 1 152 ? -2.632  -5.942  34.218  1.00 20.76 ? 151  ILE A CB  1 
ATOM   1075 C  CG1 . ILE A 1 152 ? -1.936  -4.800  33.421  1.00 17.40 ? 151  ILE A CG1 1 
ATOM   1076 C  CG2 . ILE A 1 152 ? -1.747  -7.147  34.367  1.00 22.59 ? 151  ILE A CG2 1 
ATOM   1077 C  CD1 . ILE A 1 152 ? -0.700  -4.283  34.074  1.00 20.39 ? 151  ILE A CD1 1 
ATOM   1078 N  N   . ALA A 1 153 ? -4.435  -8.692  33.696  1.00 23.54 ? 152  ALA A N   1 
ATOM   1079 C  CA  . ALA A 1 153 ? -5.116  -9.830  34.264  1.00 24.10 ? 152  ALA A CA  1 
ATOM   1080 C  C   . ALA A 1 153 ? -4.170  -10.985 34.580  1.00 25.34 ? 152  ALA A C   1 
ATOM   1081 O  O   . ALA A 1 153 ? -3.059  -11.057 34.036  1.00 26.94 ? 152  ALA A O   1 
ATOM   1082 C  CB  . ALA A 1 153 ? -6.248  -10.252 33.332  1.00 22.00 ? 152  ALA A CB  1 
ATOM   1083 N  N   . GLN A 1 154 ? -4.593  -11.852 35.495  1.00 26.91 ? 153  GLN A N   1 
ATOM   1084 C  CA  . GLN A 1 154 ? -3.774  -12.975 35.940  1.00 28.35 ? 153  GLN A CA  1 
ATOM   1085 C  C   . GLN A 1 154 ? -3.581  -13.990 34.827  1.00 28.80 ? 153  GLN A C   1 
ATOM   1086 O  O   . GLN A 1 154 ? -4.522  -14.333 34.096  1.00 29.43 ? 153  GLN A O   1 
ATOM   1087 C  CB  . GLN A 1 154 ? -4.339  -13.631 37.206  1.00 28.05 ? 153  GLN A CB  1 
ATOM   1088 C  CG  . GLN A 1 154 ? -3.599  -14.906 37.648  1.00 29.82 ? 153  GLN A CG  1 
ATOM   1089 C  CD  . GLN A 1 154 ? -3.527  -15.075 39.166  1.00 33.20 ? 153  GLN A CD  1 
ATOM   1090 O  OE1 . GLN A 1 154 ? -4.514  -14.831 39.876  1.00 34.86 ? 153  GLN A OE1 1 
ATOM   1091 N  NE2 . GLN A 1 154 ? -2.363  -15.516 39.666  1.00 35.30 ? 153  GLN A NE2 1 
ATOM   1092 O  OXT . GLN A 1 154 ? -2.439  -14.419 34.702  1.00 29.96 ? 153  GLN A OXT 1 
HETATM 1093 C  C   . ACE B 1 1   ? 3.697   7.802   28.771  1.00 35.14 ? 0    ACE B C   1 
HETATM 1094 O  O   . ACE B 1 1   ? 3.805   8.966   28.388  1.00 36.16 ? 0    ACE B O   1 
HETATM 1095 C  CH3 . ACE B 1 1   ? 4.728   6.756   28.437  1.00 35.32 ? 0    ACE B CH3 1 
ATOM   1096 N  N   . ALA B 1 2   ? 2.525   7.345   29.216  1.00 34.91 ? 1    ALA B N   1 
ATOM   1097 C  CA  . ALA B 1 2   ? 1.534   8.259   29.781  1.00 33.06 ? 1    ALA B CA  1 
ATOM   1098 C  C   . ALA B 1 2   ? 2.055   9.134   30.943  1.00 31.32 ? 1    ALA B C   1 
ATOM   1099 O  O   . ALA B 1 2   ? 2.860   8.691   31.759  1.00 32.36 ? 1    ALA B O   1 
ATOM   1100 C  CB  . ALA B 1 2   ? 0.347   7.482   30.217  1.00 33.12 ? 1    ALA B CB  1 
ATOM   1101 N  N   . THR B 1 3   ? 1.593   10.382  31.016  1.00 28.79 ? 2    THR B N   1 
ATOM   1102 C  CA  . THR B 1 3   ? 1.948   11.265  32.113  1.00 26.70 ? 2    THR B CA  1 
ATOM   1103 C  C   . THR B 1 3   ? 0.727   11.493  33.006  1.00 24.34 ? 2    THR B C   1 
ATOM   1104 O  O   . THR B 1 3   ? 0.853   11.943  34.147  1.00 24.50 ? 2    THR B O   1 
ATOM   1105 C  CB  . THR B 1 3   ? 2.456   12.622  31.585  1.00 24.67 ? 2    THR B CB  1 
ATOM   1106 O  OG1 . THR B 1 3   ? 1.507   13.129  30.643  1.00 29.36 ? 2    THR B OG1 1 
ATOM   1107 C  CG2 . THR B 1 3   ? 3.701   12.451  30.736  1.00 27.64 ? 2    THR B CG2 1 
ATOM   1108 N  N   . LYS B 1 4   ? -0.457  11.200  32.483  1.00 23.24 ? 3    LYS B N   1 
ATOM   1109 C  CA  . LYS B 1 4   ? -1.707  11.294  33.269  1.00 22.41 ? 3    LYS B CA  1 
ATOM   1110 C  C   . LYS B 1 4   ? -2.551  10.022  33.317  1.00 21.06 ? 3    LYS B C   1 
ATOM   1111 O  O   . LYS B 1 4   ? -2.706  9.302   32.313  1.00 22.97 ? 3    LYS B O   1 
ATOM   1112 C  CB  . LYS B 1 4   ? -2.631  12.393  32.766  1.00 21.46 ? 3    LYS B CB  1 
ATOM   1113 C  CG  . LYS B 1 4   ? -2.134  13.813  32.898  1.00 23.48 ? 3    LYS B CG  1 
ATOM   1114 C  CD  . LYS B 1 4   ? -3.297  14.874  32.849  1.00 23.62 ? 3    LYS B CD  1 
ATOM   1115 C  CE  . LYS B 1 4   ? -4.005  15.086  34.228  1.00 26.91 ? 3    LYS B CE  1 
ATOM   1116 N  NZ  . LYS B 1 4   ? -5.435  15.624  34.136  1.00 32.46 ? 3    LYS B NZ  1 
ATOM   1117 N  N   . ALA B 1 5   ? -3.138  9.792   34.479  1.00 21.83 ? 4    ALA B N   1 
ATOM   1118 C  CA  . ALA B 1 5   ? -4.018  8.667   34.681  1.00 22.03 ? 4    ALA B CA  1 
ATOM   1119 C  C   . ALA B 1 5   ? -5.184  9.091   35.577  1.00 21.67 ? 4    ALA B C   1 
ATOM   1120 O  O   . ALA B 1 5   ? -5.110  10.102  36.280  1.00 23.75 ? 4    ALA B O   1 
ATOM   1121 C  CB  . ALA B 1 5   ? -3.226  7.467   35.297  1.00 19.24 ? 4    ALA B CB  1 
ATOM   1122 N  N   . VAL B 1 6   ? -6.248  8.293   35.556  1.00 22.68 ? 5    VAL B N   1 
ATOM   1123 C  CA  . VAL B 1 6   ? -7.398  8.503   36.387  1.00 22.02 ? 5    VAL B CA  1 
ATOM   1124 C  C   . VAL B 1 6   ? -8.061  7.163   36.793  1.00 22.37 ? 5    VAL B C   1 
ATOM   1125 O  O   . VAL B 1 6   ? -7.990  6.186   36.053  1.00 25.29 ? 5    VAL B O   1 
ATOM   1126 C  CB  . VAL B 1 6   ? -8.401  9.464   35.716  1.00 19.95 ? 5    VAL B CB  1 
ATOM   1127 C  CG1 . VAL B 1 6   ? -9.152  8.794   34.510  1.00 19.30 ? 5    VAL B CG1 1 
ATOM   1128 C  CG2 . VAL B 1 6   ? -9.391  10.040  36.759  1.00 20.62 ? 5    VAL B CG2 1 
ATOM   1129 N  N   . CYS B 1 7   ? -8.674  7.143   37.964  1.00 22.61 ? 6    CYS B N   1 
ATOM   1130 C  CA  . CYS B 1 7   ? -9.397  5.991   38.482  1.00 22.23 ? 6    CYS B CA  1 
ATOM   1131 C  C   . CYS B 1 7   ? -10.732 6.448   39.081  1.00 21.23 ? 6    CYS B C   1 
ATOM   1132 O  O   . CYS B 1 7   ? -10.804 7.361   39.929  1.00 23.75 ? 6    CYS B O   1 
ATOM   1133 C  CB  . CYS B 1 7   ? -8.572  5.227   39.531  1.00 20.25 ? 6    CYS B CB  1 
ATOM   1134 S  SG  . CYS B 1 7   ? -9.281  3.611   40.031  1.00 25.06 ? 6    CYS B SG  1 
ATOM   1135 N  N   . VAL B 1 8   ? -11.777 5.798   38.617  1.00 22.44 ? 7    VAL B N   1 
ATOM   1136 C  CA  . VAL B 1 8   ? -13.121 5.932   39.135  1.00 21.33 ? 7    VAL B CA  1 
ATOM   1137 C  C   . VAL B 1 8   ? -13.323 4.813   40.166  1.00 21.31 ? 7    VAL B C   1 
ATOM   1138 O  O   . VAL B 1 8   ? -13.181 3.623   39.864  1.00 22.86 ? 7    VAL B O   1 
ATOM   1139 C  CB  . VAL B 1 8   ? -14.139 5.855   38.000  1.00 18.92 ? 7    VAL B CB  1 
ATOM   1140 C  CG1 . VAL B 1 8   ? -15.555 5.643   38.522  1.00 20.79 ? 7    VAL B CG1 1 
ATOM   1141 C  CG2 . VAL B 1 8   ? -14.048 7.153   37.031  1.00 18.71 ? 7    VAL B CG2 1 
ATOM   1142 N  N   . LEU B 1 9   ? -13.559 5.198   41.405  1.00 21.25 ? 8    LEU B N   1 
ATOM   1143 C  CA  . LEU B 1 9   ? -13.777 4.217   42.464  1.00 20.84 ? 8    LEU B CA  1 
ATOM   1144 C  C   . LEU B 1 9   ? -15.249 3.924   42.730  1.00 20.76 ? 8    LEU B C   1 
ATOM   1145 O  O   . LEU B 1 9   ? -16.019 4.828   43.109  1.00 21.28 ? 8    LEU B O   1 
ATOM   1146 C  CB  . LEU B 1 9   ? -13.088 4.696   43.740  1.00 20.70 ? 8    LEU B CB  1 
ATOM   1147 C  CG  . LEU B 1 9   ? -11.719 4.240   44.284  1.00 21.70 ? 8    LEU B CG  1 
ATOM   1148 C  CD1 . LEU B 1 9   ? -10.741 3.767   43.293  1.00 16.90 ? 8    LEU B CD1 1 
ATOM   1149 C  CD2 . LEU B 1 9   ? -11.062 5.356   45.032  1.00 23.05 ? 8    LEU B CD2 1 
ATOM   1150 N  N   . LYS B 1 10  ? -15.645 2.655   42.593  1.00 20.20 ? 9    LYS B N   1 
ATOM   1151 C  CA  . LYS B 1 10  ? -16.989 2.225   42.947  1.00 21.46 ? 9    LYS B CA  1 
ATOM   1152 C  C   . LYS B 1 10  ? -16.977 0.838   43.613  1.00 21.70 ? 9    LYS B C   1 
ATOM   1153 O  O   . LYS B 1 10  ? -16.068 0.020   43.347  1.00 23.25 ? 9    LYS B O   1 
ATOM   1154 C  CB  . LYS B 1 10  ? -17.861 2.090   41.700  1.00 18.70 ? 9    LYS B CB  1 
ATOM   1155 C  CG  . LYS B 1 10  ? -18.176 3.316   40.866  1.00 21.53 ? 9    LYS B CG  1 
ATOM   1156 N  N   . GLY B 1 11  ? -18.004 0.599   44.418  1.00 24.83 ? 10   GLY B N   1 
ATOM   1157 C  CA  . GLY B 1 11  ? -18.220 -0.659  45.114  1.00 26.47 ? 10   GLY B CA  1 
ATOM   1158 C  C   . GLY B 1 11  ? -19.678 -1.031  45.340  1.00 27.20 ? 10   GLY B C   1 
ATOM   1159 O  O   . GLY B 1 11  ? -20.621 -0.426  44.787  1.00 28.29 ? 10   GLY B O   1 
ATOM   1160 N  N   . ASP B 1 12  ? -19.871 -2.049  46.174  1.00 28.11 ? 11   ASP B N   1 
ATOM   1161 C  CA  . ASP B 1 12  ? -21.190 -2.598  46.479  1.00 28.08 ? 11   ASP B CA  1 
ATOM   1162 C  C   . ASP B 1 12  ? -22.105 -1.674  47.307  1.00 27.27 ? 11   ASP B C   1 
ATOM   1163 O  O   . ASP B 1 12  ? -23.331 -1.865  47.357  1.00 29.36 ? 11   ASP B O   1 
ATOM   1164 C  CB  . ASP B 1 12  ? -21.026 -3.954  47.184  1.00 28.82 ? 11   ASP B CB  1 
ATOM   1165 C  CG  . ASP B 1 12  ? -20.114 -3.877  48.414  1.00 30.61 ? 11   ASP B CG  1 
ATOM   1166 O  OD1 . ASP B 1 12  ? -19.097 -3.109  48.401  1.00 39.21 ? 11   ASP B OD1 1 
ATOM   1167 O  OD2 . ASP B 1 12  ? -20.322 -4.556  49.446  1.00 34.67 ? 11   ASP B OD2 1 
ATOM   1168 N  N   . GLY B 1 13  ? -21.499 -0.693  47.958  1.00 26.75 ? 12   GLY B N   1 
ATOM   1169 C  CA  . GLY B 1 13  ? -22.192 0.230   48.819  1.00 25.90 ? 12   GLY B CA  1 
ATOM   1170 C  C   . GLY B 1 13  ? -22.146 1.661   48.328  1.00 24.52 ? 12   GLY B C   1 
ATOM   1171 O  O   . GLY B 1 13  ? -22.144 1.927   47.130  1.00 26.44 ? 12   GLY B O   1 
ATOM   1172 N  N   . PRO B 1 14  ? -22.082 2.591   49.264  1.00 24.27 ? 13   PRO B N   1 
ATOM   1173 C  CA  . PRO B 1 14  ? -22.088 4.021   48.942  1.00 23.94 ? 13   PRO B CA  1 
ATOM   1174 C  C   . PRO B 1 14  ? -20.695 4.634   48.634  1.00 23.98 ? 13   PRO B C   1 
ATOM   1175 O  O   . PRO B 1 14  ? -20.658 5.813   48.271  1.00 25.83 ? 13   PRO B O   1 
ATOM   1176 C  CB  . PRO B 1 14  ? -22.663 4.636   50.223  1.00 23.79 ? 13   PRO B CB  1 
ATOM   1177 C  CG  . PRO B 1 14  ? -22.171 3.763   51.319  1.00 22.37 ? 13   PRO B CG  1 
ATOM   1178 C  CD  . PRO B 1 14  ? -21.949 2.355   50.702  1.00 23.97 ? 13   PRO B CD  1 
ATOM   1179 N  N   . VAL B 1 15  ? -19.595 3.893   48.756  1.00 23.52 ? 14   VAL B N   1 
ATOM   1180 C  CA  . VAL B 1 15  ? -18.248 4.497   48.590  1.00 23.75 ? 14   VAL B CA  1 
ATOM   1181 C  C   . VAL B 1 15  ? -17.964 4.818   47.149  1.00 24.22 ? 14   VAL B C   1 
ATOM   1182 O  O   . VAL B 1 15  ? -17.979 3.950   46.297  1.00 27.27 ? 14   VAL B O   1 
ATOM   1183 C  CB  . VAL B 1 15  ? -17.070 3.640   49.223  1.00 21.64 ? 14   VAL B CB  1 
ATOM   1184 C  CG1 . VAL B 1 15  ? -15.647 4.175   48.811  1.00 18.51 ? 14   VAL B CG1 1 
ATOM   1185 C  CG2 . VAL B 1 15  ? -17.183 3.545   50.726  1.00 24.07 ? 14   VAL B CG2 1 
ATOM   1186 N  N   . GLN B 1 16  ? -17.722 6.080   46.840  1.00 24.37 ? 15   GLN B N   1 
ATOM   1187 C  CA  . GLN B 1 16  ? -17.405 6.424   45.475  1.00 25.05 ? 15   GLN B CA  1 
ATOM   1188 C  C   . GLN B 1 16  ? -16.416 7.567   45.435  1.00 24.92 ? 15   GLN B C   1 
ATOM   1189 O  O   . GLN B 1 16  ? -16.357 8.365   46.384  1.00 25.75 ? 15   GLN B O   1 
ATOM   1190 C  CB  . GLN B 1 16  ? -18.653 6.751   44.660  1.00 24.71 ? 15   GLN B CB  1 
ATOM   1191 C  CG  . GLN B 1 16  ? -19.440 7.983   45.136  1.00 27.80 ? 15   GLN B CG  1 
ATOM   1192 C  CD  . GLN B 1 16  ? -20.811 8.116   44.466  1.00 32.86 ? 15   GLN B CD  1 
ATOM   1193 O  OE1 . GLN B 1 16  ? -20.937 7.933   43.247  1.00 35.96 ? 15   GLN B OE1 1 
ATOM   1194 N  NE2 . GLN B 1 16  ? -21.838 8.424   45.260  1.00 34.68 ? 15   GLN B NE2 1 
ATOM   1195 N  N   . GLY B 1 17  ? -15.644 7.610   44.344  1.00 25.13 ? 16   GLY B N   1 
ATOM   1196 C  CA  . GLY B 1 17  ? -14.694 8.675   44.107  1.00 25.50 ? 16   GLY B CA  1 
ATOM   1197 C  C   . GLY B 1 17  ? -13.880 8.635   42.822  1.00 25.01 ? 16   GLY B C   1 
ATOM   1198 O  O   . GLY B 1 17  ? -13.855 7.657   42.059  1.00 25.81 ? 16   GLY B O   1 
ATOM   1199 N  N   . ILE B 1 18  ? -13.202 9.751   42.585  1.00 25.31 ? 17   ILE B N   1 
ATOM   1200 C  CA  . ILE B 1 18  ? -12.358 9.958   41.426  1.00 24.25 ? 17   ILE B CA  1 
ATOM   1201 C  C   . ILE B 1 18  ? -10.954 10.333  41.916  1.00 23.51 ? 17   ILE B C   1 
ATOM   1202 O  O   . ILE B 1 18  ? -10.760 11.328  42.660  1.00 24.77 ? 17   ILE B O   1 
ATOM   1203 C  CB  . ILE B 1 18  ? -12.950 11.074  40.532  1.00 23.48 ? 17   ILE B CB  1 
ATOM   1204 C  CG1 . ILE B 1 18  ? -14.271 10.613  39.891  1.00 23.26 ? 17   ILE B CG1 1 
ATOM   1205 C  CG2 . ILE B 1 18  ? -11.935 11.533  39.459  1.00 25.67 ? 17   ILE B CG2 1 
ATOM   1206 C  CD1 . ILE B 1 18  ? -15.083 11.737  39.268  1.00 22.60 ? 17   ILE B CD1 1 
ATOM   1207 N  N   . ILE B 1 19  ? -9.974  9.541   41.509  1.00 23.00 ? 18   ILE B N   1 
ATOM   1208 C  CA  . ILE B 1 19  ? -8.587  9.759   41.881  1.00 21.57 ? 18   ILE B CA  1 
ATOM   1209 C  C   . ILE B 1 19  ? -7.733  10.074  40.636  1.00 22.86 ? 18   ILE B C   1 
ATOM   1210 O  O   . ILE B 1 19  ? -7.703  9.315   39.654  1.00 24.89 ? 18   ILE B O   1 
ATOM   1211 C  CB  . ILE B 1 19  ? -8.037  8.502   42.630  1.00 20.80 ? 18   ILE B CB  1 
ATOM   1212 C  CG1 . ILE B 1 19  ? -8.794  8.219   43.945  1.00 20.38 ? 18   ILE B CG1 1 
ATOM   1213 C  CG2 . ILE B 1 19  ? -6.559  8.625   42.866  1.00 16.92 ? 18   ILE B CG2 1 
ATOM   1214 C  CD1 . ILE B 1 19  ? -9.024  9.497   44.844  1.00 22.02 ? 18   ILE B CD1 1 
ATOM   1215 N  N   . ASN B 1 20  ? -7.071  11.214  40.638  1.00 22.75 ? 19   ASN B N   1 
ATOM   1216 C  CA  . ASN B 1 20  ? -6.190  11.593  39.542  1.00 22.52 ? 19   ASN B CA  1 
ATOM   1217 C  C   . ASN B 1 20  ? -4.727  11.222  39.803  1.00 22.63 ? 19   ASN B C   1 
ATOM   1218 O  O   . ASN B 1 20  ? -4.298  11.098  40.955  1.00 25.40 ? 19   ASN B O   1 
ATOM   1219 C  CB  . ASN B 1 20  ? -6.276  13.102  39.271  1.00 20.97 ? 19   ASN B CB  1 
ATOM   1220 C  CG  . ASN B 1 20  ? -7.689  13.556  38.946  1.00 21.34 ? 19   ASN B CG  1 
ATOM   1221 O  OD1 . ASN B 1 20  ? -8.377  14.147  39.798  1.00 28.11 ? 19   ASN B OD1 1 
ATOM   1222 N  ND2 . ASN B 1 20  ? -8.144  13.260  37.741  1.00 25.93 ? 19   ASN B ND2 1 
ATOM   1223 N  N   . PHE B 1 21  ? -4.011  10.971  38.717  1.00 24.38 ? 20   PHE B N   1 
ATOM   1224 C  CA  . PHE B 1 21  ? -2.576  10.712  38.709  1.00 22.37 ? 20   PHE B CA  1 
ATOM   1225 C  C   . PHE B 1 21  ? -1.875  11.536  37.610  1.00 23.04 ? 20   PHE B C   1 
ATOM   1226 O  O   . PHE B 1 21  ? -2.311  11.617  36.428  1.00 22.42 ? 20   PHE B O   1 
ATOM   1227 C  CB  . PHE B 1 21  ? -2.216  9.213   38.499  1.00 23.36 ? 20   PHE B CB  1 
ATOM   1228 C  CG  . PHE B 1 21  ? -2.936  8.243   39.392  1.00 22.24 ? 20   PHE B CG  1 
ATOM   1229 C  CD1 . PHE B 1 21  ? -4.217  7.826   39.086  1.00 24.89 ? 20   PHE B CD1 1 
ATOM   1230 C  CD2 . PHE B 1 21  ? -2.322  7.727   40.538  1.00 20.86 ? 20   PHE B CD2 1 
ATOM   1231 C  CE1 . PHE B 1 21  ? -4.923  6.904   39.927  1.00 22.46 ? 20   PHE B CE1 1 
ATOM   1232 C  CE2 . PHE B 1 21  ? -2.999  6.813   41.408  1.00 18.99 ? 20   PHE B CE2 1 
ATOM   1233 C  CZ  . PHE B 1 21  ? -4.322  6.380   41.099  1.00 18.38 ? 20   PHE B CZ  1 
ATOM   1234 N  N   . GLU B 1 22  ? -0.743  12.127  38.016  1.00 23.86 ? 21   GLU B N   1 
ATOM   1235 C  CA  . GLU B 1 22  ? 0.139   12.901  37.150  1.00 23.86 ? 21   GLU B CA  1 
ATOM   1236 C  C   . GLU B 1 22  ? 1.614   12.707  37.471  1.00 22.77 ? 21   GLU B C   1 
ATOM   1237 O  O   . GLU B 1 22  ? 2.055   12.831  38.626  1.00 24.34 ? 21   GLU B O   1 
ATOM   1238 C  CB  . GLU B 1 22  ? -0.194  14.381  37.155  1.00 23.34 ? 21   GLU B CB  1 
ATOM   1239 C  CG  . GLU B 1 22  ? 0.735   15.162  36.257  1.00 26.44 ? 21   GLU B CG  1 
ATOM   1240 C  CD  . GLU B 1 22  ? 0.425   16.634  36.273  1.00 32.23 ? 21   GLU B CD  1 
ATOM   1241 O  OE1 . GLU B 1 22  ? 0.905   17.331  37.208  1.00 36.08 ? 21   GLU B OE1 1 
ATOM   1242 O  OE2 . GLU B 1 22  ? -0.300  17.081  35.350  1.00 34.77 ? 21   GLU B OE2 1 
ATOM   1243 N  N   . GLN B 1 23  ? 2.344   12.367  36.418  1.00 22.81 ? 22   GLN B N   1 
ATOM   1244 C  CA  . GLN B 1 23  ? 3.785   12.140  36.441  1.00 22.72 ? 22   GLN B CA  1 
ATOM   1245 C  C   . GLN B 1 23  ? 4.440   12.883  35.276  1.00 23.00 ? 22   GLN B C   1 
ATOM   1246 O  O   . GLN B 1 23  ? 4.497   12.404  34.146  1.00 23.57 ? 22   GLN B O   1 
ATOM   1247 C  CB  . GLN B 1 23  ? 4.102   10.632  36.411  1.00 22.64 ? 22   GLN B CB  1 
ATOM   1248 C  CG  . GLN B 1 23  ? 5.530   10.299  36.832  1.00 20.48 ? 22   GLN B CG  1 
ATOM   1249 C  CD  . GLN B 1 23  ? 5.815   8.803   36.678  1.00 18.15 ? 22   GLN B CD  1 
ATOM   1250 O  OE1 . GLN B 1 23  ? 5.072   8.137   36.000  1.00 23.03 ? 22   GLN B OE1 1 
ATOM   1251 N  NE2 . GLN B 1 23  ? 6.864   8.305   37.303  1.00 22.75 ? 22   GLN B NE2 1 
ATOM   1252 N  N   . LYS B 1 24  ? 4.884   14.103  35.558  1.00 23.68 ? 23   LYS B N   1 
ATOM   1253 C  CA  . LYS B 1 24  ? 5.584   14.915  34.599  1.00 24.21 ? 23   LYS B CA  1 
ATOM   1254 C  C   . LYS B 1 24  ? 6.896   14.302  34.097  1.00 23.03 ? 23   LYS B C   1 
ATOM   1255 O  O   . LYS B 1 24  ? 7.176   14.371  32.930  1.00 24.22 ? 23   LYS B O   1 
ATOM   1256 C  CB  . LYS B 1 24  ? 5.826   16.304  35.187  1.00 24.28 ? 23   LYS B CB  1 
ATOM   1257 C  CG  . LYS B 1 24  ? 4.527   17.015  35.579  1.00 27.42 ? 23   LYS B CG  1 
ATOM   1258 C  CD  . LYS B 1 24  ? 3.652   17.277  34.354  1.00 31.46 ? 23   LYS B CD  1 
ATOM   1259 C  CE  . LYS B 1 24  ? 2.727   18.520  34.559  1.00 35.68 ? 23   LYS B CE  1 
ATOM   1260 N  NZ  . LYS B 1 24  ? 1.901   18.891  33.350  1.00 37.29 ? 23   LYS B NZ  1 
ATOM   1261 N  N   . GLU B 1 25  ? 7.670   13.659  34.955  1.00 23.18 ? 24   GLU B N   1 
ATOM   1262 C  CA  . GLU B 1 25  ? 8.885   13.016  34.480  1.00 22.88 ? 24   GLU B CA  1 
ATOM   1263 C  C   . GLU B 1 25  ? 8.837   11.549  34.760  1.00 21.55 ? 24   GLU B C   1 
ATOM   1264 O  O   . GLU B 1 25  ? 8.357   11.134  35.803  1.00 22.10 ? 24   GLU B O   1 
ATOM   1265 C  CB  . GLU B 1 25  ? 10.130  13.602  35.106  1.00 22.95 ? 24   GLU B CB  1 
ATOM   1266 C  CG  . GLU B 1 25  ? 10.728  14.710  34.255  1.00 27.67 ? 24   GLU B CG  1 
ATOM   1267 C  CD  . GLU B 1 25  ? 9.956   15.980  34.471  1.00 32.23 ? 24   GLU B CD  1 
ATOM   1268 O  OE1 . GLU B 1 25  ? 9.704   16.267  35.661  1.00 34.58 ? 24   GLU B OE1 1 
ATOM   1269 O  OE2 . GLU B 1 25  ? 9.588   16.664  33.482  1.00 35.47 ? 24   GLU B OE2 1 
ATOM   1270 N  N   . SER B 1 26  ? 9.358   10.762  33.827  1.00 21.31 ? 25   SER B N   1 
ATOM   1271 C  CA  . SER B 1 26  ? 9.248   9.305   33.979  1.00 20.72 ? 25   SER B CA  1 
ATOM   1272 C  C   . SER B 1 26  ? 10.101  8.740   35.121  1.00 20.52 ? 25   SER B C   1 
ATOM   1273 O  O   . SER B 1 26  ? 9.848   7.636   35.624  1.00 22.85 ? 25   SER B O   1 
ATOM   1274 C  CB  . SER B 1 26  ? 9.499   8.589   32.661  1.00 18.88 ? 25   SER B CB  1 
ATOM   1275 O  OG  . SER B 1 26  ? 10.802  8.881   32.148  1.00 19.16 ? 25   SER B OG  1 
ATOM   1276 N  N   . ASN B 1 27  ? 11.051  9.526   35.575  1.00 21.33 ? 26   ASN B N   1 
ATOM   1277 C  CA  . ASN B 1 27  ? 11.840  9.139   36.735  1.00 21.02 ? 26   ASN B CA  1 
ATOM   1278 C  C   . ASN B 1 27  ? 11.569  10.055  37.914  1.00 20.94 ? 26   ASN B C   1 
ATOM   1279 O  O   . ASN B 1 27  ? 12.366  10.136  38.836  1.00 24.09 ? 26   ASN B O   1 
ATOM   1280 C  CB  . ASN B 1 27  ? 13.343  9.050   36.380  1.00 20.63 ? 26   ASN B CB  1 
ATOM   1281 C  CG  . ASN B 1 27  ? 14.022  10.434  36.138  1.00 20.33 ? 26   ASN B CG  1 
ATOM   1282 O  OD1 . ASN B 1 27  ? 13.415  11.387  35.669  1.00 24.57 ? 26   ASN B OD1 1 
ATOM   1283 N  ND2 . ASN B 1 27  ? 15.296  10.503  36.433  1.00 26.02 ? 26   ASN B ND2 1 
ATOM   1284 N  N   . GLY B 1 28  ? 10.508  10.837  37.830  1.00 21.30 ? 27   GLY B N   1 
ATOM   1285 C  CA  . GLY B 1 28  ? 10.080  11.673  38.945  1.00 21.40 ? 27   GLY B CA  1 
ATOM   1286 C  C   . GLY B 1 28  ? 8.880   11.109  39.710  1.00 21.10 ? 27   GLY B C   1 
ATOM   1287 O  O   . GLY B 1 28  ? 8.341   10.046  39.402  1.00 22.49 ? 27   GLY B O   1 
ATOM   1288 N  N   . PRO B 1 29  ? 8.409   11.832  40.720  1.00 22.14 ? 28   PRO B N   1 
ATOM   1289 C  CA  . PRO B 1 29  ? 7.282   11.355  41.518  1.00 21.54 ? 28   PRO B CA  1 
ATOM   1290 C  C   . PRO B 1 29  ? 5.913   11.431  40.803  1.00 21.73 ? 28   PRO B C   1 
ATOM   1291 O  O   . PRO B 1 29  ? 5.711   12.180  39.832  1.00 24.03 ? 28   PRO B O   1 
ATOM   1292 C  CB  . PRO B 1 29  ? 7.303   12.271  42.747  1.00 20.14 ? 28   PRO B CB  1 
ATOM   1293 C  CG  . PRO B 1 29  ? 8.484   13.166  42.578  1.00 21.60 ? 28   PRO B CG  1 
ATOM   1294 C  CD  . PRO B 1 29  ? 8.886   13.155  41.154  1.00 21.27 ? 28   PRO B CD  1 
ATOM   1295 N  N   . VAL B 1 30  ? 4.994   10.590  41.248  1.00 23.07 ? 29   VAL B N   1 
ATOM   1296 C  CA  . VAL B 1 30  ? 3.595   10.614  40.787  1.00 22.36 ? 29   VAL B CA  1 
ATOM   1297 C  C   . VAL B 1 30  ? 2.740   11.376  41.810  1.00 23.60 ? 29   VAL B C   1 
ATOM   1298 O  O   . VAL B 1 30  ? 2.714   11.004  43.012  1.00 25.25 ? 29   VAL B O   1 
ATOM   1299 C  CB  . VAL B 1 30  ? 3.041   9.167   40.672  1.00 21.14 ? 29   VAL B CB  1 
ATOM   1300 C  CG1 . VAL B 1 30  ? 1.593   9.139   40.187  1.00 20.20 ? 29   VAL B CG1 1 
ATOM   1301 C  CG2 . VAL B 1 30  ? 3.935   8.333   39.747  1.00 23.19 ? 29   VAL B CG2 1 
ATOM   1302 N  N   . LYS B 1 31  ? 2.083   12.461  41.378  1.00 25.08 ? 30   LYS B N   1 
ATOM   1303 C  CA  . LYS B 1 31  ? 1.081   13.125  42.221  1.00 25.43 ? 30   LYS B CA  1 
ATOM   1304 C  C   . LYS B 1 31  ? -0.224  12.342  42.164  1.00 25.07 ? 30   LYS B C   1 
ATOM   1305 O  O   . LYS B 1 31  ? -0.738  12.008  41.073  1.00 27.72 ? 30   LYS B O   1 
ATOM   1306 C  CB  . LYS B 1 31  ? 0.777   14.543  41.739  1.00 25.84 ? 30   LYS B CB  1 
ATOM   1307 C  CG  . LYS B 1 31  ? 1.668   15.665  42.253  1.00 26.91 ? 30   LYS B CG  1 
ATOM   1308 C  CD  . LYS B 1 31  ? 2.143   16.512  41.057  1.00 28.08 ? 30   LYS B CD  1 
ATOM   1309 C  CE  . LYS B 1 31  ? 2.748   17.877  41.433  1.00 32.29 ? 30   LYS B CE  1 
ATOM   1310 N  NZ  . LYS B 1 31  ? 1.830   19.064  41.115  1.00 35.50 ? 30   LYS B NZ  1 
ATOM   1311 N  N   . VAL B 1 32  ? -0.778  12.037  43.333  1.00 24.73 ? 31   VAL B N   1 
ATOM   1312 C  CA  . VAL B 1 32  ? -2.036  11.335  43.413  1.00 22.70 ? 31   VAL B CA  1 
ATOM   1313 C  C   . VAL B 1 32  ? -3.060  12.179  44.151  1.00 22.99 ? 31   VAL B C   1 
ATOM   1314 O  O   . VAL B 1 32  ? -2.928  12.364  45.362  1.00 25.17 ? 31   VAL B O   1 
ATOM   1315 C  CB  . VAL B 1 32  ? -1.906  10.003  44.136  1.00 21.37 ? 31   VAL B CB  1 
ATOM   1316 C  CG1 . VAL B 1 32  ? -3.289  9.242   44.102  1.00 18.00 ? 31   VAL B CG1 1 
ATOM   1317 C  CG2 . VAL B 1 32  ? -0.754  9.194   43.568  1.00 21.73 ? 31   VAL B CG2 1 
ATOM   1318 N  N   . TRP B 1 33  ? -4.109  12.639  43.465  1.00 24.04 ? 32   TRP B N   1 
ATOM   1319 C  CA  . TRP B 1 33  ? -5.136  13.482  44.114  1.00 23.12 ? 32   TRP B CA  1 
ATOM   1320 C  C   . TRP B 1 33  ? -6.588  13.344  43.662  1.00 23.57 ? 32   TRP B C   1 
ATOM   1321 O  O   . TRP B 1 33  ? -6.880  12.914  42.537  1.00 24.75 ? 32   TRP B O   1 
ATOM   1322 C  CB  . TRP B 1 33  ? -4.779  14.973  44.017  1.00 21.85 ? 32   TRP B CB  1 
ATOM   1323 C  CG  . TRP B 1 33  ? -5.151  15.554  42.690  1.00 22.01 ? 32   TRP B CG  1 
ATOM   1324 C  CD1 . TRP B 1 33  ? -6.242  16.333  42.406  1.00 20.95 ? 32   TRP B CD1 1 
ATOM   1325 C  CD2 . TRP B 1 33  ? -4.466  15.360  41.453  1.00 19.86 ? 32   TRP B CD2 1 
ATOM   1326 N  NE1 . TRP B 1 33  ? -6.254  16.649  41.073  1.00 21.74 ? 32   TRP B NE1 1 
ATOM   1327 C  CE2 . TRP B 1 33  ? -5.168  16.081  40.469  1.00 20.10 ? 32   TRP B CE2 1 
ATOM   1328 C  CE3 . TRP B 1 33  ? -3.285  14.682  41.082  1.00 18.69 ? 32   TRP B CE3 1 
ATOM   1329 C  CZ2 . TRP B 1 33  ? -4.760  16.133  39.149  1.00 20.66 ? 32   TRP B CZ2 1 
ATOM   1330 C  CZ3 . TRP B 1 33  ? -2.883  14.727  39.752  1.00 17.45 ? 32   TRP B CZ3 1 
ATOM   1331 C  CH2 . TRP B 1 33  ? -3.623  15.447  38.803  1.00 21.90 ? 32   TRP B CH2 1 
ATOM   1332 N  N   . GLY B 1 34  ? -7.490  13.765  44.554  1.00 24.15 ? 33   GLY B N   1 
ATOM   1333 C  CA  . GLY B 1 34  ? -8.919  13.818  44.284  1.00 23.21 ? 33   GLY B CA  1 
ATOM   1334 C  C   . GLY B 1 34  ? -9.746  13.622  45.536  1.00 23.11 ? 33   GLY B C   1 
ATOM   1335 O  O   . GLY B 1 34  ? -9.308  13.996  46.623  1.00 24.31 ? 33   GLY B O   1 
ATOM   1336 N  N   . SER B 1 35  ? -10.921 13.005  45.402  1.00 24.50 ? 34   SER B N   1 
ATOM   1337 C  CA  . SER B 1 35  ? -11.821 12.790  46.535  1.00 25.78 ? 34   SER B CA  1 
ATOM   1338 C  C   . SER B 1 35  ? -12.600 11.491  46.529  1.00 25.60 ? 34   SER B C   1 
ATOM   1339 O  O   . SER B 1 35  ? -12.967 10.976  45.476  1.00 27.14 ? 34   SER B O   1 
ATOM   1340 C  CB  . SER B 1 35  ? -12.860 13.910  46.647  1.00 25.96 ? 34   SER B CB  1 
ATOM   1341 O  OG  . SER B 1 35  ? -12.225 15.170  46.738  1.00 30.60 ? 34   SER B OG  1 
ATOM   1342 N  N   . ILE B 1 36  ? -12.859 11.007  47.733  1.00 25.68 ? 35   ILE B N   1 
ATOM   1343 C  CA  . ILE B 1 36  ? -13.705 9.850   47.982  1.00 25.00 ? 35   ILE B CA  1 
ATOM   1344 C  C   . ILE B 1 36  ? -14.814 10.168  49.039  1.00 25.01 ? 35   ILE B C   1 
ATOM   1345 O  O   . ILE B 1 36  ? -14.546 10.760  50.101  1.00 26.63 ? 35   ILE B O   1 
ATOM   1346 C  CB  . ILE B 1 36  ? -12.859 8.640   48.424  1.00 23.59 ? 35   ILE B CB  1 
ATOM   1347 C  CG1 . ILE B 1 36  ? -11.677 8.370   47.470  1.00 23.62 ? 35   ILE B CG1 1 
ATOM   1348 C  CG2 . ILE B 1 36  ? -13.777 7.446   48.642  1.00 24.05 ? 35   ILE B CG2 1 
ATOM   1349 C  CD1 . ILE B 1 36  ? -10.720 7.319   47.970  1.00 23.13 ? 35   ILE B CD1 1 
ATOM   1350 N  N   . LYS B 1 37  ? -16.055 9.789   48.743  1.00 25.27 ? 36   LYS B N   1 
ATOM   1351 C  CA  . LYS B 1 37  ? -17.168 9.958   49.680  1.00 24.98 ? 36   LYS B CA  1 
ATOM   1352 C  C   . LYS B 1 37  ? -17.794 8.618   50.060  1.00 25.08 ? 36   LYS B C   1 
ATOM   1353 O  O   . LYS B 1 37  ? -17.470 7.579   49.450  1.00 26.13 ? 36   LYS B O   1 
ATOM   1354 C  CB  . LYS B 1 37  ? -18.206 10.973  49.183  1.00 24.91 ? 36   LYS B CB  1 
ATOM   1355 C  CG  . LYS B 1 37  ? -18.877 10.709  47.811  1.00 24.75 ? 36   LYS B CG  1 
ATOM   1356 C  CD  . LYS B 1 37  ? -19.943 11.794  47.506  1.00 23.55 ? 36   LYS B CD  1 
ATOM   1357 C  CE  . LYS B 1 37  ? -20.837 11.418  46.311  1.00 23.46 ? 36   LYS B CE  1 
ATOM   1358 N  NZ  . LYS B 1 37  ? -21.730 12.516  45.767  1.00 26.43 ? 36   LYS B NZ  1 
ATOM   1359 N  N   . GLY B 1 38  ? -18.632 8.625   51.094  1.00 25.62 ? 37   GLY B N   1 
ATOM   1360 C  CA  . GLY B 1 38  ? -19.288 7.412   51.570  1.00 24.88 ? 37   GLY B CA  1 
ATOM   1361 C  C   . GLY B 1 38  ? -18.536 6.538   52.538  1.00 24.81 ? 37   GLY B C   1 
ATOM   1362 O  O   . GLY B 1 38  ? -18.933 5.399   52.793  1.00 27.52 ? 37   GLY B O   1 
ATOM   1363 N  N   . LEU B 1 39  ? -17.442 7.041   53.075  1.00 25.23 ? 38   LEU B N   1 
ATOM   1364 C  CA  . LEU B 1 39  ? -16.631 6.296   54.020  1.00 24.52 ? 38   LEU B CA  1 
ATOM   1365 C  C   . LEU B 1 39  ? -17.053 6.589   55.449  1.00 25.66 ? 38   LEU B C   1 
ATOM   1366 O  O   . LEU B 1 39  ? -17.626 7.630   55.739  1.00 27.48 ? 38   LEU B O   1 
ATOM   1367 C  CB  . LEU B 1 39  ? -15.170 6.741   53.891  1.00 23.69 ? 38   LEU B CB  1 
ATOM   1368 C  CG  . LEU B 1 39  ? -14.084 6.194   52.955  1.00 23.54 ? 38   LEU B CG  1 
ATOM   1369 C  CD1 . LEU B 1 39  ? -14.449 5.059   52.042  1.00 23.85 ? 38   LEU B CD1 1 
ATOM   1370 C  CD2 . LEU B 1 39  ? -13.489 7.358   52.129  1.00 21.64 ? 38   LEU B CD2 1 
ATOM   1371 N  N   . THR B 1 40  ? -16.771 5.675   56.358  1.00 26.41 ? 39   THR B N   1 
ATOM   1372 C  CA  . THR B 1 40  ? -16.896 6.002   57.768  1.00 26.91 ? 39   THR B CA  1 
ATOM   1373 C  C   . THR B 1 40  ? -15.776 6.975   58.135  1.00 26.91 ? 39   THR B C   1 
ATOM   1374 O  O   . THR B 1 40  ? -14.724 7.000   57.488  1.00 27.59 ? 39   THR B O   1 
ATOM   1375 C  CB  . THR B 1 40  ? -16.689 4.782   58.589  1.00 26.48 ? 39   THR B CB  1 
ATOM   1376 O  OG1 . THR B 1 40  ? -15.451 4.192   58.180  1.00 28.17 ? 39   THR B OG1 1 
ATOM   1377 C  CG2 . THR B 1 40  ? -17.796 3.748   58.279  1.00 25.61 ? 39   THR B CG2 1 
ATOM   1378 N  N   . GLU B 1 41  ? -16.007 7.764   59.176  1.00 27.42 ? 40   GLU B N   1 
ATOM   1379 C  CA  . GLU B 1 41  ? -15.003 8.700   59.683  1.00 27.26 ? 40   GLU B CA  1 
ATOM   1380 C  C   . GLU B 1 41  ? -13.691 7.987   60.016  1.00 27.35 ? 40   GLU B C   1 
ATOM   1381 O  O   . GLU B 1 41  ? -13.665 6.890   60.576  1.00 27.71 ? 40   GLU B O   1 
ATOM   1382 C  CB  . GLU B 1 41  ? -15.530 9.446   60.913  1.00 27.34 ? 40   GLU B CB  1 
ATOM   1383 C  CG  . GLU B 1 41  ? -14.631 10.582  61.391  1.00 28.35 ? 40   GLU B CG  1 
ATOM   1384 C  CD  . GLU B 1 41  ? -15.291 11.464  62.449  1.00 30.45 ? 40   GLU B CD  1 
ATOM   1385 O  OE1 . GLU B 1 41  ? -16.389 11.106  62.931  1.00 32.15 ? 40   GLU B OE1 1 
ATOM   1386 O  OE2 . GLU B 1 41  ? -14.716 12.517  62.811  1.00 31.64 ? 40   GLU B OE2 1 
ATOM   1387 N  N   . GLY B 1 42  ? -12.590 8.601   59.638  1.00 27.30 ? 41   GLY B N   1 
ATOM   1388 C  CA  . GLY B 1 42  ? -11.322 8.036   60.013  1.00 27.56 ? 41   GLY B CA  1 
ATOM   1389 C  C   . GLY B 1 42  ? -10.515 7.485   58.872  1.00 26.56 ? 41   GLY B C   1 
ATOM   1390 O  O   . GLY B 1 42  ? -10.787 7.714   57.680  1.00 27.77 ? 41   GLY B O   1 
ATOM   1391 N  N   . LEU B 1 43  ? -9.507  6.736   59.283  1.00 26.88 ? 42   LEU B N   1 
ATOM   1392 C  CA  . LEU B 1 43  ? -8.490  6.188   58.427  1.00 26.14 ? 42   LEU B CA  1 
ATOM   1393 C  C   . LEU B 1 43  ? -8.921  4.969   57.596  1.00 25.62 ? 42   LEU B C   1 
ATOM   1394 O  O   . LEU B 1 43  ? -9.622  4.075   58.095  1.00 25.97 ? 42   LEU B O   1 
ATOM   1395 C  CB  . LEU B 1 43  ? -7.292  5.852   59.303  1.00 25.92 ? 42   LEU B CB  1 
ATOM   1396 C  CG  . LEU B 1 43  ? -6.024  6.695   59.191  1.00 27.27 ? 42   LEU B CG  1 
ATOM   1397 C  CD1 . LEU B 1 43  ? -6.301  8.177   59.123  1.00 28.42 ? 42   LEU B CD1 1 
ATOM   1398 C  CD2 . LEU B 1 43  ? -5.132  6.373   60.370  1.00 30.57 ? 42   LEU B CD2 1 
ATOM   1399 N  N   . HIS B 1 44  ? -8.510  4.961   56.325  1.00 25.91 ? 43   HIS B N   1 
ATOM   1400 C  CA  . HIS B 1 44  ? -8.829  3.869   55.378  1.00 24.91 ? 43   HIS B CA  1 
ATOM   1401 C  C   . HIS B 1 44  ? -7.637  3.527   54.488  1.00 24.18 ? 43   HIS B C   1 
ATOM   1402 O  O   . HIS B 1 44  ? -7.039  4.377   53.802  1.00 25.26 ? 43   HIS B O   1 
ATOM   1403 C  CB  . HIS B 1 44  ? -10.042 4.215   54.475  1.00 23.65 ? 43   HIS B CB  1 
ATOM   1404 C  CG  . HIS B 1 44  ? -11.349 4.361   55.197  1.00 23.74 ? 43   HIS B CG  1 
ATOM   1405 N  ND1 . HIS B 1 44  ? -12.277 3.346   55.288  1.00 24.15 ? 43   HIS B ND1 1 
ATOM   1406 C  CD2 . HIS B 1 44  ? -11.896 5.421   55.838  1.00 14.42 ? 43   HIS B CD2 1 
ATOM   1407 C  CE1 . HIS B 1 44  ? -13.334 3.770   55.954  1.00 22.56 ? 43   HIS B CE1 1 
ATOM   1408 N  NE2 . HIS B 1 44  ? -13.127 5.025   56.307  1.00 24.62 ? 43   HIS B NE2 1 
ATOM   1409 N  N   . GLY B 1 45  ? -7.278  2.254   54.455  1.00 24.98 ? 44   GLY B N   1 
ATOM   1410 C  CA  . GLY B 1 45  ? -6.185  1.828   53.612  1.00 23.52 ? 44   GLY B CA  1 
ATOM   1411 C  C   . GLY B 1 45  ? -6.397  2.168   52.141  1.00 22.39 ? 44   GLY B C   1 
ATOM   1412 O  O   . GLY B 1 45  ? -7.513  2.046   51.611  1.00 25.43 ? 44   GLY B O   1 
ATOM   1413 N  N   . PHE B 1 46  ? -5.324  2.600   51.488  1.00 22.60 ? 45   PHE B N   1 
ATOM   1414 C  CA  . PHE B 1 46  ? -5.320  3.084   50.106  1.00 21.18 ? 45   PHE B CA  1 
ATOM   1415 C  C   . PHE B 1 46  ? -4.166  2.396   49.368  1.00 22.81 ? 45   PHE B C   1 
ATOM   1416 O  O   . PHE B 1 46  ? -2.979  2.772   49.508  1.00 23.03 ? 45   PHE B O   1 
ATOM   1417 C  CB  . PHE B 1 46  ? -5.159  4.613   50.177  1.00 21.54 ? 45   PHE B CB  1 
ATOM   1418 C  CG  . PHE B 1 46  ? -5.469  5.338   48.918  1.00 18.54 ? 45   PHE B CG  1 
ATOM   1419 C  CD1 . PHE B 1 46  ? -6.753  5.319   48.385  1.00 23.62 ? 45   PHE B CD1 1 
ATOM   1420 C  CD2 . PHE B 1 46  ? -4.479  6.117   48.309  1.00 18.97 ? 45   PHE B CD2 1 
ATOM   1421 C  CE1 . PHE B 1 46  ? -7.065  6.005   47.207  1.00 22.95 ? 45   PHE B CE1 1 
ATOM   1422 C  CE2 . PHE B 1 46  ? -4.766  6.818   47.104  1.00 18.80 ? 45   PHE B CE2 1 
ATOM   1423 C  CZ  . PHE B 1 46  ? -6.067  6.767   46.564  1.00 21.69 ? 45   PHE B CZ  1 
ATOM   1424 N  N   . HIS B 1 47  ? -4.513  1.341   48.628  1.00 23.79 ? 46   HIS B N   1 
ATOM   1425 C  CA  . HIS B 1 47  ? -3.577  0.473   47.932  1.00 23.58 ? 46   HIS B CA  1 
ATOM   1426 C  C   . HIS B 1 47  ? -3.797  0.199   46.443  1.00 22.35 ? 46   HIS B C   1 
ATOM   1427 O  O   . HIS B 1 47  ? -4.948  0.087   45.940  1.00 26.16 ? 46   HIS B O   1 
ATOM   1428 C  CB  . HIS B 1 47  ? -3.511  -0.882  48.633  1.00 22.54 ? 46   HIS B CB  1 
ATOM   1429 C  CG  . HIS B 1 47  ? -3.372  -0.784  50.116  1.00 23.31 ? 46   HIS B CG  1 
ATOM   1430 N  ND1 . HIS B 1 47  ? -4.167  -1.492  50.975  1.00 25.99 ? 46   HIS B ND1 1 
ATOM   1431 C  CD2 . HIS B 1 47  ? -2.567  -0.021  50.887  1.00 23.67 ? 46   HIS B CD2 1 
ATOM   1432 C  CE1 . HIS B 1 47  ? -3.858  -1.177  52.217  1.00 26.46 ? 46   HIS B CE1 1 
ATOM   1433 N  NE2 . HIS B 1 47  ? -2.890  -0.284  52.187  1.00 27.03 ? 46   HIS B NE2 1 
ATOM   1434 N  N   . VAL B 1 48  ? -2.681  0.019   45.753  1.00 24.28 ? 47   VAL B N   1 
ATOM   1435 C  CA  . VAL B 1 48  ? -2.731  -0.429  44.402  1.00 23.14 ? 47   VAL B CA  1 
ATOM   1436 C  C   . VAL B 1 48  ? -2.602  -1.929  44.477  1.00 21.55 ? 47   VAL B C   1 
ATOM   1437 O  O   . VAL B 1 48  ? -1.615  -2.437  45.005  1.00 25.62 ? 47   VAL B O   1 
ATOM   1438 C  CB  . VAL B 1 48  ? -1.630  0.159   43.545  1.00 21.84 ? 47   VAL B CB  1 
ATOM   1439 C  CG1 . VAL B 1 48  ? -1.810  -0.248  42.103  1.00 23.13 ? 47   VAL B CG1 1 
ATOM   1440 C  CG2 . VAL B 1 48  ? -1.647  1.700   43.676  1.00 25.75 ? 47   VAL B CG2 1 
ATOM   1441 N  N   . HIS B 1 49  ? -3.623  -2.611  43.988  1.00 22.96 ? 48   HIS B N   1 
ATOM   1442 C  CA  . HIS B 1 49  ? -3.608  -4.077  43.907  1.00 21.50 ? 48   HIS B CA  1 
ATOM   1443 C  C   . HIS B 1 49  ? -3.122  -4.469  42.506  1.00 21.15 ? 48   HIS B C   1 
ATOM   1444 O  O   . HIS B 1 49  ? -3.145  -3.635  41.559  1.00 24.50 ? 48   HIS B O   1 
ATOM   1445 C  CB  . HIS B 1 49  ? -4.970  -4.680  44.279  1.00 19.88 ? 48   HIS B CB  1 
ATOM   1446 C  CG  . HIS B 1 49  ? -5.308  -4.548  45.736  1.00 19.23 ? 48   HIS B CG  1 
ATOM   1447 N  ND1 . HIS B 1 49  ? -5.533  -5.628  46.559  1.00 24.05 ? 48   HIS B ND1 1 
ATOM   1448 C  CD2 . HIS B 1 49  ? -5.409  -3.447  46.519  1.00 18.95 ? 48   HIS B CD2 1 
ATOM   1449 C  CE1 . HIS B 1 49  ? -5.798  -5.194  47.780  1.00 21.86 ? 48   HIS B CE1 1 
ATOM   1450 N  NE2 . HIS B 1 49  ? -5.718  -3.867  47.782  1.00 22.41 ? 48   HIS B NE2 1 
ATOM   1451 N  N   . GLU B 1 50  ? -2.644  -5.720  42.401  1.00 21.68 ? 49   GLU B N   1 
ATOM   1452 C  CA  . GLU B 1 50  ? -2.029  -6.301  41.221  1.00 21.37 ? 49   GLU B CA  1 
ATOM   1453 C  C   . GLU B 1 50  ? -2.823  -6.292  39.936  1.00 20.53 ? 49   GLU B C   1 
ATOM   1454 O  O   . GLU B 1 50  ? -2.294  -5.866  38.918  1.00 22.71 ? 49   GLU B O   1 
ATOM   1455 C  CB  . GLU B 1 50  ? -1.485  -7.737  41.462  1.00 21.42 ? 49   GLU B CB  1 
ATOM   1456 C  CG  . GLU B 1 50  ? -0.468  -8.129  40.392  1.00 20.45 ? 49   GLU B CG  1 
ATOM   1457 C  CD  . GLU B 1 50  ? 0.138   -9.505  40.577  1.00 24.90 ? 49   GLU B CD  1 
ATOM   1458 O  OE1 . GLU B 1 50  ? -0.233  -10.215 41.535  1.00 29.77 ? 49   GLU B OE1 1 
ATOM   1459 O  OE2 . GLU B 1 50  ? 1.009   -9.851  39.768  1.00 28.36 ? 49   GLU B OE2 1 
ATOM   1460 N  N   . PHE B 1 51  ? -4.070  -6.758  39.966  1.00 21.81 ? 50   PHE B N   1 
ATOM   1461 C  CA  . PHE B 1 51  ? -4.793  -6.884  38.719  1.00 22.50 ? 50   PHE B CA  1 
ATOM   1462 C  C   . PHE B 1 51  ? -5.880  -5.884  38.460  1.00 22.68 ? 50   PHE B C   1 
ATOM   1463 O  O   . PHE B 1 51  ? -6.600  -5.506  39.372  1.00 25.00 ? 50   PHE B O   1 
ATOM   1464 C  CB  . PHE B 1 51  ? -5.343  -8.301  38.591  1.00 23.08 ? 50   PHE B CB  1 
ATOM   1465 C  CG  . PHE B 1 51  ? -4.280  -9.324  38.657  1.00 24.15 ? 50   PHE B CG  1 
ATOM   1466 C  CD1 . PHE B 1 51  ? -3.311  -9.376  37.686  1.00 25.17 ? 50   PHE B CD1 1 
ATOM   1467 C  CD2 . PHE B 1 51  ? -4.200  -10.204 39.750  1.00 26.58 ? 50   PHE B CD2 1 
ATOM   1468 C  CE1 . PHE B 1 51  ? -2.265  -10.313 37.782  1.00 23.44 ? 50   PHE B CE1 1 
ATOM   1469 C  CE2 . PHE B 1 51  ? -3.182  -11.124 39.833  1.00 24.14 ? 50   PHE B CE2 1 
ATOM   1470 C  CZ  . PHE B 1 51  ? -2.221  -11.178 38.856  1.00 22.99 ? 50   PHE B CZ  1 
ATOM   1471 N  N   . GLY B 1 52  ? -5.957  -5.429  37.199  1.00 23.61 ? 51   GLY B N   1 
ATOM   1472 C  CA  . GLY B 1 52  ? -7.052  -4.605  36.699  1.00 23.28 ? 51   GLY B CA  1 
ATOM   1473 C  C   . GLY B 1 52  ? -8.227  -5.499  36.267  1.00 23.45 ? 51   GLY B C   1 
ATOM   1474 O  O   . GLY B 1 52  ? -8.744  -5.444  35.147  1.00 23.10 ? 51   GLY B O   1 
ATOM   1475 N  N   . ASP B 1 53  ? -8.619  -6.383  37.169  1.00 24.79 ? 52   ASP B N   1 
ATOM   1476 C  CA  . ASP B 1 53  ? -9.645  -7.345  36.915  1.00 24.48 ? 52   ASP B CA  1 
ATOM   1477 C  C   . ASP B 1 53  ? -10.784 -7.214  37.911  1.00 23.13 ? 52   ASP B C   1 
ATOM   1478 O  O   . ASP B 1 53  ? -10.676 -7.593  39.091  1.00 24.67 ? 52   ASP B O   1 
ATOM   1479 C  CB  . ASP B 1 53  ? -9.055  -8.741  37.066  1.00 25.25 ? 52   ASP B CB  1 
ATOM   1480 C  CG  . ASP B 1 53  ? -10.075 -9.830  36.828  1.00 25.31 ? 52   ASP B CG  1 
ATOM   1481 O  OD1 . ASP B 1 53  ? -11.314 -9.614  36.999  1.00 26.05 ? 52   ASP B OD1 1 
ATOM   1482 O  OD2 . ASP B 1 53  ? -9.714  -10.977 36.465  1.00 32.45 ? 52   ASP B OD2 1 
ATOM   1483 N  N   . ASN B 1 54  ? -11.897 -6.702  37.432  1.00 23.33 ? 53   ASN B N   1 
ATOM   1484 C  CA  . ASN B 1 54  ? -13.040 -6.540  38.270  1.00 23.55 ? 53   ASN B CA  1 
ATOM   1485 C  C   . ASN B 1 54  ? -14.140 -7.548  38.000  1.00 23.04 ? 53   ASN B C   1 
ATOM   1486 O  O   . ASN B 1 54  ? -15.291 -7.353  38.400  1.00 22.82 ? 53   ASN B O   1 
ATOM   1487 C  CB  . ASN B 1 54  ? -13.585 -5.133  38.113  1.00 23.13 ? 53   ASN B CB  1 
ATOM   1488 C  CG  . ASN B 1 54  ? -14.731 -4.847  39.089  1.00 27.23 ? 53   ASN B CG  1 
ATOM   1489 O  OD1 . ASN B 1 54  ? -14.511 -4.576  40.281  1.00 33.08 ? 53   ASN B OD1 1 
ATOM   1490 N  ND2 . ASN B 1 54  ? -15.954 -4.905  38.588  1.00 35.35 ? 53   ASN B ND2 1 
ATOM   1491 N  N   . THR B 1 55  ? -13.803 -8.630  37.308  1.00 23.94 ? 54   THR B N   1 
ATOM   1492 C  CA  . THR B 1 55  ? -14.828 -9.572  36.957  1.00 23.97 ? 54   THR B CA  1 
ATOM   1493 C  C   . THR B 1 55  ? -15.689 -9.965  38.153  1.00 24.59 ? 54   THR B C   1 
ATOM   1494 O  O   . THR B 1 55  ? -16.901 -10.101 38.019  1.00 26.31 ? 54   THR B O   1 
ATOM   1495 C  CB  . THR B 1 55  ? -14.263 -10.838 36.290  1.00 23.11 ? 54   THR B CB  1 
ATOM   1496 O  OG1 . THR B 1 55  ? -13.156 -11.299 37.052  1.00 25.19 ? 54   THR B OG1 1 
ATOM   1497 C  CG2 . THR B 1 55  ? -13.707 -10.568 34.911  1.00 21.85 ? 54   THR B CG2 1 
ATOM   1498 N  N   . ALA B 1 56  ? -15.086 -10.158 39.315  1.00 26.40 ? 55   ALA B N   1 
ATOM   1499 C  CA  . ALA B 1 56  ? -15.858 -10.501 40.487  1.00 26.38 ? 55   ALA B CA  1 
ATOM   1500 C  C   . ALA B 1 56  ? -15.918 -9.415  41.518  1.00 25.76 ? 55   ALA B C   1 
ATOM   1501 O  O   . ALA B 1 56  ? -16.064 -9.706  42.693  1.00 28.17 ? 55   ALA B O   1 
ATOM   1502 C  CB  . ALA B 1 56  ? -15.349 -11.807 41.149  1.00 26.00 ? 55   ALA B CB  1 
ATOM   1503 N  N   . GLY B 1 57  ? -15.881 -8.165  41.104  1.00 26.46 ? 56   GLY B N   1 
ATOM   1504 C  CA  . GLY B 1 57  ? -15.786 -7.110  42.092  1.00 25.29 ? 56   GLY B CA  1 
ATOM   1505 C  C   . GLY B 1 57  ? -14.316 -6.898  42.414  1.00 25.67 ? 56   GLY B C   1 
ATOM   1506 O  O   . GLY B 1 57  ? -13.423 -7.435  41.719  1.00 26.21 ? 56   GLY B O   1 
ATOM   1507 N  N   . CYS B 1 58  ? -14.079 -6.108  43.457  1.00 25.41 ? 57   CYS B N   1 
ATOM   1508 C  CA  . CYS B 1 58  ? -12.779 -5.792  43.986  1.00 24.98 ? 57   CYS B CA  1 
ATOM   1509 C  C   . CYS B 1 58  ? -11.883 -6.991  44.333  1.00 25.14 ? 57   CYS B C   1 
ATOM   1510 O  O   . CYS B 1 58  ? -10.677 -6.894  44.145  1.00 26.81 ? 57   CYS B O   1 
ATOM   1511 C  CB  . CYS B 1 58  ? -12.933 -4.815  45.156  1.00 23.38 ? 57   CYS B CB  1 
ATOM   1512 S  SG  . CYS B 1 58  ? -13.778 -3.304  44.596  1.00 28.07 ? 57   CYS B SG  1 
ATOM   1513 N  N   . THR B 1 59  ? -12.461 -8.117  44.766  1.00 26.76 ? 58   THR B N   1 
ATOM   1514 C  CA  . THR B 1 59  ? -11.645 -9.286  45.100  1.00 26.81 ? 58   THR B CA  1 
ATOM   1515 C  C   . THR B 1 59  ? -10.814 -9.757  43.911  1.00 25.90 ? 58   THR B C   1 
ATOM   1516 O  O   . THR B 1 59  ? -9.716  -10.294 44.071  1.00 26.18 ? 58   THR B O   1 
ATOM   1517 C  CB  . THR B 1 59  ? -12.503 -10.479 45.727  1.00 26.09 ? 58   THR B CB  1 
ATOM   1518 O  OG1 . THR B 1 59  ? -13.292 -11.139 44.716  1.00 30.95 ? 58   THR B OG1 1 
ATOM   1519 C  CG2 . THR B 1 59  ? -13.546 -9.942  46.666  1.00 26.69 ? 58   THR B CG2 1 
ATOM   1520 N  N   . SER B 1 60  ? -11.317 -9.545  42.707  1.00 27.15 ? 59   SER B N   1 
ATOM   1521 C  CA  . SER B 1 60  ? -10.596 -10.055 41.561  1.00 27.16 ? 59   SER B CA  1 
ATOM   1522 C  C   . SER B 1 60  ? -9.336  -9.258  41.238  1.00 26.53 ? 59   SER B C   1 
ATOM   1523 O  O   . SER B 1 60  ? -8.538  -9.656  40.401  1.00 28.44 ? 59   SER B O   1 
ATOM   1524 C  CB  . SER B 1 60  ? -11.523 -10.265 40.356  1.00 27.17 ? 59   SER B CB  1 
ATOM   1525 O  OG  . SER B 1 60  ? -12.563 -9.300  40.332  1.00 31.25 ? 59   SER B OG  1 
ATOM   1526 N  N   . ALA B 1 61  ? -9.142  -8.141  41.925  1.00 25.52 ? 60   ALA B N   1 
ATOM   1527 C  CA  . ALA B 1 61  ? -7.928  -7.360  41.736  1.00 25.36 ? 60   ALA B CA  1 
ATOM   1528 C  C   . ALA B 1 61  ? -6.699  -8.069  42.353  1.00 24.86 ? 60   ALA B C   1 
ATOM   1529 O  O   . ALA B 1 61  ? -5.565  -7.680  42.116  1.00 26.47 ? 60   ALA B O   1 
ATOM   1530 C  CB  . ALA B 1 61  ? -8.118  -5.919  42.305  1.00 22.96 ? 60   ALA B CB  1 
ATOM   1531 N  N   . GLY B 1 62  ? -6.929  -9.124  43.141  1.00 25.53 ? 61   GLY B N   1 
ATOM   1532 C  CA  . GLY B 1 62  ? -5.849  -9.868  43.773  1.00 25.19 ? 61   GLY B CA  1 
ATOM   1533 C  C   . GLY B 1 62  ? -5.090  -9.174  44.888  1.00 24.40 ? 61   GLY B C   1 
ATOM   1534 O  O   . GLY B 1 62  ? -5.607  -8.257  45.530  1.00 26.16 ? 61   GLY B O   1 
ATOM   1535 N  N   . PRO B 1 63  ? -3.834  -9.568  45.084  1.00 25.28 ? 62   PRO B N   1 
ATOM   1536 C  CA  . PRO B 1 63  ? -3.021  -9.109  46.232  1.00 24.34 ? 62   PRO B CA  1 
ATOM   1537 C  C   . PRO B 1 63  ? -2.531  -7.706  45.977  1.00 24.52 ? 62   PRO B C   1 
ATOM   1538 O  O   . PRO B 1 63  ? -2.879  -7.182  44.926  1.00 25.22 ? 62   PRO B O   1 
ATOM   1539 C  CB  . PRO B 1 63  ? -1.793  -10.029 46.211  1.00 24.47 ? 62   PRO B CB  1 
ATOM   1540 C  CG  . PRO B 1 63  ? -1.867  -10.854 44.904  1.00 24.21 ? 62   PRO B CG  1 
ATOM   1541 C  CD  . PRO B 1 63  ? -3.106  -10.478 44.173  1.00 25.29 ? 62   PRO B CD  1 
ATOM   1542 N  N   . HIS B 1 64  ? -1.709  -7.161  46.875  1.00 25.45 ? 63   HIS B N   1 
ATOM   1543 C  CA  . HIS B 1 64  ? -1.113  -5.840  46.659  1.00 24.61 ? 63   HIS B CA  1 
ATOM   1544 C  C   . HIS B 1 64  ? -0.168  -5.869  45.456  1.00 24.24 ? 63   HIS B C   1 
ATOM   1545 O  O   . HIS B 1 64  ? 0.471   -6.888  45.193  1.00 25.37 ? 63   HIS B O   1 
ATOM   1546 C  CB  . HIS B 1 64  ? -0.313  -5.419  47.885  1.00 24.19 ? 63   HIS B CB  1 
ATOM   1547 C  CG  . HIS B 1 64  ? -1.136  -4.875  49.003  1.00 24.63 ? 63   HIS B CG  1 
ATOM   1548 N  ND1 . HIS B 1 64  ? -0.575  -4.208  50.067  1.00 28.18 ? 63   HIS B ND1 1 
ATOM   1549 C  CD2 . HIS B 1 64  ? -2.468  -4.915  49.242  1.00 27.33 ? 63   HIS B CD2 1 
ATOM   1550 C  CE1 . HIS B 1 64  ? -1.525  -3.834  50.898  1.00 25.79 ? 63   HIS B CE1 1 
ATOM   1551 N  NE2 . HIS B 1 64  ? -2.683  -4.264  50.431  1.00 30.89 ? 63   HIS B NE2 1 
ATOM   1552 N  N   . PHE B 1 65  ? -0.062  -4.776  44.698  1.00 24.76 ? 64   PHE B N   1 
ATOM   1553 C  CA  . PHE B 1 65  ? 0.969   -4.738  43.655  1.00 23.43 ? 64   PHE B CA  1 
ATOM   1554 C  C   . PHE B 1 65  ? 2.356   -4.784  44.350  1.00 23.65 ? 64   PHE B C   1 
ATOM   1555 O  O   . PHE B 1 65  ? 2.806   -3.818  44.963  1.00 25.87 ? 64   PHE B O   1 
ATOM   1556 C  CB  . PHE B 1 65  ? 0.823   -3.514  42.716  1.00 21.65 ? 64   PHE B CB  1 
ATOM   1557 C  CG  . PHE B 1 65  ? 1.840   -3.479  41.564  1.00 15.98 ? 64   PHE B CG  1 
ATOM   1558 C  CD1 . PHE B 1 65  ? 2.160   -4.622  40.835  1.00 15.47 ? 64   PHE B CD1 1 
ATOM   1559 C  CD2 . PHE B 1 65  ? 2.417   -2.298  41.146  1.00 16.35 ? 64   PHE B CD2 1 
ATOM   1560 C  CE1 . PHE B 1 65  ? 3.048   -4.594  39.801  1.00 13.39 ? 64   PHE B CE1 1 
ATOM   1561 C  CE2 . PHE B 1 65  ? 3.308   -2.273  40.070  1.00 12.85 ? 64   PHE B CE2 1 
ATOM   1562 C  CZ  . PHE B 1 65  ? 3.630   -3.401  39.375  1.00 14.61 ? 64   PHE B CZ  1 
ATOM   1563 N  N   . ASN B 1 66  ? 3.039   -5.919  44.255  1.00 24.22 ? 65   ASN B N   1 
ATOM   1564 C  CA  . ASN B 1 66  ? 4.316   -6.105  44.972  1.00 24.71 ? 65   ASN B CA  1 
ATOM   1565 C  C   . ASN B 1 66  ? 5.334   -6.856  44.112  1.00 24.81 ? 65   ASN B C   1 
ATOM   1566 O  O   . ASN B 1 66  ? 5.727   -7.974  44.416  1.00 25.74 ? 65   ASN B O   1 
ATOM   1567 C  CB  . ASN B 1 66  ? 4.002   -6.771  46.322  1.00 25.25 ? 65   ASN B CB  1 
ATOM   1568 C  CG  . ASN B 1 66  ? 5.230   -7.152  47.146  1.00 25.08 ? 65   ASN B CG  1 
ATOM   1569 O  OD1 . ASN B 1 66  ? 6.259   -6.476  47.162  1.00 28.93 ? 65   ASN B OD1 1 
ATOM   1570 N  ND2 . ASN B 1 66  ? 5.099   -8.265  47.854  1.00 28.31 ? 65   ASN B ND2 1 
ATOM   1571 N  N   . PRO B 1 67  ? 5.771   -6.229  43.029  1.00 25.77 ? 66   PRO B N   1 
ATOM   1572 C  CA  . PRO B 1 67  ? 6.687   -6.901  42.098  1.00 25.72 ? 66   PRO B CA  1 
ATOM   1573 C  C   . PRO B 1 67  ? 8.094   -7.102  42.653  1.00 26.17 ? 66   PRO B C   1 
ATOM   1574 O  O   . PRO B 1 67  ? 8.769   -7.999  42.140  1.00 27.50 ? 66   PRO B O   1 
ATOM   1575 C  CB  . PRO B 1 67  ? 6.725   -5.974  40.898  1.00 26.00 ? 66   PRO B CB  1 
ATOM   1576 C  CG  . PRO B 1 67  ? 6.360   -4.647  41.442  1.00 24.71 ? 66   PRO B CG  1 
ATOM   1577 C  CD  . PRO B 1 67  ? 5.444   -4.852  42.603  1.00 23.90 ? 66   PRO B CD  1 
ATOM   1578 N  N   . LEU B 1 68  ? 8.522   -6.319  43.651  1.00 26.85 ? 67   LEU B N   1 
ATOM   1579 C  CA  . LEU B 1 68  ? 9.857   -6.490  44.244  1.00 28.25 ? 67   LEU B CA  1 
ATOM   1580 C  C   . LEU B 1 68  ? 9.779   -7.367  45.481  1.00 28.85 ? 67   LEU B C   1 
ATOM   1581 O  O   . LEU B 1 68  ? 10.748  -7.478  46.237  1.00 30.07 ? 67   LEU B O   1 
ATOM   1582 C  CB  . LEU B 1 68  ? 10.567  -5.161  44.551  1.00 27.13 ? 67   LEU B CB  1 
ATOM   1583 C  CG  . LEU B 1 68  ? 10.784  -4.192  43.377  1.00 28.93 ? 67   LEU B CG  1 
ATOM   1584 C  CD1 . LEU B 1 68  ? 11.560  -2.965  43.843  1.00 28.34 ? 67   LEU B CD1 1 
ATOM   1585 C  CD2 . LEU B 1 68  ? 11.463  -4.824  42.140  1.00 28.62 ? 67   LEU B CD2 1 
ATOM   1586 N  N   . SER B 1 69  ? 8.611   -7.969  45.686  1.00 29.81 ? 68   SER B N   1 
ATOM   1587 C  CA  . SER B 1 69  ? 8.420   -8.979  46.716  1.00 30.49 ? 68   SER B CA  1 
ATOM   1588 C  C   . SER B 1 69  ? 8.773   -8.597  48.160  1.00 30.48 ? 68   SER B C   1 
ATOM   1589 O  O   . SER B 1 69  ? 9.306   -9.431  48.912  1.00 30.85 ? 68   SER B O   1 
ATOM   1590 C  CB  . SER B 1 69  ? 9.222   -10.231 46.331  1.00 31.04 ? 68   SER B CB  1 
ATOM   1591 O  OG  . SER B 1 69  ? 8.427   -11.162 45.613  1.00 34.12 ? 68   SER B OG  1 
ATOM   1592 N  N   . ARG B 1 70  ? 8.494   -7.360  48.559  1.00 30.10 ? 69   ARG B N   1 
ATOM   1593 C  CA  . ARG B 1 70  ? 8.827   -6.940  49.909  1.00 30.10 ? 69   ARG B CA  1 
ATOM   1594 C  C   . ARG B 1 70  ? 7.662   -7.146  50.868  1.00 29.67 ? 69   ARG B C   1 
ATOM   1595 O  O   . ARG B 1 70  ? 6.570   -7.480  50.468  1.00 30.10 ? 69   ARG B O   1 
ATOM   1596 C  CB  . ARG B 1 70  ? 9.283   -5.480  49.910  1.00 30.33 ? 69   ARG B CB  1 
ATOM   1597 C  CG  . ARG B 1 70  ? 10.339  -5.171  48.841  1.00 32.37 ? 69   ARG B CG  1 
ATOM   1598 C  CD  . ARG B 1 70  ? 11.387  -4.139  49.285  1.00 36.90 ? 69   ARG B CD  1 
ATOM   1599 N  NE  . ARG B 1 70  ? 12.295  -3.744  48.212  1.00 39.53 ? 69   ARG B NE  1 
ATOM   1600 C  CZ  . ARG B 1 70  ? 13.250  -4.520  47.725  1.00 40.38 ? 69   ARG B CZ  1 
ATOM   1601 N  NH1 . ARG B 1 70  ? 13.419  -5.740  48.224  1.00 42.66 ? 69   ARG B NH1 1 
ATOM   1602 N  NH2 . ARG B 1 70  ? 14.040  -4.084  46.743  1.00 39.53 ? 69   ARG B NH2 1 
ATOM   1603 N  N   . LYS B 1 71  ? 7.902   -6.988  52.154  1.00 29.58 ? 70   LYS B N   1 
ATOM   1604 C  CA  . LYS B 1 71  ? 6.811   -7.089  53.082  1.00 29.27 ? 70   LYS B CA  1 
ATOM   1605 C  C   . LYS B 1 71  ? 6.122   -5.733  53.113  1.00 28.58 ? 70   LYS B C   1 
ATOM   1606 O  O   . LYS B 1 71  ? 6.693   -4.718  52.692  1.00 29.64 ? 70   LYS B O   1 
ATOM   1607 C  CB  . LYS B 1 71  ? 7.293   -7.496  54.474  1.00 29.42 ? 70   LYS B CB  1 
ATOM   1608 C  CG  . LYS B 1 71  ? 8.125   -6.424  55.160  1.00 29.46 ? 70   LYS B CG  1 
ATOM   1609 C  CD  . LYS B 1 71  ? 8.867   -6.934  56.397  1.00 33.25 ? 70   LYS B CD  1 
ATOM   1610 C  CE  . LYS B 1 71  ? 9.645   -5.758  57.084  1.00 34.38 ? 70   LYS B CE  1 
ATOM   1611 N  NZ  . LYS B 1 71  ? 9.930   -5.914  58.572  1.00 36.49 ? 70   LYS B NZ  1 
ATOM   1612 N  N   . HIS B 1 72  ? 4.909   -5.730  53.631  1.00 27.67 ? 71   HIS B N   1 
ATOM   1613 C  CA  . HIS B 1 72  ? 4.084   -4.539  53.670  1.00 26.09 ? 71   HIS B CA  1 
ATOM   1614 C  C   . HIS B 1 72  ? 4.609   -3.443  54.605  1.00 26.01 ? 71   HIS B C   1 
ATOM   1615 O  O   . HIS B 1 72  ? 5.082   -3.705  55.692  1.00 26.72 ? 71   HIS B O   1 
ATOM   1616 C  CB  . HIS B 1 72  ? 2.669   -4.932  54.071  1.00 26.01 ? 71   HIS B CB  1 
ATOM   1617 C  CG  . HIS B 1 72  ? 1.721   -3.776  54.186  1.00 26.30 ? 71   HIS B CG  1 
ATOM   1618 N  ND1 . HIS B 1 72  ? 1.229   -3.105  53.091  1.00 26.80 ? 71   HIS B ND1 1 
ATOM   1619 C  CD2 . HIS B 1 72  ? 1.156   -3.191  55.271  1.00 27.72 ? 71   HIS B CD2 1 
ATOM   1620 C  CE1 . HIS B 1 72  ? 0.405   -2.156  53.492  1.00 27.87 ? 71   HIS B CE1 1 
ATOM   1621 N  NE2 . HIS B 1 72  ? 0.351   -2.176  54.809  1.00 28.86 ? 71   HIS B NE2 1 
ATOM   1622 N  N   . GLY B 1 73  ? 4.521   -2.197  54.167  1.00 26.49 ? 72   GLY B N   1 
ATOM   1623 C  CA  . GLY B 1 73  ? 4.943   -1.086  54.995  1.00 26.21 ? 72   GLY B CA  1 
ATOM   1624 C  C   . GLY B 1 73  ? 4.102   0.112   54.617  1.00 25.55 ? 72   GLY B C   1 
ATOM   1625 O  O   . GLY B 1 73  ? 3.151   -0.015  53.834  1.00 25.67 ? 72   GLY B O   1 
ATOM   1626 N  N   . GLY B 1 74  ? 4.453   1.259   55.191  1.00 26.13 ? 73   GLY B N   1 
ATOM   1627 C  CA  . GLY B 1 74  ? 3.841   2.537   54.839  1.00 25.44 ? 73   GLY B CA  1 
ATOM   1628 C  C   . GLY B 1 74  ? 4.656   3.200   53.720  1.00 24.25 ? 73   GLY B C   1 
ATOM   1629 O  O   . GLY B 1 74  ? 5.836   2.905   53.503  1.00 26.70 ? 73   GLY B O   1 
ATOM   1630 N  N   . PRO B 1 75  ? 4.030   4.096   52.980  1.00 24.19 ? 74   PRO B N   1 
ATOM   1631 C  CA  . PRO B 1 75  ? 4.671   4.746   51.824  1.00 24.16 ? 74   PRO B CA  1 
ATOM   1632 C  C   . PRO B 1 75  ? 6.051   5.322   52.085  1.00 24.53 ? 74   PRO B C   1 
ATOM   1633 O  O   . PRO B 1 75  ? 6.897   5.352   51.197  1.00 26.37 ? 74   PRO B O   1 
ATOM   1634 C  CB  . PRO B 1 75  ? 3.679   5.854   51.448  1.00 23.11 ? 74   PRO B CB  1 
ATOM   1635 C  CG  . PRO B 1 75  ? 2.816   5.986   52.649  1.00 22.03 ? 74   PRO B CG  1 
ATOM   1636 C  CD  . PRO B 1 75  ? 2.654   4.560   53.178  1.00 22.38 ? 74   PRO B CD  1 
ATOM   1637 N  N   . LYS B 1 76  ? 6.306   5.804   53.292  1.00 25.65 ? 75   LYS B N   1 
ATOM   1638 C  CA  . LYS B 1 76  ? 7.615   6.355   53.572  1.00 25.27 ? 75   LYS B CA  1 
ATOM   1639 C  C   . LYS B 1 76  ? 8.628   5.300   53.981  1.00 25.27 ? 75   LYS B C   1 
ATOM   1640 O  O   . LYS B 1 76  ? 9.796   5.599   54.171  1.00 26.95 ? 75   LYS B O   1 
ATOM   1641 C  CB  . LYS B 1 76  ? 7.502   7.469   54.594  1.00 24.47 ? 75   LYS B CB  1 
ATOM   1642 C  CG  . LYS B 1 76  ? 6.444   8.474   54.186  1.00 25.93 ? 75   LYS B CG  1 
ATOM   1643 C  CD  . LYS B 1 76  ? 6.840   9.906   54.569  1.00 26.97 ? 75   LYS B CD  1 
ATOM   1644 N  N   . ASP B 1 77  ? 8.207   4.050   54.078  1.00 25.77 ? 76   ASP B N   1 
ATOM   1645 C  CA  . ASP B 1 77  ? 9.171   3.034   54.466  1.00 25.82 ? 76   ASP B CA  1 
ATOM   1646 C  C   . ASP B 1 77  ? 9.955   2.520   53.282  1.00 26.18 ? 76   ASP B C   1 
ATOM   1647 O  O   . ASP B 1 77  ? 9.427   2.384   52.165  1.00 26.63 ? 76   ASP B O   1 
ATOM   1648 C  CB  . ASP B 1 77  ? 8.504   1.862   55.204  1.00 25.69 ? 76   ASP B CB  1 
ATOM   1649 C  CG  . ASP B 1 77  ? 7.850   2.288   56.499  1.00 25.73 ? 76   ASP B CG  1 
ATOM   1650 O  OD1 . ASP B 1 77  ? 8.524   2.954   57.317  1.00 29.23 ? 76   ASP B OD1 1 
ATOM   1651 O  OD2 . ASP B 1 77  ? 6.664   2.018   56.789  1.00 29.42 ? 76   ASP B OD2 1 
ATOM   1652 N  N   . GLU B 1 78  ? 11.219  2.245   53.554  1.00 27.51 ? 77   GLU B N   1 
ATOM   1653 C  CA  . GLU B 1 78  ? 12.118  1.659   52.584  1.00 28.12 ? 77   GLU B CA  1 
ATOM   1654 C  C   . GLU B 1 78  ? 11.524  0.316   52.191  1.00 28.81 ? 77   GLU B C   1 
ATOM   1655 O  O   . GLU B 1 78  ? 11.425  0.017   51.003  1.00 30.27 ? 77   GLU B O   1 
ATOM   1656 C  CB  . GLU B 1 78  ? 13.524  1.484   53.160  1.00 27.97 ? 77   GLU B CB  1 
ATOM   1657 N  N   . GLU B 1 79  ? 11.124  -0.481  53.178  1.00 28.91 ? 78   GLU B N   1 
ATOM   1658 C  CA  . GLU B 1 79  ? 10.532  -1.794  52.878  1.00 29.11 ? 78   GLU B CA  1 
ATOM   1659 C  C   . GLU B 1 79  ? 9.020   -1.696  52.766  1.00 27.73 ? 78   GLU B C   1 
ATOM   1660 O  O   . GLU B 1 79  ? 8.335   -1.474  53.770  1.00 29.20 ? 78   GLU B O   1 
ATOM   1661 C  CB  . GLU B 1 79  ? 10.924  -2.841  53.917  1.00 29.06 ? 78   GLU B CB  1 
ATOM   1662 C  CG  . GLU B 1 79  ? 10.318  -4.235  53.700  1.00 32.68 ? 78   GLU B CG  1 
ATOM   1663 C  CD  . GLU B 1 79  ? 11.263  -5.216  52.995  1.00 36.22 ? 78   GLU B CD  1 
ATOM   1664 O  OE1 . GLU B 1 79  ? 12.370  -4.793  52.586  1.00 38.71 ? 78   GLU B OE1 1 
ATOM   1665 O  OE2 . GLU B 1 79  ? 10.907  -6.416  52.848  1.00 37.08 ? 78   GLU B OE2 1 
ATOM   1666 N  N   . ARG B 1 80  ? 8.510   -1.819  51.541  1.00 27.25 ? 79   ARG B N   1 
ATOM   1667 C  CA  . ARG B 1 80  ? 7.064   -1.800  51.246  1.00 25.90 ? 79   ARG B CA  1 
ATOM   1668 C  C   . ARG B 1 80  ? 6.795   -2.247  49.846  1.00 25.39 ? 79   ARG B C   1 
ATOM   1669 O  O   . ARG B 1 80  ? 7.688   -2.210  48.994  1.00 28.43 ? 79   ARG B O   1 
ATOM   1670 C  CB  . ARG B 1 80  ? 6.478   -0.392  51.382  1.00 24.63 ? 79   ARG B CB  1 
ATOM   1671 C  CG  . ARG B 1 80  ? 7.248   0.654   50.575  1.00 22.46 ? 79   ARG B CG  1 
ATOM   1672 C  CD  . ARG B 1 80  ? 6.590   1.060   49.327  1.00 29.40 ? 79   ARG B CD  1 
ATOM   1673 N  NE  . ARG B 1 80  ? 6.413   2.506   49.321  1.00 29.55 ? 79   ARG B NE  1 
ATOM   1674 C  CZ  . ARG B 1 80  ? 5.662   3.179   48.468  1.00 25.16 ? 79   ARG B CZ  1 
ATOM   1675 N  NH1 . ARG B 1 80  ? 4.986   2.582   47.499  1.00 27.57 ? 79   ARG B NH1 1 
ATOM   1676 N  NH2 . ARG B 1 80  ? 5.600   4.497   48.579  1.00 26.30 ? 79   ARG B NH2 1 
ATOM   1677 N  N   . HIS B 1 81  ? 5.548   -2.649  49.607  1.00 25.76 ? 80   HIS B N   1 
ATOM   1678 C  CA  . HIS B 1 81  ? 5.072   -2.970  48.272  1.00 23.55 ? 80   HIS B CA  1 
ATOM   1679 C  C   . HIS B 1 81  ? 5.033   -1.690  47.463  1.00 23.78 ? 80   HIS B C   1 
ATOM   1680 O  O   . HIS B 1 81  ? 4.796   -0.591  48.029  1.00 24.14 ? 80   HIS B O   1 
ATOM   1681 C  CB  . HIS B 1 81  ? 3.645   -3.495  48.347  1.00 22.05 ? 80   HIS B CB  1 
ATOM   1682 C  CG  . HIS B 1 81  ? 3.460   -4.646  49.292  1.00 20.77 ? 80   HIS B CG  1 
ATOM   1683 N  ND1 . HIS B 1 81  ? 2.343   -4.782  50.081  1.00 23.53 ? 80   HIS B ND1 1 
ATOM   1684 C  CD2 . HIS B 1 81  ? 4.268   -5.690  49.604  1.00 24.40 ? 80   HIS B CD2 1 
ATOM   1685 C  CE1 . HIS B 1 81  ? 2.442   -5.887  50.794  1.00 21.23 ? 80   HIS B CE1 1 
ATOM   1686 N  NE2 . HIS B 1 81  ? 3.610   -6.447  50.534  1.00 25.93 ? 80   HIS B NE2 1 
ATOM   1687 N  N   . VAL B 1 82  ? 5.182   -1.838  46.145  1.00 24.25 ? 81   VAL B N   1 
ATOM   1688 C  CA  . VAL B 1 82  ? 4.973   -0.717  45.231  1.00 23.51 ? 81   VAL B CA  1 
ATOM   1689 C  C   . VAL B 1 82  ? 3.581   -0.161  45.454  1.00 23.25 ? 81   VAL B C   1 
ATOM   1690 O  O   . VAL B 1 82  ? 3.409   1.037   45.463  1.00 25.42 ? 81   VAL B O   1 
ATOM   1691 C  CB  . VAL B 1 82  ? 5.205   -1.085  43.722  1.00 22.87 ? 81   VAL B CB  1 
ATOM   1692 C  CG1 . VAL B 1 82  ? 4.562   -0.045  42.800  1.00 23.57 ? 81   VAL B CG1 1 
ATOM   1693 C  CG2 . VAL B 1 82  ? 6.728   -1.221  43.389  1.00 22.52 ? 81   VAL B CG2 1 
ATOM   1694 N  N   . GLY B 1 83  ? 2.587   -1.010  45.721  1.00 22.84 ? 82   GLY B N   1 
ATOM   1695 C  CA  . GLY B 1 83  ? 1.225   -0.534  45.924  1.00 22.84 ? 82   GLY B CA  1 
ATOM   1696 C  C   . GLY B 1 83  ? 0.841   0.044   47.281  1.00 21.77 ? 82   GLY B C   1 
ATOM   1697 O  O   . GLY B 1 83  ? -0.319  0.283   47.508  1.00 25.85 ? 82   GLY B O   1 
ATOM   1698 N  N   . ASP B 1 84  ? 1.809   0.260   48.170  1.00 22.62 ? 83   ASP B N   1 
ATOM   1699 C  CA  . ASP B 1 84  ? 1.543   0.724   49.541  1.00 21.70 ? 83   ASP B CA  1 
ATOM   1700 C  C   . ASP B 1 84  ? 1.462   2.244   49.632  1.00 21.82 ? 83   ASP B C   1 
ATOM   1701 O  O   . ASP B 1 84  ? 2.475   2.905   49.890  1.00 24.31 ? 83   ASP B O   1 
ATOM   1702 C  CB  . ASP B 1 84  ? 2.641   0.246   50.472  1.00 22.41 ? 83   ASP B CB  1 
ATOM   1703 C  CG  . ASP B 1 84  ? 2.520   -1.246  50.792  1.00 19.91 ? 83   ASP B CG  1 
ATOM   1704 O  OD1 . ASP B 1 84  ? 1.446   -1.784  50.502  1.00 25.48 ? 83   ASP B OD1 1 
ATOM   1705 O  OD2 . ASP B 1 84  ? 3.427   -1.914  51.307  1.00 25.99 ? 83   ASP B OD2 1 
ATOM   1706 N  N   . LEU B 1 85  ? 0.275   2.784   49.472  1.00 22.88 ? 84   LEU B N   1 
ATOM   1707 C  CA  . LEU B 1 85  ? 0.075   4.227   49.503  1.00 22.50 ? 84   LEU B CA  1 
ATOM   1708 C  C   . LEU B 1 85  ? -0.569  4.683   50.821  1.00 23.67 ? 84   LEU B C   1 
ATOM   1709 O  O   . LEU B 1 85  ? -1.220  5.722   50.893  1.00 27.15 ? 84   LEU B O   1 
ATOM   1710 C  CB  . LEU B 1 85  ? -0.681  4.677   48.264  1.00 22.73 ? 84   LEU B CB  1 
ATOM   1711 C  CG  . LEU B 1 85  ? -0.118  4.418   46.859  1.00 19.81 ? 84   LEU B CG  1 
ATOM   1712 C  CD1 . LEU B 1 85  ? -0.914  5.187   45.772  1.00 21.04 ? 84   LEU B CD1 1 
ATOM   1713 C  CD2 . LEU B 1 85  ? 1.405   4.547   46.743  1.00 22.30 ? 84   LEU B CD2 1 
ATOM   1714 N  N   . GLY B 1 86  ? -0.407  3.890   51.872  1.00 24.60 ? 85   GLY B N   1 
ATOM   1715 C  CA  . GLY B 1 86  ? -0.843  4.265   53.210  1.00 24.10 ? 85   GLY B CA  1 
ATOM   1716 C  C   . GLY B 1 86  ? -2.347  4.284   53.452  1.00 24.16 ? 85   GLY B C   1 
ATOM   1717 O  O   . GLY B 1 86  ? -3.060  3.301   53.223  1.00 24.52 ? 85   GLY B O   1 
ATOM   1718 N  N   . ASN B 1 87  ? -2.823  5.447   53.886  1.00 24.99 ? 86   ASN B N   1 
ATOM   1719 C  CA  . ASN B 1 87  ? -4.196  5.650   54.289  1.00 25.10 ? 86   ASN B CA  1 
ATOM   1720 C  C   . ASN B 1 87  ? -4.656  6.967   53.790  1.00 25.10 ? 86   ASN B C   1 
ATOM   1721 O  O   . ASN B 1 87  ? -3.841  7.900   53.611  1.00 26.55 ? 86   ASN B O   1 
ATOM   1722 C  CB  . ASN B 1 87  ? -4.310  5.775   55.814  1.00 24.87 ? 86   ASN B CB  1 
ATOM   1723 C  CG  . ASN B 1 87  ? -4.023  4.503   56.517  1.00 26.07 ? 86   ASN B CG  1 
ATOM   1724 O  OD1 . ASN B 1 87  ? -4.771  3.525   56.393  1.00 24.63 ? 86   ASN B OD1 1 
ATOM   1725 N  ND2 . ASN B 1 87  ? -2.909  4.476   57.241  1.00 29.37 ? 86   ASN B ND2 1 
ATOM   1726 N  N   . VAL B 1 88  ? -5.955  7.052   53.577  1.00 26.21 ? 87   VAL B N   1 
ATOM   1727 C  CA  . VAL B 1 88  ? -6.541  8.337   53.279  1.00 26.11 ? 87   VAL B CA  1 
ATOM   1728 C  C   . VAL B 1 88  ? -7.426  8.682   54.464  1.00 26.76 ? 87   VAL B C   1 
ATOM   1729 O  O   . VAL B 1 88  ? -7.845  7.808   55.221  1.00 28.32 ? 87   VAL B O   1 
ATOM   1730 C  CB  . VAL B 1 88  ? -7.320  8.349   51.950  1.00 25.00 ? 87   VAL B CB  1 
ATOM   1731 C  CG1 . VAL B 1 88  ? -6.374  8.102   50.761  1.00 25.24 ? 87   VAL B CG1 1 
ATOM   1732 C  CG2 . VAL B 1 88  ? -8.524  7.393   51.991  1.00 23.78 ? 87   VAL B CG2 1 
ATOM   1733 N  N   . THR B 1 89  ? -7.753  9.955   54.635  1.00 28.14 ? 88   THR B N   1 
ATOM   1734 C  CA  . THR B 1 89  ? -8.492  10.327  55.835  1.00 28.32 ? 88   THR B CA  1 
ATOM   1735 C  C   . THR B 1 89  ? -9.893  10.877  55.601  1.00 27.62 ? 88   THR B C   1 
ATOM   1736 O  O   . THR B 1 89  ? -10.093 11.957  55.039  1.00 29.08 ? 88   THR B O   1 
ATOM   1737 C  CB  . THR B 1 89  ? -7.642  11.279  56.728  1.00 27.83 ? 88   THR B CB  1 
ATOM   1738 O  OG1 . THR B 1 89  ? -6.480  10.596  57.213  1.00 30.85 ? 88   THR B OG1 1 
ATOM   1739 C  CG2 . THR B 1 89  ? -8.384  11.606  58.023  1.00 29.19 ? 88   THR B CG2 1 
ATOM   1740 N  N   . ALA B 1 90  ? -10.882 10.112  56.026  1.00 27.62 ? 89   ALA B N   1 
ATOM   1741 C  CA  . ALA B 1 90  ? -12.258 10.565  55.905  1.00 26.34 ? 89   ALA B CA  1 
ATOM   1742 C  C   . ALA B 1 90  ? -12.715 11.441  57.080  1.00 25.91 ? 89   ALA B C   1 
ATOM   1743 O  O   . ALA B 1 90  ? -12.512 11.094  58.256  1.00 26.00 ? 89   ALA B O   1 
ATOM   1744 C  CB  . ALA B 1 90  ? -13.193 9.366   55.699  1.00 26.47 ? 89   ALA B CB  1 
ATOM   1745 N  N   . ASP B 1 91  ? -13.339 12.571  56.752  1.00 25.87 ? 90   ASP B N   1 
ATOM   1746 C  CA  . ASP B 1 91  ? -13.884 13.480  57.767  1.00 26.27 ? 90   ASP B CA  1 
ATOM   1747 C  C   . ASP B 1 91  ? -15.186 12.995  58.425  1.00 26.34 ? 90   ASP B C   1 
ATOM   1748 O  O   . ASP B 1 91  ? -15.623 11.866  58.191  1.00 26.58 ? 90   ASP B O   1 
ATOM   1749 C  CB  . ASP B 1 91  ? -13.994 14.940  57.256  1.00 26.39 ? 90   ASP B CB  1 
ATOM   1750 C  CG  . ASP B 1 91  ? -15.060 15.146  56.162  1.00 27.06 ? 90   ASP B CG  1 
ATOM   1751 O  OD1 . ASP B 1 91  ? -15.894 14.256  55.905  1.00 27.51 ? 90   ASP B OD1 1 
ATOM   1752 O  OD2 . ASP B 1 91  ? -15.148 16.215  55.510  1.00 28.95 ? 90   ASP B OD2 1 
ATOM   1753 N  N   . LYS B 1 92  ? -15.786 13.840  59.255  1.00 26.54 ? 91   LYS B N   1 
ATOM   1754 C  CA  . LYS B 1 92  ? -17.007 13.479  59.962  1.00 26.46 ? 91   LYS B CA  1 
ATOM   1755 C  C   . LYS B 1 92  ? -18.140 13.176  58.996  1.00 26.64 ? 91   LYS B C   1 
ATOM   1756 O  O   . LYS B 1 92  ? -19.058 12.422  59.326  1.00 27.23 ? 91   LYS B O   1 
ATOM   1757 C  CB  . LYS B 1 92  ? -17.417 14.556  60.978  1.00 26.52 ? 91   LYS B CB  1 
ATOM   1758 C  CG  . LYS B 1 92  ? -17.768 15.951  60.425  1.00 26.60 ? 91   LYS B CG  1 
ATOM   1759 C  CD  . LYS B 1 92  ? -18.381 16.802  61.555  1.00 29.75 ? 91   LYS B CD  1 
ATOM   1760 C  CE  . LYS B 1 92  ? -18.529 18.296  61.248  1.00 28.84 ? 91   LYS B CE  1 
ATOM   1761 N  N   . ASP B 1 93  ? -18.060 13.733  57.790  1.00 26.88 ? 92   ASP B N   1 
ATOM   1762 C  CA  . ASP B 1 93  ? -19.110 13.531  56.797  1.00 26.53 ? 92   ASP B CA  1 
ATOM   1763 C  C   . ASP B 1 93  ? -18.846 12.387  55.806  1.00 25.82 ? 92   ASP B C   1 
ATOM   1764 O  O   . ASP B 1 93  ? -19.572 12.227  54.815  1.00 26.77 ? 92   ASP B O   1 
ATOM   1765 C  CB  . ASP B 1 93  ? -19.371 14.831  56.034  1.00 26.88 ? 92   ASP B CB  1 
ATOM   1766 C  CG  . ASP B 1 93  ? -19.992 15.923  56.910  1.00 27.37 ? 92   ASP B CG  1 
ATOM   1767 O  OD1 . ASP B 1 93  ? -20.919 15.642  57.707  1.00 28.43 ? 92   ASP B OD1 1 
ATOM   1768 O  OD2 . ASP B 1 93  ? -19.633 17.120  56.842  1.00 30.90 ? 92   ASP B OD2 1 
ATOM   1769 N  N   . GLY B 1 94  ? -17.805 11.603  56.050  1.00 25.35 ? 93   GLY B N   1 
ATOM   1770 C  CA  . GLY B 1 94  ? -17.461 10.501  55.171  1.00 24.62 ? 93   GLY B CA  1 
ATOM   1771 C  C   . GLY B 1 94  ? -16.667 10.892  53.925  1.00 24.30 ? 93   GLY B C   1 
ATOM   1772 O  O   . GLY B 1 94  ? -16.472 10.076  53.019  1.00 25.06 ? 93   GLY B O   1 
ATOM   1773 N  N   . VAL B 1 95  ? -16.210 12.143  53.880  1.00 24.69 ? 94   VAL B N   1 
ATOM   1774 C  CA  . VAL B 1 95  ? -15.451 12.646  52.741  1.00 24.99 ? 94   VAL B CA  1 
ATOM   1775 C  C   . VAL B 1 95  ? -13.937 12.657  52.990  1.00 26.11 ? 94   VAL B C   1 
ATOM   1776 O  O   . VAL B 1 95  ? -13.447 13.243  53.967  1.00 26.87 ? 94   VAL B O   1 
ATOM   1777 C  CB  . VAL B 1 95  ? -15.915 14.056  52.309  1.00 24.61 ? 94   VAL B CB  1 
ATOM   1778 C  CG1 . VAL B 1 95  ? -15.191 14.493  51.057  1.00 24.89 ? 94   VAL B CG1 1 
ATOM   1779 C  CG2 . VAL B 1 95  ? -17.417 14.080  52.071  1.00 24.41 ? 94   VAL B CG2 1 
ATOM   1780 N  N   . ALA B 1 96  ? -13.192 12.000  52.104  1.00 26.89 ? 95   ALA B N   1 
ATOM   1781 C  CA  . ALA B 1 96  ? -11.738 11.983  52.235  1.00 27.11 ? 95   ALA B CA  1 
ATOM   1782 C  C   . ALA B 1 96  ? -11.075 12.705  51.088  1.00 27.44 ? 95   ALA B C   1 
ATOM   1783 O  O   . ALA B 1 96  ? -11.187 12.318  49.910  1.00 29.51 ? 95   ALA B O   1 
ATOM   1784 C  CB  . ALA B 1 96  ? -11.184 10.558  52.387  1.00 25.43 ? 95   ALA B CB  1 
ATOM   1785 N  N   . ASP B 1 97  ? -10.389 13.779  51.426  1.00 28.64 ? 96   ASP B N   1 
ATOM   1786 C  CA  . ASP B 1 97  ? -9.673  14.540  50.417  1.00 29.13 ? 96   ASP B CA  1 
ATOM   1787 C  C   . ASP B 1 97  ? -8.295  13.893  50.204  1.00 29.07 ? 96   ASP B C   1 
ATOM   1788 O  O   . ASP B 1 97  ? -7.558  13.674  51.157  1.00 30.27 ? 96   ASP B O   1 
ATOM   1789 C  CB  . ASP B 1 97  ? -9.539  15.972  50.888  1.00 28.98 ? 96   ASP B CB  1 
ATOM   1790 C  CG  . ASP B 1 97  ? -9.217  16.912  49.769  1.00 31.32 ? 96   ASP B CG  1 
ATOM   1791 O  OD1 . ASP B 1 97  ? -10.156 17.571  49.268  1.00 36.66 ? 96   ASP B OD1 1 
ATOM   1792 O  OD2 . ASP B 1 97  ? -8.060  17.071  49.326  1.00 36.59 ? 96   ASP B OD2 1 
ATOM   1793 N  N   . VAL B 1 98  ? -7.951  13.529  48.978  1.00 29.51 ? 97   VAL B N   1 
ATOM   1794 C  CA  . VAL B 1 98  ? -6.665  12.873  48.768  1.00 29.41 ? 97   VAL B CA  1 
ATOM   1795 C  C   . VAL B 1 98  ? -5.649  13.794  48.144  1.00 29.76 ? 97   VAL B C   1 
ATOM   1796 O  O   . VAL B 1 98  ? -5.932  14.441  47.139  1.00 30.28 ? 97   VAL B O   1 
ATOM   1797 C  CB  . VAL B 1 98  ? -6.804  11.618  47.889  1.00 29.35 ? 97   VAL B CB  1 
ATOM   1798 C  CG1 . VAL B 1 98  ? -5.439  10.946  47.666  1.00 28.59 ? 97   VAL B CG1 1 
ATOM   1799 C  CG2 . VAL B 1 98  ? -7.799  10.669  48.505  1.00 29.48 ? 97   VAL B CG2 1 
ATOM   1800 N  N   . SER B 1 99  ? -4.479  13.879  48.777  1.00 30.07 ? 98   SER B N   1 
ATOM   1801 C  CA  . SER B 1 99  ? -3.340  14.590  48.197  1.00 30.26 ? 98   SER B CA  1 
ATOM   1802 C  C   . SER B 1 99  ? -2.033  13.939  48.644  1.00 29.56 ? 98   SER B C   1 
ATOM   1803 O  O   . SER B 1 99  ? -1.532  14.196  49.750  1.00 31.05 ? 98   SER B O   1 
ATOM   1804 C  CB  . SER B 1 99  ? -3.384  16.079  48.512  1.00 30.45 ? 98   SER B CB  1 
ATOM   1805 O  OG  . SER B 1 99  ? -3.158  16.825  47.322  1.00 33.35 ? 98   SER B OG  1 
ATOM   1806 N  N   . ILE B 1 100 ? -1.496  13.102  47.754  1.00 29.39 ? 99   ILE B N   1 
ATOM   1807 C  CA  . ILE B 1 100 ? -0.324  12.275  47.973  1.00 27.60 ? 99   ILE B CA  1 
ATOM   1808 C  C   . ILE B 1 100 ? 0.684   12.441  46.861  1.00 27.33 ? 99   ILE B C   1 
ATOM   1809 O  O   . ILE B 1 100 ? 0.345   12.625  45.690  1.00 28.62 ? 99   ILE B O   1 
ATOM   1810 C  CB  . ILE B 1 100 ? -0.730  10.777  47.986  1.00 27.32 ? 99   ILE B CB  1 
ATOM   1811 C  CG1 . ILE B 1 100 ? -1.464  10.423  49.264  1.00 26.87 ? 99   ILE B CG1 1 
ATOM   1812 C  CG2 . ILE B 1 100 ? 0.497   9.908   47.863  1.00 28.34 ? 99   ILE B CG2 1 
ATOM   1813 C  CD1 . ILE B 1 100 ? -2.436  9.224   49.109  1.00 22.83 ? 99   ILE B CD1 1 
ATOM   1814 N  N   . GLU B 1 101 ? 1.943   12.353  47.239  1.00 26.79 ? 100  GLU B N   1 
ATOM   1815 C  CA  . GLU B 1 101 ? 3.018   12.343  46.295  1.00 26.23 ? 100  GLU B CA  1 
ATOM   1816 C  C   . GLU B 1 101 ? 3.899   11.136  46.604  1.00 25.02 ? 100  GLU B C   1 
ATOM   1817 O  O   . GLU B 1 101 ? 4.385   10.985  47.732  1.00 26.56 ? 100  GLU B O   1 
ATOM   1818 C  CB  . GLU B 1 101 ? 3.786   13.660  46.367  1.00 25.24 ? 100  GLU B CB  1 
ATOM   1819 C  CG  . GLU B 1 101 ? 4.609   13.938  45.120  1.00 29.91 ? 100  GLU B CG  1 
ATOM   1820 C  CD  . GLU B 1 101 ? 5.290   15.306  45.115  1.00 33.60 ? 100  GLU B CD  1 
ATOM   1821 O  OE1 . GLU B 1 101 ? 6.504   15.357  45.429  1.00 35.42 ? 100  GLU B OE1 1 
ATOM   1822 O  OE2 . GLU B 1 101 ? 4.621   16.324  44.780  1.00 36.31 ? 100  GLU B OE2 1 
ATOM   1823 N  N   . ASP B 1 102 ? 4.070   10.280  45.596  1.00 24.05 ? 101  ASP B N   1 
ATOM   1824 C  CA  . ASP B 1 102 ? 4.849   9.039   45.689  1.00 22.45 ? 101  ASP B CA  1 
ATOM   1825 C  C   . ASP B 1 102 ? 5.914   8.830   44.589  1.00 22.09 ? 101  ASP B C   1 
ATOM   1826 O  O   . ASP B 1 102 ? 5.644   9.023   43.410  1.00 22.82 ? 101  ASP B O   1 
ATOM   1827 C  CB  . ASP B 1 102 ? 3.871   7.852   45.669  1.00 21.69 ? 101  ASP B CB  1 
ATOM   1828 C  CG  . ASP B 1 102 ? 4.478   6.608   46.264  1.00 20.18 ? 101  ASP B CG  1 
ATOM   1829 O  OD1 . ASP B 1 102 ? 4.632   6.589   47.488  1.00 23.92 ? 101  ASP B OD1 1 
ATOM   1830 O  OD2 . ASP B 1 102 ? 4.851   5.622   45.583  1.00 26.09 ? 101  ASP B OD2 1 
ATOM   1831 N  N   . SER B 1 103 ? 7.075   8.300   44.976  1.00 22.19 ? 102  SER B N   1 
ATOM   1832 C  CA  . SER B 1 103 ? 8.214   8.106   44.097  1.00 22.96 ? 102  SER B CA  1 
ATOM   1833 C  C   . SER B 1 103 ? 8.518   6.634   43.832  1.00 21.65 ? 102  SER B C   1 
ATOM   1834 O  O   . SER B 1 103 ? 9.536   6.300   43.261  1.00 24.08 ? 102  SER B O   1 
ATOM   1835 C  CB  . SER B 1 103 ? 9.431   8.740   44.704  1.00 21.52 ? 102  SER B CB  1 
ATOM   1836 O  OG  . SER B 1 103 ? 9.365   10.171  44.618  1.00 27.13 ? 102  SER B OG  1 
ATOM   1837 N  N   . VAL B 1 104 ? 7.661   5.779   44.338  1.00 22.91 ? 103  VAL B N   1 
ATOM   1838 C  CA  . VAL B 1 104 ? 7.800   4.344   44.109  1.00 21.25 ? 103  VAL B CA  1 
ATOM   1839 C  C   . VAL B 1 104 ? 6.874   3.888   42.991  1.00 21.27 ? 103  VAL B C   1 
ATOM   1840 O  O   . VAL B 1 104 ? 7.307   3.138   42.123  1.00 24.00 ? 103  VAL B O   1 
ATOM   1841 C  CB  . VAL B 1 104 ? 7.573   3.564   45.383  1.00 18.85 ? 103  VAL B CB  1 
ATOM   1842 C  CG1 . VAL B 1 104 ? 7.735   2.049   45.103  1.00 21.19 ? 103  VAL B CG1 1 
ATOM   1843 C  CG2 . VAL B 1 104 ? 8.583   4.013   46.447  1.00 20.53 ? 103  VAL B CG2 1 
ATOM   1844 N  N   . ILE B 1 105 ? 5.603   4.285   43.020  1.00 22.47 ? 104  ILE B N   1 
ATOM   1845 C  CA  . ILE B 1 105 ? 4.720   4.037   41.898  1.00 20.97 ? 104  ILE B CA  1 
ATOM   1846 C  C   . ILE B 1 105 ? 5.203   4.813   40.657  1.00 21.73 ? 104  ILE B C   1 
ATOM   1847 O  O   . ILE B 1 105 ? 5.948   5.795   40.774  1.00 23.67 ? 104  ILE B O   1 
ATOM   1848 C  CB  . ILE B 1 105 ? 3.238   4.313   42.231  1.00 21.25 ? 104  ILE B CB  1 
ATOM   1849 C  CG1 . ILE B 1 105 ? 2.986   5.784   42.611  1.00 17.76 ? 104  ILE B CG1 1 
ATOM   1850 C  CG2 . ILE B 1 105 ? 2.748   3.386   43.229  1.00 17.91 ? 104  ILE B CG2 1 
ATOM   1851 C  CD1 . ILE B 1 105 ? 1.535   6.128   42.551  1.00 20.98 ? 104  ILE B CD1 1 
ATOM   1852 N  N   . SER B 1 106 ? 4.872   4.298   39.483  1.00 22.36 ? 105  SER B N   1 
ATOM   1853 C  CA  . SER B 1 106 ? 5.049   4.951   38.206  1.00 22.38 ? 105  SER B CA  1 
ATOM   1854 C  C   . SER B 1 106 ? 3.855   4.744   37.283  1.00 20.95 ? 105  SER B C   1 
ATOM   1855 O  O   . SER B 1 106 ? 3.018   3.816   37.436  1.00 25.10 ? 105  SER B O   1 
ATOM   1856 C  CB  . SER B 1 106 ? 6.339   4.497   37.511  1.00 20.17 ? 105  SER B CB  1 
ATOM   1857 O  OG  . SER B 1 106 ? 6.775   5.461   36.590  1.00 26.75 ? 105  SER B OG  1 
ATOM   1858 N  N   . LEU B 1 107 ? 3.743   5.686   36.381  1.00 22.92 ? 106  LEU B N   1 
ATOM   1859 C  CA  . LEU B 1 107 ? 2.802   5.682   35.293  1.00 21.26 ? 106  LEU B CA  1 
ATOM   1860 C  C   . LEU B 1 107 ? 3.432   5.053   34.027  1.00 22.74 ? 106  LEU B C   1 
ATOM   1861 O  O   . LEU B 1 107 ? 2.803   5.023   32.946  1.00 25.24 ? 106  LEU B O   1 
ATOM   1862 C  CB  . LEU B 1 107 ? 2.312   7.128   35.064  1.00 19.79 ? 106  LEU B CB  1 
ATOM   1863 C  CG  . LEU B 1 107 ? 1.409   7.702   36.184  1.00 18.52 ? 106  LEU B CG  1 
ATOM   1864 C  CD1 . LEU B 1 107 ? 0.580   9.035   35.763  1.00 18.18 ? 106  LEU B CD1 1 
ATOM   1865 C  CD2 . LEU B 1 107 ? 0.455   6.629   36.814  1.00 21.15 ? 106  LEU B CD2 1 
ATOM   1866 N  N   . SER B 1 108 ? 4.648   4.522   34.166  1.00 24.53 ? 107  SER B N   1 
ATOM   1867 C  CA  . SER B 1 108 ? 5.373   3.847   33.071  1.00 26.11 ? 107  SER B CA  1 
ATOM   1868 C  C   . SER B 1 108 ? 6.438   2.888   33.636  1.00 26.61 ? 107  SER B C   1 
ATOM   1869 O  O   . SER B 1 108 ? 6.703   2.922   34.834  1.00 26.54 ? 107  SER B O   1 
ATOM   1870 C  CB  . SER B 1 108 ? 5.982   4.816   32.029  1.00 25.25 ? 107  SER B CB  1 
ATOM   1871 O  OG  . SER B 1 108 ? 6.690   5.938   32.585  1.00 27.83 ? 107  SER B OG  1 
ATOM   1872 N  N   . GLY B 1 109 ? 7.015   2.033   32.775  1.00 28.44 ? 108  GLY B N   1 
ATOM   1873 C  CA  . GLY B 1 109 ? 8.024   1.038   33.163  1.00 29.70 ? 108  GLY B CA  1 
ATOM   1874 C  C   . GLY B 1 109 ? 7.530   -0.147  34.007  1.00 31.05 ? 108  GLY B C   1 
ATOM   1875 O  O   . GLY B 1 109 ? 6.352   -0.455  33.965  1.00 32.13 ? 108  GLY B O   1 
ATOM   1876 N  N   . ASP B 1 110 ? 8.426   -0.790  34.774  1.00 32.54 ? 109  ASP B N   1 
ATOM   1877 C  CA  . ASP B 1 110 ? 8.080   -1.931  35.663  1.00 33.08 ? 109  ASP B CA  1 
ATOM   1878 C  C   . ASP B 1 110 ? 7.146   -1.658  36.870  1.00 32.26 ? 109  ASP B C   1 
ATOM   1879 O  O   . ASP B 1 110 ? 6.358   -2.521  37.245  1.00 33.20 ? 109  ASP B O   1 
ATOM   1880 C  CB  . ASP B 1 110 ? 9.336   -2.624  36.244  1.00 33.90 ? 109  ASP B CB  1 
ATOM   1881 C  CG  . ASP B 1 110 ? 10.244  -3.242  35.191  1.00 36.78 ? 109  ASP B CG  1 
ATOM   1882 O  OD1 . ASP B 1 110 ? 9.772   -3.698  34.102  1.00 40.15 ? 109  ASP B OD1 1 
ATOM   1883 O  OD2 . ASP B 1 110 ? 11.485  -3.322  35.398  1.00 40.69 ? 109  ASP B OD2 1 
ATOM   1884 N  N   . HIS B 1 111 ? 7.273   -0.498  37.506  1.00 30.97 ? 110  HIS B N   1 
ATOM   1885 C  CA  . HIS B 1 111 ? 6.438   -0.122  38.644  1.00 30.34 ? 110  HIS B CA  1 
ATOM   1886 C  C   . HIS B 1 111 ? 5.114   0.518   38.122  1.00 29.21 ? 110  HIS B C   1 
ATOM   1887 O  O   . HIS B 1 111 ? 4.388   1.183   38.895  1.00 29.68 ? 110  HIS B O   1 
ATOM   1888 C  CB  . HIS B 1 111 ? 7.188   0.882   39.596  1.00 30.30 ? 110  HIS B CB  1 
ATOM   1889 C  CG  . HIS B 1 111 ? 8.303   0.280   40.422  1.00 29.74 ? 110  HIS B CG  1 
ATOM   1890 N  ND1 . HIS B 1 111 ? 9.011   1.014   41.355  1.00 29.78 ? 110  HIS B ND1 1 
ATOM   1891 C  CD2 . HIS B 1 111 ? 8.819   -0.978  40.470  1.00 29.41 ? 110  HIS B CD2 1 
ATOM   1892 C  CE1 . HIS B 1 111 ? 9.907   0.238   41.941  1.00 29.22 ? 110  HIS B CE1 1 
ATOM   1893 N  NE2 . HIS B 1 111 ? 9.825   -0.970  41.407  1.00 29.76 ? 110  HIS B NE2 1 
ATOM   1894 N  N   . CYS B 1 112 ? 4.854   0.366   36.810  1.00 28.35 ? 111  CYS B N   1 
ATOM   1895 C  CA  . CYS B 1 112 ? 3.682   0.951   36.152  1.00 27.18 ? 111  CYS B CA  1 
ATOM   1896 C  C   . CYS B 1 112 ? 2.370   0.439   36.713  1.00 24.75 ? 111  CYS B C   1 
ATOM   1897 O  O   . CYS B 1 112 ? 2.133   -0.765  36.742  1.00 25.72 ? 111  CYS B O   1 
ATOM   1898 C  CB  . CYS B 1 112 ? 3.716   0.788   34.635  1.00 25.87 ? 111  CYS B CB  1 
ATOM   1899 S  SG  . CYS B 1 112 ? 2.265   1.442   33.796  1.00 31.46 ? 111  CYS B SG  1 
ATOM   1900 N  N   . ILE B 1 113 ? 1.526   1.361   37.133  1.00 23.06 ? 112  ILE B N   1 
ATOM   1901 C  CA  . ILE B 1 113 ? 0.243   1.020   37.725  1.00 20.52 ? 112  ILE B CA  1 
ATOM   1902 C  C   . ILE B 1 113 ? -0.953  1.226   36.823  1.00 20.97 ? 112  ILE B C   1 
ATOM   1903 O  O   . ILE B 1 113 ? -2.060  0.985   37.267  1.00 22.71 ? 112  ILE B O   1 
ATOM   1904 C  CB  . ILE B 1 113 ? 0.021   1.761   39.067  1.00 19.18 ? 112  ILE B CB  1 
ATOM   1905 C  CG1 . ILE B 1 113 ? -0.124  3.304   38.836  1.00 12.14 ? 112  ILE B CG1 1 
ATOM   1906 C  CG2 . ILE B 1 113 ? 1.097   1.325   40.209  1.00 21.17 ? 112  ILE B CG2 1 
ATOM   1907 C  CD1 . ILE B 1 113 ? -0.431  4.013   40.179  1.00 15.43 ? 112  ILE B CD1 1 
ATOM   1908 N  N   . ILE B 1 114 ? -0.729  1.709   35.587  1.00 21.78 ? 113  ILE B N   1 
ATOM   1909 C  CA  . ILE B 1 114 ? -1.802  1.861   34.594  1.00 20.54 ? 113  ILE B CA  1 
ATOM   1910 C  C   . ILE B 1 114 ? -2.314  0.457   34.331  1.00 20.15 ? 113  ILE B C   1 
ATOM   1911 O  O   . ILE B 1 114 ? -1.528  -0.430  34.030  1.00 23.23 ? 113  ILE B O   1 
ATOM   1912 C  CB  . ILE B 1 114 ? -1.246  2.332   33.253  1.00 17.70 ? 113  ILE B CB  1 
ATOM   1913 C  CG1 . ILE B 1 114 ? -0.667  3.748   33.341  1.00 21.86 ? 113  ILE B CG1 1 
ATOM   1914 C  CG2 . ILE B 1 114 ? -2.374  2.390   32.252  1.00 20.26 ? 113  ILE B CG2 1 
ATOM   1915 C  CD1 . ILE B 1 114 ? -1.603  4.637   34.078  1.00 24.60 ? 113  ILE B CD1 1 
ATOM   1916 N  N   . GLY B 1 115 ? -3.606  0.240   34.439  1.00 23.06 ? 114  GLY B N   1 
ATOM   1917 C  CA  . GLY B 1 115 ? -4.128  -1.093  34.181  1.00 22.04 ? 114  GLY B CA  1 
ATOM   1918 C  C   . GLY B 1 115 ? -4.169  -1.929  35.426  1.00 20.40 ? 114  GLY B C   1 
ATOM   1919 O  O   . GLY B 1 115 ? -4.506  -3.128  35.397  1.00 21.38 ? 114  GLY B O   1 
ATOM   1920 N  N   . ARG B 1 116 ? -3.759  -1.369  36.558  1.00 21.28 ? 115  ARG B N   1 
ATOM   1921 C  CA  . ARG B 1 116 ? -3.887  -2.140  37.760  1.00 20.19 ? 115  ARG B CA  1 
ATOM   1922 C  C   . ARG B 1 116 ? -5.079  -1.482  38.459  1.00 21.53 ? 115  ARG B C   1 
ATOM   1923 O  O   . ARG B 1 116 ? -5.717  -0.577  37.876  1.00 25.46 ? 115  ARG B O   1 
ATOM   1924 C  CB  . ARG B 1 116 ? -2.560  -2.180  38.550  1.00 16.92 ? 115  ARG B CB  1 
ATOM   1925 C  CG  . ARG B 1 116 ? -1.409  -2.821  37.699  1.00 14.61 ? 115  ARG B CG  1 
ATOM   1926 C  CD  . ARG B 1 116 ? -0.156  -3.279  38.494  1.00 13.56 ? 115  ARG B CD  1 
ATOM   1927 N  NE  . ARG B 1 116 ? 0.892   -3.561  37.561  1.00 16.26 ? 115  ARG B NE  1 
ATOM   1928 C  CZ  . ARG B 1 116 ? 1.163   -4.794  37.150  1.00 15.69 ? 115  ARG B CZ  1 
ATOM   1929 N  NH1 . ARG B 1 116 ? 0.439   -5.788  37.622  1.00 23.35 ? 115  ARG B NH1 1 
ATOM   1930 N  NH2 . ARG B 1 116 ? 2.140   -5.012  36.287  1.00 19.06 ? 115  ARG B NH2 1 
ATOM   1931 N  N   . THR B 1 117 ? -5.378  -1.929  39.670  1.00 21.87 ? 116  THR B N   1 
ATOM   1932 C  CA  . THR B 1 117 ? -6.518  -1.491  40.453  1.00 20.92 ? 116  THR B CA  1 
ATOM   1933 C  C   . THR B 1 117 ? -6.174  -0.728  41.734  1.00 20.42 ? 116  THR B C   1 
ATOM   1934 O  O   . THR B 1 117 ? -5.316  -1.092  42.546  1.00 24.59 ? 116  THR B O   1 
ATOM   1935 C  CB  . THR B 1 117 ? -7.438  -2.741  40.775  1.00 17.35 ? 116  THR B CB  1 
ATOM   1936 O  OG1 . THR B 1 117 ? -8.009  -3.252  39.592  1.00 22.23 ? 116  THR B OG1 1 
ATOM   1937 C  CG2 . THR B 1 117 ? -8.667  -2.398  41.723  1.00 17.44 ? 116  THR B CG2 1 
ATOM   1938 N  N   . LEU B 1 118 ? -6.794  0.415   41.868  1.00 22.50 ? 117  LEU B N   1 
ATOM   1939 C  CA  . LEU B 1 118 ? -6.777  1.173   43.086  1.00 19.86 ? 117  LEU B CA  1 
ATOM   1940 C  C   . LEU B 1 118 ? -7.968  0.770   43.998  1.00 21.04 ? 117  LEU B C   1 
ATOM   1941 O  O   . LEU B 1 118 ? -9.096  0.663   43.535  1.00 24.38 ? 117  LEU B O   1 
ATOM   1942 C  CB  . LEU B 1 118 ? -6.822  2.649   42.689  1.00 17.23 ? 117  LEU B CB  1 
ATOM   1943 C  CG  . LEU B 1 118 ? -6.735  3.521   43.954  1.00 14.02 ? 117  LEU B CG  1 
ATOM   1944 C  CD1 . LEU B 1 118 ? -5.455  3.362   44.710  1.00 21.79 ? 117  LEU B CD1 1 
ATOM   1945 C  CD2 . LEU B 1 118 ? -6.922  5.065   43.592  1.00 15.16 ? 117  LEU B CD2 1 
ATOM   1946 N  N   . VAL B 1 119 ? -7.720  0.517   45.286  1.00 22.06 ? 118  VAL B N   1 
ATOM   1947 C  CA  . VAL B 1 119 ? -8.719  0.084   46.276  1.00 22.39 ? 118  VAL B CA  1 
ATOM   1948 C  C   . VAL B 1 119 ? -8.668  0.903   47.571  1.00 21.13 ? 118  VAL B C   1 
ATOM   1949 O  O   . VAL B 1 119 ? -7.570  1.131   48.144  1.00 24.91 ? 118  VAL B O   1 
ATOM   1950 C  CB  . VAL B 1 119 ? -8.446  -1.347  46.764  1.00 21.91 ? 118  VAL B CB  1 
ATOM   1951 C  CG1 . VAL B 1 119 ? -9.423  -1.734  47.914  1.00 20.40 ? 118  VAL B CG1 1 
ATOM   1952 C  CG2 . VAL B 1 119 ? -8.449  -2.353  45.617  1.00 20.69 ? 118  VAL B CG2 1 
ATOM   1953 N  N   . VAL B 1 120 ? -9.819  1.406   47.987  1.00 22.38 ? 119  VAL B N   1 
ATOM   1954 C  CA  . VAL B 1 120 ? -9.956  1.956   49.320  1.00 21.91 ? 119  VAL B CA  1 
ATOM   1955 C  C   . VAL B 1 120 ? -10.542 0.881   50.251  1.00 20.81 ? 119  VAL B C   1 
ATOM   1956 O  O   . VAL B 1 120 ? -11.636 0.319   49.989  1.00 24.52 ? 119  VAL B O   1 
ATOM   1957 C  CB  . VAL B 1 120 ? -10.747 3.257   49.312  1.00 20.38 ? 119  VAL B CB  1 
ATOM   1958 C  CG1 . VAL B 1 120 ? -12.114 3.051   48.653  1.00 20.23 ? 119  VAL B CG1 1 
ATOM   1959 C  CG2 . VAL B 1 120 ? -10.835 3.789   50.706  1.00 20.81 ? 119  VAL B CG2 1 
ATOM   1960 N  N   . HIS B 1 121 ? -9.824  0.580   51.326  1.00 22.95 ? 120  HIS B N   1 
ATOM   1961 C  CA  . HIS B 1 121 ? -10.219 -0.465  52.291  1.00 22.35 ? 120  HIS B CA  1 
ATOM   1962 C  C   . HIS B 1 121 ? -11.142 -0.095  53.502  1.00 23.30 ? 120  HIS B C   1 
ATOM   1963 O  O   . HIS B 1 121 ? -11.297 1.075   53.907  1.00 25.13 ? 120  HIS B O   1 
ATOM   1964 C  CB  . HIS B 1 121 ? -8.980  -1.227  52.799  1.00 20.16 ? 120  HIS B CB  1 
ATOM   1965 C  CG  . HIS B 1 121 ? -8.278  -2.044  51.757  1.00 19.43 ? 120  HIS B CG  1 
ATOM   1966 N  ND1 . HIS B 1 121 ? -8.374  -3.417  51.712  1.00 26.16 ? 120  HIS B ND1 1 
ATOM   1967 C  CD2 . HIS B 1 121 ? -7.470  -1.690  50.731  1.00 19.20 ? 120  HIS B CD2 1 
ATOM   1968 C  CE1 . HIS B 1 121 ? -7.671  -3.873  50.697  1.00 17.79 ? 120  HIS B CE1 1 
ATOM   1969 N  NE2 . HIS B 1 121 ? -7.098  -2.843  50.090  1.00 24.83 ? 120  HIS B NE2 1 
ATOM   1970 N  N   . GLU B 1 122 ? -11.747 -1.119  54.081  1.00 24.78 ? 121  GLU B N   1 
ATOM   1971 C  CA  . GLU B 1 122 ? -12.648 -0.994  55.220  1.00 24.29 ? 121  GLU B CA  1 
ATOM   1972 C  C   . GLU B 1 122 ? -12.076 -0.227  56.436  1.00 25.08 ? 121  GLU B C   1 
ATOM   1973 O  O   . GLU B 1 122 ? -12.753 0.628   57.016  1.00 27.11 ? 121  GLU B O   1 
ATOM   1974 C  CB  . GLU B 1 122 ? -13.044 -2.406  55.655  1.00 25.30 ? 121  GLU B CB  1 
ATOM   1975 C  CG  . GLU B 1 122 ? -13.721 -2.543  57.019  1.00 24.72 ? 121  GLU B CG  1 
ATOM   1976 C  CD  . GLU B 1 122 ? -14.050 -3.992  57.376  1.00 26.39 ? 121  GLU B CD  1 
ATOM   1977 O  OE1 . GLU B 1 122 ? -14.766 -4.217  58.373  1.00 32.59 ? 121  GLU B OE1 1 
ATOM   1978 O  OE2 . GLU B 1 122 ? -13.615 -4.921  56.667  1.00 28.61 ? 121  GLU B OE2 1 
ATOM   1979 N  N   . LYS B 1 123 ? -10.847 -0.548  56.825  1.00 25.56 ? 122  LYS B N   1 
ATOM   1980 C  CA  . LYS B 1 123 ? -10.226 0.046   58.007  1.00 25.98 ? 122  LYS B CA  1 
ATOM   1981 C  C   . LYS B 1 123 ? -8.880  0.680   57.707  1.00 25.38 ? 122  LYS B C   1 
ATOM   1982 O  O   . LYS B 1 123 ? -8.362  0.636   56.593  1.00 26.28 ? 122  LYS B O   1 
ATOM   1983 C  CB  . LYS B 1 123 ? -9.967  -1.019  59.070  1.00 25.68 ? 122  LYS B CB  1 
ATOM   1984 C  CG  . LYS B 1 123 ? -11.170 -1.844  59.469  1.00 27.67 ? 122  LYS B CG  1 
ATOM   1985 C  CD  . LYS B 1 123 ? -10.721 -3.228  60.001  1.00 29.56 ? 122  LYS B CD  1 
ATOM   1986 N  N   . ALA B 1 124 ? -8.298  1.235   58.750  1.00 26.81 ? 123  ALA B N   1 
ATOM   1987 C  CA  . ALA B 1 124 ? -6.971  1.802   58.693  1.00 26.14 ? 123  ALA B CA  1 
ATOM   1988 C  C   . ALA B 1 124 ? -5.869  0.783   58.371  1.00 25.89 ? 123  ALA B C   1 
ATOM   1989 O  O   . ALA B 1 124 ? -5.871  -0.345  58.850  1.00 26.90 ? 123  ALA B O   1 
ATOM   1990 C  CB  . ALA B 1 124 ? -6.679  2.506   59.968  1.00 25.80 ? 123  ALA B CB  1 
ATOM   1991 N  N   . ASP B 1 125 ? -5.003  1.166   57.453  1.00 26.02 ? 124  ASP B N   1 
ATOM   1992 C  CA  . ASP B 1 125 ? -3.806  0.386   57.150  1.00 25.45 ? 124  ASP B CA  1 
ATOM   1993 C  C   . ASP B 1 125 ? -2.813  0.617   58.299  1.00 24.94 ? 124  ASP B C   1 
ATOM   1994 O  O   . ASP B 1 125 ? -2.361  1.761   58.525  1.00 26.13 ? 124  ASP B O   1 
ATOM   1995 C  CB  . ASP B 1 125 ? -3.257  0.841   55.805  1.00 25.95 ? 124  ASP B CB  1 
ATOM   1996 C  CG  . ASP B 1 125 ? -1.949  0.177   55.445  1.00 23.63 ? 124  ASP B CG  1 
ATOM   1997 O  OD1 . ASP B 1 125 ? -1.496  -0.725  56.171  1.00 31.44 ? 124  ASP B OD1 1 
ATOM   1998 O  OD2 . ASP B 1 125 ? -1.315  0.493   54.417  1.00 29.41 ? 124  ASP B OD2 1 
ATOM   1999 N  N   . ASP B 1 126 ? -2.490  -0.441  59.057  1.00 23.47 ? 125  ASP B N   1 
ATOM   2000 C  CA  . ASP B 1 126 ? -1.547  -0.324  60.173  1.00 22.76 ? 125  ASP B CA  1 
ATOM   2001 C  C   . ASP B 1 126 ? -0.025  -0.207  59.831  1.00 22.41 ? 125  ASP B C   1 
ATOM   2002 O  O   . ASP B 1 126 ? 0.837   -0.269  60.720  1.00 24.20 ? 125  ASP B O   1 
ATOM   2003 C  CB  . ASP B 1 126 ? -1.816  -1.433  61.195  1.00 21.56 ? 125  ASP B CB  1 
ATOM   2004 C  CG  . ASP B 1 126 ? -1.325  -2.777  60.725  1.00 17.06 ? 125  ASP B CG  1 
ATOM   2005 O  OD1 . ASP B 1 126 ? -0.347  -2.800  59.968  1.00 24.00 ? 125  ASP B OD1 1 
ATOM   2006 O  OD2 . ASP B 1 126 ? -1.836  -3.854  61.081  1.00 21.50 ? 125  ASP B OD2 1 
ATOM   2007 N  N   . LEU B 1 127 ? 0.271   0.008   58.541  1.00 24.59 ? 126  LEU B N   1 
ATOM   2008 C  CA  . LEU B 1 127 ? 1.584   0.219   57.971  1.00 23.94 ? 126  LEU B CA  1 
ATOM   2009 C  C   . LEU B 1 127 ? 2.609   -0.842  58.246  1.00 23.62 ? 126  LEU B C   1 
ATOM   2010 O  O   . LEU B 1 127 ? 3.794   -0.563  58.217  1.00 25.86 ? 126  LEU B O   1 
ATOM   2011 C  CB  . LEU B 1 127 ? 2.142   1.551   58.444  1.00 23.59 ? 126  LEU B CB  1 
ATOM   2012 C  CG  . LEU B 1 127 ? 1.101   2.636   58.260  1.00 21.90 ? 126  LEU B CG  1 
ATOM   2013 C  CD1 . LEU B 1 127 ? 1.793   3.957   58.594  1.00 21.95 ? 126  LEU B CD1 1 
ATOM   2014 C  CD2 . LEU B 1 127 ? 0.556   2.624   56.829  1.00 23.23 ? 126  LEU B CD2 1 
ATOM   2015 N  N   . GLY B 1 128 ? 2.163   -2.066  58.482  1.00 24.57 ? 127  GLY B N   1 
ATOM   2016 C  CA  . GLY B 1 128 ? 3.069   -3.121  58.891  1.00 23.38 ? 127  GLY B CA  1 
ATOM   2017 C  C   . GLY B 1 128 ? 3.424   -3.185  60.382  1.00 23.51 ? 127  GLY B C   1 
ATOM   2018 O  O   . GLY B 1 128 ? 4.184   -4.052  60.771  1.00 25.29 ? 127  GLY B O   1 
ATOM   2019 N  N   . LYS B 1 129 ? 2.887   -2.284  61.217  1.00 24.27 ? 128  LYS B N   1 
ATOM   2020 C  CA  . LYS B 1 129 ? 3.198   -2.248  62.649  1.00 22.92 ? 128  LYS B CA  1 
ATOM   2021 C  C   . LYS B 1 129 ? 2.008   -2.575  63.523  1.00 22.14 ? 128  LYS B C   1 
ATOM   2022 O  O   . LYS B 1 129 ? 1.895   -2.085  64.640  1.00 22.59 ? 128  LYS B O   1 
ATOM   2023 C  CB  . LYS B 1 129 ? 3.709   -0.867  63.053  1.00 23.96 ? 128  LYS B CB  1 
ATOM   2024 C  CG  . LYS B 1 129 ? 4.876   -0.351  62.228  1.00 25.67 ? 128  LYS B CG  1 
ATOM   2025 C  CD  . LYS B 1 129 ? 6.206   -0.953  62.680  1.00 29.48 ? 128  LYS B CD  1 
ATOM   2026 C  CE  . LYS B 1 129 ? 7.375   -0.422  61.847  1.00 32.16 ? 128  LYS B CE  1 
ATOM   2027 N  NZ  . LYS B 1 129 ? 8.447   -1.455  61.723  1.00 34.55 ? 128  LYS B NZ  1 
ATOM   2028 N  N   . GLY B 1 130 ? 1.129   -3.417  63.015  1.00 21.18 ? 129  GLY B N   1 
ATOM   2029 C  CA  . GLY B 1 130 ? -0.060  -3.822  63.742  1.00 19.53 ? 129  GLY B CA  1 
ATOM   2030 C  C   . GLY B 1 130 ? 0.199   -4.948  64.708  1.00 19.61 ? 129  GLY B C   1 
ATOM   2031 O  O   . GLY B 1 130 ? -0.663  -5.302  65.500  1.00 20.29 ? 129  GLY B O   1 
ATOM   2032 N  N   . GLY B 1 131 ? 1.401   -5.506  64.626  1.00 19.78 ? 130  GLY B N   1 
ATOM   2033 C  CA  . GLY B 1 131 ? 1.875   -6.505  65.554  1.00 18.79 ? 130  GLY B CA  1 
ATOM   2034 C  C   . GLY B 1 131 ? 1.375   -7.919  65.393  1.00 18.86 ? 130  GLY B C   1 
ATOM   2035 O  O   . GLY B 1 131 ? 1.304   -8.635  66.371  1.00 20.08 ? 130  GLY B O   1 
ATOM   2036 N  N   . ASN B 1 132 ? 1.049   -8.301  64.160  1.00 21.03 ? 131  ASN B N   1 
ATOM   2037 C  CA  . ASN B 1 132 ? 0.658   -9.680  63.826  1.00 21.13 ? 131  ASN B CA  1 
ATOM   2038 C  C   . ASN B 1 132 ? 1.005   -10.009 62.366  1.00 21.66 ? 131  ASN B C   1 
ATOM   2039 O  O   . ASN B 1 132 ? 1.447   -9.147  61.591  1.00 22.30 ? 131  ASN B O   1 
ATOM   2040 C  CB  . ASN B 1 132 ? -0.820  -10.029 64.186  1.00 21.18 ? 131  ASN B CB  1 
ATOM   2041 C  CG  . ASN B 1 132 ? -1.872  -9.223  63.402  1.00 19.29 ? 131  ASN B CG  1 
ATOM   2042 O  OD1 . ASN B 1 132 ? -1.678  -8.821  62.262  1.00 19.73 ? 131  ASN B OD1 1 
ATOM   2043 N  ND2 . ASN B 1 132 ? -3.037  -9.055  64.013  1.00 24.39 ? 131  ASN B ND2 1 
ATOM   2044 N  N   . GLU B 1 133 ? 0.830   -11.267 61.990  1.00 22.97 ? 132  GLU B N   1 
ATOM   2045 C  CA  . GLU B 1 133 ? 1.166   -11.710 60.644  1.00 24.05 ? 132  GLU B CA  1 
ATOM   2046 C  C   . GLU B 1 133 ? 0.429   -10.988 59.502  1.00 23.74 ? 132  GLU B C   1 
ATOM   2047 O  O   . GLU B 1 133 ? 1.030   -10.615 58.486  1.00 24.48 ? 132  GLU B O   1 
ATOM   2048 C  CB  . GLU B 1 133 ? 0.971   -13.220 60.561  1.00 24.18 ? 132  GLU B CB  1 
ATOM   2049 C  CG  . GLU B 1 133 ? 1.409   -13.800 59.234  1.00 28.69 ? 132  GLU B CG  1 
ATOM   2050 C  CD  . GLU B 1 133 ? 1.312   -15.308 59.227  1.00 34.03 ? 132  GLU B CD  1 
ATOM   2051 O  OE1 . GLU B 1 133 ? 0.216   -15.832 59.564  1.00 37.25 ? 132  GLU B OE1 1 
ATOM   2052 O  OE2 . GLU B 1 133 ? 2.334   -15.968 58.911  1.00 38.06 ? 132  GLU B OE2 1 
ATOM   2053 N  N   . GLU B 1 134 ? -0.869  -10.769 59.676  1.00 23.77 ? 133  GLU B N   1 
ATOM   2054 C  CA  . GLU B 1 134 ? -1.683  -10.101 58.681  1.00 24.55 ? 133  GLU B CA  1 
ATOM   2055 C  C   . GLU B 1 134 ? -1.181  -8.676  58.486  1.00 23.74 ? 133  GLU B C   1 
ATOM   2056 O  O   . GLU B 1 134 ? -1.245  -8.128  57.393  1.00 24.74 ? 133  GLU B O   1 
ATOM   2057 C  CB  . GLU B 1 134 ? -3.164  -10.119 59.100  1.00 23.94 ? 133  GLU B CB  1 
ATOM   2058 C  CG  . GLU B 1 134 ? -4.157  -9.886  57.978  1.00 27.19 ? 133  GLU B CG  1 
ATOM   2059 C  CD  . GLU B 1 134 ? -3.856  -10.719 56.743  1.00 29.18 ? 133  GLU B CD  1 
ATOM   2060 O  OE1 . GLU B 1 134 ? -3.836  -11.973 56.836  1.00 34.06 ? 133  GLU B OE1 1 
ATOM   2061 O  OE2 . GLU B 1 134 ? -3.630  -10.111 55.687  1.00 30.88 ? 133  GLU B OE2 1 
ATOM   2062 N  N   . SER B 1 135 ? -0.637  -8.100  59.546  1.00 23.82 ? 134  SER B N   1 
ATOM   2063 C  CA  . SER B 1 135 ? -0.110  -6.734  59.480  1.00 23.44 ? 134  SER B CA  1 
ATOM   2064 C  C   . SER B 1 135 ? 1.019   -6.613  58.431  1.00 24.07 ? 134  SER B C   1 
ATOM   2065 O  O   . SER B 1 135 ? 1.052   -5.653  57.649  1.00 24.71 ? 134  SER B O   1 
ATOM   2066 C  CB  . SER B 1 135 ? 0.375   -6.294  60.863  1.00 21.68 ? 134  SER B CB  1 
ATOM   2067 O  OG  . SER B 1 135 ? 0.991   -5.009  60.827  1.00 22.27 ? 134  SER B OG  1 
ATOM   2068 N  N   . THR B 1 136 ? 1.907   -7.603  58.389  1.00 24.80 ? 135  THR B N   1 
ATOM   2069 C  CA  . THR B 1 136 ? 3.025   -7.595  57.441  1.00 26.25 ? 135  THR B CA  1 
ATOM   2070 C  C   . THR B 1 136 ? 2.618   -7.966  56.034  1.00 26.66 ? 135  THR B C   1 
ATOM   2071 O  O   . THR B 1 136 ? 3.487   -8.193  55.194  1.00 28.91 ? 135  THR B O   1 
ATOM   2072 C  CB  . THR B 1 136 ? 4.120   -8.584  57.851  1.00 25.37 ? 135  THR B CB  1 
ATOM   2073 O  OG1 . THR B 1 136 ? 3.577   -9.909  57.885  1.00 28.28 ? 135  THR B OG1 1 
ATOM   2074 C  CG2 . THR B 1 136 ? 4.584   -8.358  59.280  1.00 26.76 ? 135  THR B CG2 1 
ATOM   2075 N  N   . LYS B 1 137 ? 1.318   -8.051  55.792  1.00 27.70 ? 136  LYS B N   1 
ATOM   2076 C  CA  . LYS B 1 137 ? 0.773   -8.409  54.488  1.00 27.66 ? 136  LYS B CA  1 
ATOM   2077 C  C   . LYS B 1 137 ? -0.225  -7.418  53.915  1.00 28.10 ? 136  LYS B C   1 
ATOM   2078 O  O   . LYS B 1 137 ? -0.084  -6.990  52.766  1.00 29.18 ? 136  LYS B O   1 
ATOM   2079 C  CB  . LYS B 1 137 ? 0.139   -9.792  54.531  1.00 27.69 ? 136  LYS B CB  1 
ATOM   2080 C  CG  . LYS B 1 137 ? 1.126   -10.912 54.510  1.00 28.72 ? 136  LYS B CG  1 
ATOM   2081 C  CD  . LYS B 1 137 ? 0.373   -12.232 54.584  1.00 31.21 ? 136  LYS B CD  1 
ATOM   2082 C  CE  . LYS B 1 137 ? 1.080   -13.241 55.472  1.00 31.53 ? 136  LYS B CE  1 
ATOM   2083 N  NZ  . LYS B 1 137 ? 0.252   -14.476 55.659  1.00 33.29 ? 136  LYS B NZ  1 
ATOM   2084 N  N   . THR B 1 138 ? -1.262  -7.086  54.678  1.00 29.13 ? 137  THR B N   1 
ATOM   2085 C  CA  . THR B 1 138 ? -2.286  -6.169  54.193  1.00 29.22 ? 137  THR B CA  1 
ATOM   2086 C  C   . THR B 1 138 ? -2.400  -4.942  55.070  1.00 28.66 ? 137  THR B C   1 
ATOM   2087 O  O   . THR B 1 138 ? -3.186  -4.034  54.779  1.00 29.29 ? 137  THR B O   1 
ATOM   2088 C  CB  . THR B 1 138 ? -3.665  -6.839  54.186  1.00 29.37 ? 137  THR B CB  1 
ATOM   2089 O  OG1 . THR B 1 138 ? -3.979  -7.307  55.504  1.00 31.93 ? 137  THR B OG1 1 
ATOM   2090 C  CG2 . THR B 1 138 ? -3.665  -8.102  53.337  1.00 28.72 ? 137  THR B CG2 1 
ATOM   2091 N  N   . GLY B 1 139 ? -1.645  -4.947  56.166  1.00 28.03 ? 138  GLY B N   1 
ATOM   2092 C  CA  . GLY B 1 139 ? -1.735  -3.892  57.158  1.00 26.31 ? 138  GLY B CA  1 
ATOM   2093 C  C   . GLY B 1 139 ? -3.057  -3.920  57.906  1.00 25.71 ? 138  GLY B C   1 
ATOM   2094 O  O   . GLY B 1 139 ? -3.462  -2.911  58.488  1.00 25.61 ? 138  GLY B O   1 
ATOM   2095 N  N   . ASN B 1 140 ? -3.731  -5.073  57.897  1.00 25.81 ? 139  ASN B N   1 
ATOM   2096 C  CA  . ASN B 1 140 ? -5.038  -5.199  58.512  1.00 27.01 ? 139  ASN B CA  1 
ATOM   2097 C  C   . ASN B 1 140 ? -6.062  -4.171  58.046  1.00 26.39 ? 139  ASN B C   1 
ATOM   2098 O  O   . ASN B 1 140 ? -6.852  -3.679  58.852  1.00 27.29 ? 139  ASN B O   1 
ATOM   2099 C  CB  . ASN B 1 140 ? -4.908  -5.088  60.032  1.00 27.00 ? 139  ASN B CB  1 
ATOM   2100 C  CG  . ASN B 1 140 ? -4.245  -6.290  60.642  1.00 29.12 ? 139  ASN B CG  1 
ATOM   2101 O  OD1 . ASN B 1 140 ? -4.754  -7.414  60.531  1.00 30.71 ? 139  ASN B OD1 1 
ATOM   2102 N  ND2 . ASN B 1 140 ? -3.103  -6.071  61.301  1.00 29.36 ? 139  ASN B ND2 1 
ATOM   2103 N  N   . ALA B 1 141 ? -6.069  -3.851  56.763  1.00 26.44 ? 140  ALA B N   1 
ATOM   2104 C  CA  . ALA B 1 141 ? -6.953  -2.793  56.287  1.00 25.72 ? 140  ALA B CA  1 
ATOM   2105 C  C   . ALA B 1 141 ? -8.377  -3.298  56.029  1.00 25.13 ? 140  ALA B C   1 
ATOM   2106 O  O   . ALA B 1 141 ? -9.306  -2.516  55.777  1.00 25.87 ? 140  ALA B O   1 
ATOM   2107 C  CB  . ALA B 1 141 ? -6.362  -2.128  55.069  1.00 26.01 ? 140  ALA B CB  1 
ATOM   2108 N  N   . GLY B 1 142 ? -8.556  -4.617  56.132  1.00 25.46 ? 141  GLY B N   1 
ATOM   2109 C  CA  . GLY B 1 142 ? -9.866  -5.209  56.010  1.00 24.91 ? 141  GLY B CA  1 
ATOM   2110 C  C   . GLY B 1 142 ? -10.398 -5.267  54.594  1.00 24.70 ? 141  GLY B C   1 
ATOM   2111 O  O   . GLY B 1 142 ? -9.624  -5.324  53.607  1.00 25.63 ? 141  GLY B O   1 
ATOM   2112 N  N   . SER B 1 143 ? -11.720 -5.237  54.488  1.00 24.47 ? 142  SER B N   1 
ATOM   2113 C  CA  . SER B 1 143 ? -12.386 -5.435  53.195  1.00 23.81 ? 142  SER B CA  1 
ATOM   2114 C  C   . SER B 1 143 ? -12.221 -4.332  52.104  1.00 22.48 ? 142  SER B C   1 
ATOM   2115 O  O   . SER B 1 143 ? -11.717 -3.225  52.338  1.00 23.37 ? 142  SER B O   1 
ATOM   2116 C  CB  . SER B 1 143 ? -13.847 -5.848  53.394  1.00 23.83 ? 142  SER B CB  1 
ATOM   2117 O  OG  . SER B 1 143 ? -14.656 -4.719  53.704  1.00 28.98 ? 142  SER B OG  1 
ATOM   2118 N  N   . ARG B 1 144 ? -12.604 -4.658  50.892  1.00 23.01 ? 143  ARG B N   1 
ATOM   2119 C  CA  . ARG B 1 144 ? -12.484 -3.679  49.816  1.00 21.62 ? 143  ARG B CA  1 
ATOM   2120 C  C   . ARG B 1 144 ? -13.799 -2.883  49.702  1.00 21.25 ? 143  ARG B C   1 
ATOM   2121 O  O   . ARG B 1 144 ? -14.818 -3.387  49.271  1.00 23.94 ? 143  ARG B O   1 
ATOM   2122 C  CB  . ARG B 1 144 ? -12.050 -4.374  48.527  1.00 19.73 ? 143  ARG B CB  1 
ATOM   2123 C  CG  . ARG B 1 144 ? -10.973 -5.423  48.825  1.00 20.80 ? 143  ARG B CG  1 
ATOM   2124 C  CD  . ARG B 1 144 ? -10.430 -6.208  47.617  1.00 20.62 ? 143  ARG B CD  1 
ATOM   2125 N  NE  . ARG B 1 144 ? -9.296  -6.976  48.091  1.00 25.08 ? 143  ARG B NE  1 
ATOM   2126 C  CZ  . ARG B 1 144 ? -8.401  -7.644  47.363  1.00 21.28 ? 143  ARG B CZ  1 
ATOM   2127 N  NH1 . ARG B 1 144 ? -8.436  -7.682  46.020  1.00 23.21 ? 143  ARG B NH1 1 
ATOM   2128 N  NH2 . ARG B 1 144 ? -7.457  -8.298  48.026  1.00 22.93 ? 143  ARG B NH2 1 
ATOM   2129 N  N   . LEU B 1 145 ? -13.791 -1.617  50.085  1.00 21.44 ? 144  LEU B N   1 
ATOM   2130 C  CA  . LEU B 1 145 ? -14.996 -0.823  49.948  1.00 20.60 ? 144  LEU B CA  1 
ATOM   2131 C  C   . LEU B 1 145 ? -15.361 -0.362  48.517  1.00 20.69 ? 144  LEU B C   1 
ATOM   2132 O  O   . LEU B 1 145 ? -16.523 -0.437  48.153  1.00 23.44 ? 144  LEU B O   1 
ATOM   2133 C  CB  . LEU B 1 145 ? -14.953 0.394   50.868  1.00 18.78 ? 144  LEU B CB  1 
ATOM   2134 C  CG  . LEU B 1 145 ? -14.824 0.142   52.377  1.00 18.55 ? 144  LEU B CG  1 
ATOM   2135 C  CD1 . LEU B 1 145 ? -14.547 1.462   53.179  1.00 15.25 ? 144  LEU B CD1 1 
ATOM   2136 C  CD2 . LEU B 1 145 ? -16.020 -0.580  52.978  1.00 15.48 ? 144  LEU B CD2 1 
ATOM   2137 N  N   . ALA B 1 146 ? -14.399 0.145   47.753  1.00 21.40 ? 145  ALA B N   1 
ATOM   2138 C  CA  . ALA B 1 146 ? -14.567 0.582   46.366  1.00 20.23 ? 145  ALA B CA  1 
ATOM   2139 C  C   . ALA B 1 146 ? -13.224 0.417   45.632  1.00 20.25 ? 145  ALA B C   1 
ATOM   2140 O  O   . ALA B 1 146 ? -12.129 0.395   46.253  1.00 23.85 ? 145  ALA B O   1 
ATOM   2141 C  CB  . ALA B 1 146 ? -15.081 2.064   46.254  1.00 16.02 ? 145  ALA B CB  1 
ATOM   2142 N  N   . CYS B 1 147 ? -13.310 0.260   44.322  1.00 22.69 ? 146  CYS B N   1 
ATOM   2143 C  CA  . CYS B 1 147 ? -12.168 0.108   43.428  1.00 22.48 ? 146  CYS B CA  1 
ATOM   2144 C  C   . CYS B 1 147 ? -12.467 0.515   41.986  1.00 21.34 ? 146  CYS B C   1 
ATOM   2145 O  O   . CYS B 1 147 ? -13.630 0.630   41.550  1.00 23.18 ? 146  CYS B O   1 
ATOM   2146 C  CB  . CYS B 1 147 ? -11.603 -1.332  43.461  1.00 20.77 ? 146  CYS B CB  1 
ATOM   2147 S  SG  . CYS B 1 147 ? -12.819 -2.512  42.942  1.00 30.05 ? 146  CYS B SG  1 
ATOM   2148 N  N   . GLY B 1 148 ? -11.382 0.662   41.238  1.00 21.70 ? 147  GLY B N   1 
ATOM   2149 C  CA  . GLY B 1 148 ? -11.389 1.050   39.837  1.00 20.74 ? 147  GLY B CA  1 
ATOM   2150 C  C   . GLY B 1 148 ? -10.074 0.767   39.212  1.00 19.10 ? 147  GLY B C   1 
ATOM   2151 O  O   . GLY B 1 148 ? -9.001  0.880   39.867  1.00 21.07 ? 147  GLY B O   1 
ATOM   2152 N  N   . VAL B 1 149 ? -10.153 0.435   37.921  1.00 19.97 ? 148  VAL B N   1 
ATOM   2153 C  CA  . VAL B 1 149 ? -8.985  0.153   37.122  1.00 19.30 ? 148  VAL B CA  1 
ATOM   2154 C  C   . VAL B 1 149 ? -8.335  1.518   36.820  1.00 17.46 ? 148  VAL B C   1 
ATOM   2155 O  O   . VAL B 1 149 ? -9.030  2.493   36.586  1.00 22.94 ? 148  VAL B O   1 
ATOM   2156 C  CB  . VAL B 1 149 ? -9.321  -0.679  35.870  1.00 17.79 ? 148  VAL B CB  1 
ATOM   2157 C  CG1 . VAL B 1 149 ? -8.109  -0.874  34.975  1.00 17.60 ? 148  VAL B CG1 1 
ATOM   2158 C  CG2 . VAL B 1 149 ? -9.983  -2.016  36.272  1.00 18.86 ? 148  VAL B CG2 1 
ATOM   2159 N  N   . ILE B 1 150 ? -7.044  1.584   36.949  1.00 18.45 ? 149  ILE B N   1 
ATOM   2160 C  CA  . ILE B 1 150 ? -6.297  2.805   36.671  1.00 17.64 ? 149  ILE B CA  1 
ATOM   2161 C  C   . ILE B 1 150 ? -6.150  2.958   35.156  1.00 16.94 ? 149  ILE B C   1 
ATOM   2162 O  O   . ILE B 1 150 ? -5.526  2.130   34.464  1.00 22.05 ? 149  ILE B O   1 
ATOM   2163 C  CB  . ILE B 1 150 ? -5.001  2.783   37.423  1.00 14.69 ? 149  ILE B CB  1 
ATOM   2164 C  CG1 . ILE B 1 150 ? -5.253  2.666   38.936  1.00 16.30 ? 149  ILE B CG1 1 
ATOM   2165 C  CG2 . ILE B 1 150 ? -4.050  4.015   37.003  1.00 11.18 ? 149  ILE B CG2 1 
ATOM   2166 C  CD1 . ILE B 1 150 ? -4.012  2.558   39.639  1.00 14.78 ? 149  ILE B CD1 1 
ATOM   2167 N  N   . GLY B 1 151 ? -6.685  4.044   34.613  1.00 18.10 ? 150  GLY B N   1 
ATOM   2168 C  CA  . GLY B 1 151 ? -6.729  4.206   33.185  1.00 19.50 ? 150  GLY B CA  1 
ATOM   2169 C  C   . GLY B 1 151 ? -5.958  5.388   32.684  1.00 19.98 ? 150  GLY B C   1 
ATOM   2170 O  O   . GLY B 1 151 ? -5.768  6.347   33.452  1.00 23.05 ? 150  GLY B O   1 
ATOM   2171 N  N   . ILE B 1 152 ? -5.489  5.294   31.444  1.00 22.34 ? 151  ILE B N   1 
ATOM   2172 C  CA  . ILE B 1 152 ? -4.788  6.381   30.756  1.00 20.54 ? 151  ILE B CA  1 
ATOM   2173 C  C   . ILE B 1 152 ? -5.727  7.573   30.626  1.00 21.56 ? 151  ILE B C   1 
ATOM   2174 O  O   . ILE B 1 152 ? -6.846  7.461   30.126  1.00 23.56 ? 151  ILE B O   1 
ATOM   2175 C  CB  . ILE B 1 152 ? -4.253  6.001   29.370  1.00 19.92 ? 151  ILE B CB  1 
ATOM   2176 C  CG1 . ILE B 1 152 ? -3.286  4.811   29.471  1.00 17.04 ? 151  ILE B CG1 1 
ATOM   2177 C  CG2 . ILE B 1 152 ? -3.467  7.197   28.794  1.00 20.62 ? 151  ILE B CG2 1 
ATOM   2178 C  CD1 . ILE B 1 152 ? -2.704  4.493   28.176  1.00 18.19 ? 151  ILE B CD1 1 
ATOM   2179 N  N   . ALA B 1 153 ? -5.266  8.716   31.091  1.00 22.62 ? 152  ALA B N   1 
ATOM   2180 C  CA  . ALA B 1 153 ? -6.081  9.923   31.043  1.00 22.46 ? 152  ALA B CA  1 
ATOM   2181 C  C   . ALA B 1 153 ? -5.512  11.030  30.106  1.00 24.22 ? 152  ALA B C   1 
ATOM   2182 O  O   . ALA B 1 153 ? -4.319  11.031  29.767  1.00 25.14 ? 152  ALA B O   1 
ATOM   2183 C  CB  . ALA B 1 153 ? -6.292  10.407  32.471  1.00 19.86 ? 152  ALA B CB  1 
ATOM   2184 N  N   . GLN B 1 154 ? -6.384  11.931  29.652  1.00 26.31 ? 153  GLN B N   1 
ATOM   2185 C  CA  . GLN B 1 154 ? -6.037  13.002  28.724  1.00 28.86 ? 153  GLN B CA  1 
ATOM   2186 C  C   . GLN B 1 154 ? -5.183  14.059  29.417  1.00 29.16 ? 153  GLN B C   1 
ATOM   2187 O  O   . GLN B 1 154 ? -5.481  14.585  30.492  1.00 30.58 ? 153  GLN B O   1 
ATOM   2188 C  CB  . GLN B 1 154 ? -7.305  13.615  28.132  1.00 28.52 ? 153  GLN B CB  1 
ATOM   2189 C  CG  . GLN B 1 154 ? -7.103  14.555  26.966  1.00 32.00 ? 153  GLN B CG  1 
ATOM   2190 C  CD  . GLN B 1 154 ? -8.431  14.967  26.327  1.00 35.36 ? 153  GLN B CD  1 
ATOM   2191 O  OE1 . GLN B 1 154 ? -9.470  15.009  27.009  1.00 37.85 ? 153  GLN B OE1 1 
ATOM   2192 N  NE2 . GLN B 1 154 ? -8.408  15.240  25.023  1.00 37.05 ? 153  GLN B NE2 1 
ATOM   2193 O  OXT . GLN B 1 154 ? -4.115  14.375  28.918  1.00 30.28 ? 153  GLN B OXT 1 
ATOM   2194 N  N   . ALA C 1 2   ? 15.309  2.096   27.313  1.00 31.84 ? 1    ALA C N   1 
ATOM   2195 C  CA  . ALA C 1 2   ? 16.540  1.263   27.547  1.00 30.27 ? 1    ALA C CA  1 
ATOM   2196 C  C   . ALA C 1 2   ? 17.005  1.181   28.994  1.00 29.28 ? 1    ALA C C   1 
ATOM   2197 O  O   . ALA C 1 2   ? 16.881  2.110   29.774  1.00 30.22 ? 1    ALA C O   1 
ATOM   2198 C  CB  . ALA C 1 2   ? 17.678  1.707   26.664  1.00 30.58 ? 1    ALA C CB  1 
ATOM   2199 N  N   . THR C 1 3   ? 17.576  0.050   29.343  1.00 27.46 ? 2    THR C N   1 
ATOM   2200 C  CA  . THR C 1 3   ? 18.119  -0.098  30.673  1.00 26.15 ? 2    THR C CA  1 
ATOM   2201 C  C   . THR C 1 3   ? 19.637  0.087   30.655  1.00 24.75 ? 2    THR C C   1 
ATOM   2202 O  O   . THR C 1 3   ? 20.253  0.325   31.718  1.00 26.87 ? 2    THR C O   1 
ATOM   2203 C  CB  . THR C 1 3   ? 17.760  -1.477  31.268  1.00 24.31 ? 2    THR C CB  1 
ATOM   2204 O  OG1 . THR C 1 3   ? 18.385  -2.506  30.494  1.00 27.93 ? 2    THR C OG1 1 
ATOM   2205 C  CG2 . THR C 1 3   ? 16.274  -1.786  31.139  1.00 24.84 ? 2    THR C CG2 1 
ATOM   2206 N  N   . LYS C 1 4   ? 20.252  -0.074  29.485  1.00 22.88 ? 3    LYS C N   1 
ATOM   2207 C  CA  . LYS C 1 4   ? 21.710  0.101   29.364  1.00 23.57 ? 3    LYS C CA  1 
ATOM   2208 C  C   . LYS C 1 4   ? 22.139  1.021   28.217  1.00 21.51 ? 3    LYS C C   1 
ATOM   2209 O  O   . LYS C 1 4   ? 21.605  0.969   27.104  1.00 23.57 ? 3    LYS C O   1 
ATOM   2210 C  CB  . LYS C 1 4   ? 22.449  -1.230  29.187  1.00 23.32 ? 3    LYS C CB  1 
ATOM   2211 C  CG  . LYS C 1 4   ? 22.318  -2.196  30.313  1.00 29.19 ? 3    LYS C CG  1 
ATOM   2212 C  CD  . LYS C 1 4   ? 23.568  -3.060  30.409  1.00 35.51 ? 3    LYS C CD  1 
ATOM   2213 C  CE  . LYS C 1 4   ? 24.100  -3.048  31.832  1.00 38.52 ? 3    LYS C CE  1 
ATOM   2214 N  NZ  . LYS C 1 4   ? 25.575  -3.360  31.900  1.00 42.47 ? 3    LYS C NZ  1 
ATOM   2215 N  N   . ALA C 1 5   ? 23.138  1.837   28.498  1.00 23.52 ? 4    ALA C N   1 
ATOM   2216 C  CA  . ALA C 1 5   ? 23.774  2.693   27.542  1.00 20.46 ? 4    ALA C CA  1 
ATOM   2217 C  C   . ALA C 1 5   ? 25.316  2.713   27.769  1.00 20.06 ? 4    ALA C C   1 
ATOM   2218 O  O   . ALA C 1 5   ? 25.819  2.371   28.837  1.00 22.40 ? 4    ALA C O   1 
ATOM   2219 C  CB  . ALA C 1 5   ? 23.159  4.142   27.554  1.00 19.65 ? 4    ALA C CB  1 
ATOM   2220 N  N   . VAL C 1 6   ? 26.008  3.131   26.737  1.00 21.14 ? 5    VAL C N   1 
ATOM   2221 C  CA  . VAL C 1 6   ? 27.443  3.237   26.632  1.00 20.89 ? 5    VAL C CA  1 
ATOM   2222 C  C   . VAL C 1 6   ? 27.893  4.417   25.703  1.00 20.72 ? 5    VAL C C   1 
ATOM   2223 O  O   . VAL C 1 6   ? 27.248  4.776   24.666  1.00 23.35 ? 5    VAL C O   1 
ATOM   2224 C  CB  . VAL C 1 6   ? 28.013  1.965   26.007  1.00 18.51 ? 5    VAL C CB  1 
ATOM   2225 C  CG1 . VAL C 1 6   ? 27.819  2.033   24.458  1.00 18.78 ? 5    VAL C CG1 1 
ATOM   2226 C  CG2 . VAL C 1 6   ? 29.530  1.859   26.283  1.00 21.36 ? 5    VAL C CG2 1 
ATOM   2227 N  N   . CYS C 1 7   ? 29.047  4.965   26.054  1.00 21.44 ? 6    CYS C N   1 
ATOM   2228 C  CA  . CYS C 1 7   ? 29.666  6.057   25.387  1.00 20.67 ? 6    CYS C CA  1 
ATOM   2229 C  C   . CYS C 1 7   ? 31.197  5.947   25.338  1.00 18.73 ? 6    CYS C C   1 
ATOM   2230 O  O   . CYS C 1 7   ? 31.850  5.693   26.345  1.00 23.17 ? 6    CYS C O   1 
ATOM   2231 C  CB  . CYS C 1 7   ? 29.240  7.327   26.096  1.00 18.90 ? 6    CYS C CB  1 
ATOM   2232 S  SG  . CYS C 1 7   ? 29.933  8.748   25.374  1.00 27.92 ? 6    CYS C SG  1 
ATOM   2233 N  N   . VAL C 1 8   ? 31.728  6.109   24.144  1.00 20.33 ? 7    VAL C N   1 
ATOM   2234 C  CA  . VAL C 1 8   ? 33.143  6.221   23.840  1.00 19.16 ? 7    VAL C CA  1 
ATOM   2235 C  C   . VAL C 1 8   ? 33.508  7.709   23.726  1.00 20.56 ? 7    VAL C C   1 
ATOM   2236 O  O   . VAL C 1 8   ? 32.973  8.423   22.897  1.00 23.41 ? 7    VAL C O   1 
ATOM   2237 C  CB  . VAL C 1 8   ? 33.512  5.510   22.546  1.00 17.65 ? 7    VAL C CB  1 
ATOM   2238 C  CG1 . VAL C 1 8   ? 35.031  5.665   22.184  1.00 18.08 ? 7    VAL C CG1 1 
ATOM   2239 C  CG2 . VAL C 1 8   ? 33.082  3.945   22.615  1.00 16.70 ? 7    VAL C CG2 1 
ATOM   2240 N  N   . LEU C 1 9   ? 34.467  8.108   24.548  1.00 23.79 ? 8    LEU C N   1 
ATOM   2241 C  CA  . LEU C 1 9   ? 34.959  9.504   24.592  1.00 23.39 ? 8    LEU C CA  1 
ATOM   2242 C  C   . LEU C 1 9   ? 36.239  9.605   23.815  1.00 23.94 ? 8    LEU C C   1 
ATOM   2243 O  O   . LEU C 1 9   ? 37.204  8.872   24.074  1.00 26.12 ? 8    LEU C O   1 
ATOM   2244 C  CB  . LEU C 1 9   ? 35.149  9.996   26.049  1.00 23.04 ? 8    LEU C CB  1 
ATOM   2245 C  CG  . LEU C 1 9   ? 34.000  9.767   27.048  1.00 26.26 ? 8    LEU C CG  1 
ATOM   2246 C  CD1 . LEU C 1 9   ? 34.420  9.845   28.457  1.00 27.64 ? 8    LEU C CD1 1 
ATOM   2247 C  CD2 . LEU C 1 9   ? 32.855  10.742  26.810  1.00 24.55 ? 8    LEU C CD2 1 
ATOM   2248 N  N   . LYS C 1 10  ? 36.233  10.484  22.820  1.00 22.62 ? 9    LYS C N   1 
ATOM   2249 C  CA  . LYS C 1 10  ? 37.417  10.833  22.075  1.00 22.79 ? 9    LYS C CA  1 
ATOM   2250 C  C   . LYS C 1 10  ? 37.378  12.334  21.877  1.00 21.78 ? 9    LYS C C   1 
ATOM   2251 O  O   . LYS C 1 10  ? 36.272  12.922  21.844  1.00 23.79 ? 9    LYS C O   1 
ATOM   2252 C  CB  . LYS C 1 10  ? 37.430  10.130  20.728  1.00 22.10 ? 9    LYS C CB  1 
ATOM   2253 C  CG  . LYS C 1 10  ? 37.775  8.628   20.788  1.00 22.72 ? 9    LYS C CG  1 
ATOM   2254 C  CD  . LYS C 1 10  ? 37.909  8.079   19.385  1.00 28.71 ? 9    LYS C CD  1 
ATOM   2255 C  CE  . LYS C 1 10  ? 37.416  6.624   19.281  1.00 29.23 ? 9    LYS C CE  1 
ATOM   2256 N  NZ  . LYS C 1 10  ? 38.331  5.711   19.994  1.00 34.00 ? 9    LYS C NZ  1 
ATOM   2257 N  N   . GLY C 1 11  ? 38.569  12.904  21.718  1.00 23.97 ? 10   GLY C N   1 
ATOM   2258 C  CA  . GLY C 1 11  ? 38.814  14.321  21.446  1.00 23.89 ? 10   GLY C CA  1 
ATOM   2259 C  C   . GLY C 1 11  ? 39.987  14.613  20.514  1.00 24.74 ? 10   GLY C C   1 
ATOM   2260 O  O   . GLY C 1 11  ? 40.535  13.759  19.806  1.00 26.46 ? 10   GLY C O   1 
ATOM   2261 N  N   . ASP C 1 12  ? 40.434  15.855  20.511  1.00 24.77 ? 11   ASP C N   1 
ATOM   2262 C  CA  . ASP C 1 12  ? 41.533  16.189  19.629  1.00 25.24 ? 11   ASP C CA  1 
ATOM   2263 C  C   . ASP C 1 12  ? 42.857  15.744  20.216  1.00 24.23 ? 11   ASP C C   1 
ATOM   2264 O  O   . ASP C 1 12  ? 43.817  15.578  19.478  1.00 26.74 ? 11   ASP C O   1 
ATOM   2265 C  CB  . ASP C 1 12  ? 41.552  17.696  19.366  1.00 25.75 ? 11   ASP C CB  1 
ATOM   2266 C  CG  . ASP C 1 12  ? 40.459  18.110  18.409  1.00 29.72 ? 11   ASP C CG  1 
ATOM   2267 O  OD1 . ASP C 1 12  ? 40.181  17.317  17.487  1.00 35.21 ? 11   ASP C OD1 1 
ATOM   2268 O  OD2 . ASP C 1 12  ? 39.800  19.171  18.502  1.00 34.31 ? 11   ASP C OD2 1 
ATOM   2269 N  N   . GLY C 1 13  ? 42.882  15.544  21.537  1.00 24.57 ? 12   GLY C N   1 
ATOM   2270 C  CA  . GLY C 1 13  ? 44.085  15.184  22.262  1.00 23.34 ? 12   GLY C CA  1 
ATOM   2271 C  C   . GLY C 1 13  ? 44.097  13.712  22.598  1.00 23.16 ? 12   GLY C C   1 
ATOM   2272 O  O   . GLY C 1 13  ? 43.461  12.912  21.928  1.00 23.49 ? 12   GLY C O   1 
ATOM   2273 N  N   . PRO C 1 14  ? 44.782  13.366  23.674  1.00 23.66 ? 13   PRO C N   1 
ATOM   2274 C  CA  . PRO C 1 14  ? 44.901  11.968  24.089  1.00 23.87 ? 13   PRO C CA  1 
ATOM   2275 C  C   . PRO C 1 14  ? 43.788  11.500  25.031  1.00 23.80 ? 13   PRO C C   1 
ATOM   2276 O  O   . PRO C 1 14  ? 43.792  10.318  25.439  1.00 26.14 ? 13   PRO C O   1 
ATOM   2277 C  CB  . PRO C 1 14  ? 46.247  11.957  24.810  1.00 23.24 ? 13   PRO C CB  1 
ATOM   2278 C  CG  . PRO C 1 14  ? 46.396  13.408  25.378  1.00 22.74 ? 13   PRO C CG  1 
ATOM   2279 C  CD  . PRO C 1 14  ? 45.439  14.282  24.617  1.00 22.57 ? 13   PRO C CD  1 
ATOM   2280 N  N   . VAL C 1 15  ? 42.857  12.368  25.420  1.00 23.51 ? 14   VAL C N   1 
ATOM   2281 C  CA  . VAL C 1 15  ? 41.807  11.933  26.352  1.00 23.53 ? 14   VAL C CA  1 
ATOM   2282 C  C   . VAL C 1 15  ? 40.858  10.922  25.714  1.00 22.86 ? 14   VAL C C   1 
ATOM   2283 O  O   . VAL C 1 15  ? 40.158  11.219  24.773  1.00 25.16 ? 14   VAL C O   1 
ATOM   2284 C  CB  . VAL C 1 15  ? 40.977  13.111  26.965  1.00 22.11 ? 14   VAL C CB  1 
ATOM   2285 C  CG1 . VAL C 1 15  ? 39.882  12.592  27.933  1.00 21.39 ? 14   VAL C CG1 1 
ATOM   2286 C  CG2 . VAL C 1 15  ? 41.874  14.114  27.649  1.00 22.16 ? 14   VAL C CG2 1 
ATOM   2287 N  N   . GLN C 1 16  ? 40.856  9.692   26.199  1.00 25.17 ? 15   GLN C N   1 
ATOM   2288 C  CA  . GLN C 1 16  ? 39.875  8.731   25.706  1.00 24.90 ? 15   GLN C CA  1 
ATOM   2289 C  C   . GLN C 1 16  ? 39.368  7.890   26.863  1.00 24.77 ? 15   GLN C C   1 
ATOM   2290 O  O   . GLN C 1 16  ? 40.025  7.798   27.912  1.00 25.46 ? 15   GLN C O   1 
ATOM   2291 C  CB  . GLN C 1 16  ? 40.430  7.868   24.576  1.00 24.63 ? 15   GLN C CB  1 
ATOM   2292 C  CG  . GLN C 1 16  ? 41.865  7.499   24.785  1.00 26.98 ? 15   GLN C CG  1 
ATOM   2293 C  CD  . GLN C 1 16  ? 42.320  6.375   23.883  1.00 27.75 ? 15   GLN C CD  1 
ATOM   2294 O  OE1 . GLN C 1 16  ? 41.586  5.405   23.683  1.00 34.99 ? 15   GLN C OE1 1 
ATOM   2295 N  NE2 . GLN C 1 16  ? 43.532  6.486   23.359  1.00 30.85 ? 15   GLN C NE2 1 
ATOM   2296 N  N   . GLY C 1 17  ? 38.191  7.288   26.671  1.00 25.30 ? 16   GLY C N   1 
ATOM   2297 C  CA  . GLY C 1 17  ? 37.588  6.467   27.696  1.00 24.64 ? 16   GLY C CA  1 
ATOM   2298 C  C   . GLY C 1 17  ? 36.278  5.831   27.254  1.00 23.86 ? 16   GLY C C   1 
ATOM   2299 O  O   . GLY C 1 17  ? 35.776  6.078   26.132  1.00 24.92 ? 16   GLY C O   1 
ATOM   2300 N  N   . ILE C 1 18  ? 35.777  4.953   28.118  1.00 23.21 ? 17   ILE C N   1 
ATOM   2301 C  CA  . ILE C 1 18  ? 34.487  4.310   27.958  1.00 22.39 ? 17   ILE C CA  1 
ATOM   2302 C  C   . ILE C 1 18  ? 33.678  4.464   29.217  1.00 21.73 ? 17   ILE C C   1 
ATOM   2303 O  O   . ILE C 1 18  ? 34.137  4.166   30.332  1.00 23.47 ? 17   ILE C O   1 
ATOM   2304 C  CB  . ILE C 1 18  ? 34.600  2.841   27.539  1.00 21.23 ? 17   ILE C CB  1 
ATOM   2305 C  CG1 . ILE C 1 18  ? 35.129  2.742   26.094  1.00 23.05 ? 17   ILE C CG1 1 
ATOM   2306 C  CG2 . ILE C 1 18  ? 33.239  2.139   27.602  1.00 22.53 ? 17   ILE C CG2 1 
ATOM   2307 C  CD1 . ILE C 1 18  ? 35.726  1.333   25.786  1.00 18.56 ? 17   ILE C CD1 1 
ATOM   2308 N  N   . ILE C 1 19  ? 32.463  4.953   29.054  1.00 21.86 ? 18   ILE C N   1 
ATOM   2309 C  CA  . ILE C 1 19  ? 31.589  5.122   30.182  1.00 19.24 ? 18   ILE C CA  1 
ATOM   2310 C  C   . ILE C 1 19  ? 30.281  4.352   29.971  1.00 19.76 ? 18   ILE C C   1 
ATOM   2311 O  O   . ILE C 1 19  ? 29.637  4.429   28.880  1.00 22.60 ? 18   ILE C O   1 
ATOM   2312 C  CB  . ILE C 1 19  ? 31.300  6.666   30.382  1.00 16.27 ? 18   ILE C CB  1 
ATOM   2313 C  CG1 . ILE C 1 19  ? 32.580  7.460   30.717  1.00 16.34 ? 18   ILE C CG1 1 
ATOM   2314 C  CG2 . ILE C 1 19  ? 30.195  6.834   31.389  1.00 17.46 ? 18   ILE C CG2 1 
ATOM   2315 C  CD1 . ILE C 1 19  ? 33.191  7.144   32.127  1.00 21.55 ? 18   ILE C CD1 1 
ATOM   2316 N  N   . ASN C 1 20  ? 29.926  3.556   30.962  1.00 23.50 ? 19   ASN C N   1 
ATOM   2317 C  CA  . ASN C 1 20  ? 28.732  2.737   30.944  1.00 23.70 ? 19   ASN C CA  1 
ATOM   2318 C  C   . ASN C 1 20  ? 27.602  3.333   31.750  1.00 24.23 ? 19   ASN C C   1 
ATOM   2319 O  O   . ASN C 1 20  ? 27.808  3.977   32.789  1.00 26.35 ? 19   ASN C O   1 
ATOM   2320 C  CB  . ASN C 1 20  ? 29.001  1.301   31.434  1.00 23.64 ? 19   ASN C CB  1 
ATOM   2321 C  CG  . ASN C 1 20  ? 30.156  0.626   30.691  1.00 21.42 ? 19   ASN C CG  1 
ATOM   2322 O  OD1 . ASN C 1 20  ? 31.271  0.519   31.217  1.00 26.85 ? 19   ASN C OD1 1 
ATOM   2323 N  ND2 . ASN C 1 20  ? 29.924  0.279   29.439  1.00 18.10 ? 19   ASN C ND2 1 
ATOM   2324 N  N   . PHE C 1 21  ? 26.410  3.189   31.216  1.00 24.78 ? 20   PHE C N   1 
ATOM   2325 C  CA  . PHE C 1 21  ? 25.206  3.517   31.974  1.00 23.81 ? 20   PHE C CA  1 
ATOM   2326 C  C   . PHE C 1 21  ? 24.240  2.352   32.152  1.00 23.93 ? 20   PHE C C   1 
ATOM   2327 O  O   . PHE C 1 21  ? 23.975  1.556   31.222  1.00 25.70 ? 20   PHE C O   1 
ATOM   2328 C  CB  . PHE C 1 21  ? 24.433  4.690   31.374  1.00 23.74 ? 20   PHE C CB  1 
ATOM   2329 C  CG  . PHE C 1 21  ? 25.272  5.892   31.017  1.00 23.20 ? 20   PHE C CG  1 
ATOM   2330 C  CD1 . PHE C 1 21  ? 26.135  5.869   29.932  1.00 21.76 ? 20   PHE C CD1 1 
ATOM   2331 C  CD2 . PHE C 1 21  ? 25.200  7.042   31.766  1.00 24.59 ? 20   PHE C CD2 1 
ATOM   2332 C  CE1 . PHE C 1 21  ? 26.892  7.018   29.565  1.00 25.36 ? 20   PHE C CE1 1 
ATOM   2333 C  CE2 . PHE C 1 21  ? 25.957  8.131   31.445  1.00 19.83 ? 20   PHE C CE2 1 
ATOM   2334 C  CZ  . PHE C 1 21  ? 26.782  8.145   30.306  1.00 21.78 ? 20   PHE C CZ  1 
ATOM   2335 N  N   . GLU C 1 22  ? 23.666  2.296   33.342  1.00 23.32 ? 21   GLU C N   1 
ATOM   2336 C  CA  . GLU C 1 22  ? 22.679  1.318   33.730  1.00 23.34 ? 21   GLU C CA  1 
ATOM   2337 C  C   . GLU C 1 22  ? 21.552  1.824   34.640  1.00 22.12 ? 21   GLU C C   1 
ATOM   2338 O  O   . GLU C 1 22  ? 21.800  2.369   35.726  1.00 24.82 ? 21   GLU C O   1 
ATOM   2339 C  CB  . GLU C 1 22  ? 23.377  0.135   34.344  1.00 21.67 ? 21   GLU C CB  1 
ATOM   2340 C  CG  . GLU C 1 22  ? 22.452  -0.988  34.695  1.00 27.16 ? 21   GLU C CG  1 
ATOM   2341 C  CD  . GLU C 1 22  ? 23.202  -2.168  35.302  1.00 30.80 ? 21   GLU C CD  1 
ATOM   2342 O  OE1 . GLU C 1 22  ? 23.047  -2.384  36.522  1.00 34.14 ? 21   GLU C OE1 1 
ATOM   2343 O  OE2 . GLU C 1 22  ? 23.965  -2.856  34.576  1.00 35.11 ? 21   GLU C OE2 1 
ATOM   2344 N  N   . GLN C 1 23  ? 20.329  1.674   34.145  1.00 23.02 ? 22   GLN C N   1 
ATOM   2345 C  CA  . GLN C 1 23  ? 19.070  1.975   34.851  1.00 22.54 ? 22   GLN C CA  1 
ATOM   2346 C  C   . GLN C 1 23  ? 18.167  0.721   34.943  1.00 23.05 ? 22   GLN C C   1 
ATOM   2347 O  O   . GLN C 1 23  ? 17.562  0.270   33.934  1.00 22.86 ? 22   GLN C O   1 
ATOM   2348 C  CB  . GLN C 1 23  ? 18.314  3.063   34.119  1.00 22.83 ? 22   GLN C CB  1 
ATOM   2349 C  CG  . GLN C 1 23  ? 17.371  3.869   35.015  1.00 20.91 ? 22   GLN C CG  1 
ATOM   2350 C  CD  . GLN C 1 23  ? 16.693  4.953   34.215  1.00 21.01 ? 22   GLN C CD  1 
ATOM   2351 O  OE1 . GLN C 1 23  ? 16.729  4.916   32.983  1.00 26.02 ? 22   GLN C OE1 1 
ATOM   2352 N  NE2 . GLN C 1 23  ? 16.071  5.924   34.894  1.00 27.50 ? 22   GLN C NE2 1 
ATOM   2353 N  N   . LYS C 1 24  ? 18.023  0.218   36.157  1.00 23.29 ? 23   LYS C N   1 
ATOM   2354 C  CA  . LYS C 1 24  ? 17.260  -1.011  36.430  1.00 23.48 ? 23   LYS C CA  1 
ATOM   2355 C  C   . LYS C 1 24  ? 15.756  -0.761  36.386  1.00 22.63 ? 23   LYS C C   1 
ATOM   2356 O  O   . LYS C 1 24  ? 15.008  -1.540  35.827  1.00 25.21 ? 23   LYS C O   1 
ATOM   2357 C  CB  . LYS C 1 24  ? 17.652  -1.607  37.782  1.00 24.04 ? 23   LYS C CB  1 
ATOM   2358 C  CG  . LYS C 1 24  ? 18.958  -2.439  37.765  1.00 24.94 ? 23   LYS C CG  1 
ATOM   2359 C  CD  . LYS C 1 24  ? 19.457  -2.707  39.177  1.00 28.54 ? 23   LYS C CD  1 
ATOM   2360 C  CE  . LYS C 1 24  ? 20.598  -3.759  39.176  1.00 28.96 ? 23   LYS C CE  1 
ATOM   2361 N  NZ  . LYS C 1 24  ? 20.644  -4.635  40.392  1.00 34.88 ? 23   LYS C NZ  1 
ATOM   2362 N  N   . GLU C 1 25  ? 15.340  0.377   36.924  1.00 22.46 ? 24   GLU C N   1 
ATOM   2363 C  CA  . GLU C 1 25  ? 13.947  0.743   37.025  1.00 21.19 ? 24   GLU C CA  1 
ATOM   2364 C  C   . GLU C 1 25  ? 13.756  2.071   36.334  1.00 20.32 ? 24   GLU C C   1 
ATOM   2365 O  O   . GLU C 1 25  ? 14.610  2.973   36.440  1.00 21.37 ? 24   GLU C O   1 
ATOM   2366 C  CB  . GLU C 1 25  ? 13.540  0.774   38.500  1.00 19.67 ? 24   GLU C CB  1 
ATOM   2367 C  CG  . GLU C 1 25  ? 13.421  -0.643  39.113  1.00 26.20 ? 24   GLU C CG  1 
ATOM   2368 C  CD  . GLU C 1 25  ? 13.830  -0.703  40.573  1.00 28.97 ? 24   GLU C CD  1 
ATOM   2369 O  OE1 . GLU C 1 25  ? 14.496  0.247   41.057  1.00 33.60 ? 24   GLU C OE1 1 
ATOM   2370 O  OE2 . GLU C 1 25  ? 13.487  -1.705  41.244  1.00 30.74 ? 24   GLU C OE2 1 
ATOM   2371 N  N   . SER C 1 26  ? 12.676  2.189   35.566  1.00 19.78 ? 25   SER C N   1 
ATOM   2372 C  CA  . SER C 1 26  ? 12.520  3.415   34.787  1.00 18.08 ? 25   SER C CA  1 
ATOM   2373 C  C   . SER C 1 26  ? 12.373  4.674   35.606  1.00 17.74 ? 25   SER C C   1 
ATOM   2374 O  O   . SER C 1 26  ? 12.686  5.782   35.125  1.00 20.55 ? 25   SER C O   1 
ATOM   2375 C  CB  . SER C 1 26  ? 11.420  3.302   33.759  1.00 16.13 ? 25   SER C CB  1 
ATOM   2376 O  OG  . SER C 1 26  ? 10.141  3.212   34.384  1.00 15.43 ? 25   SER C OG  1 
ATOM   2377 N  N   . ASN C 1 27  ? 11.989  4.513   36.847  1.00 19.91 ? 26   ASN C N   1 
ATOM   2378 C  CA  . ASN C 1 27  ? 11.907  5.631   37.755  1.00 19.94 ? 26   ASN C CA  1 
ATOM   2379 C  C   . ASN C 1 27  ? 12.982  5.536   38.828  1.00 21.12 ? 26   ASN C C   1 
ATOM   2380 O  O   . ASN C 1 27  ? 12.905  6.165   39.879  1.00 23.17 ? 26   ASN C O   1 
ATOM   2381 C  CB  . ASN C 1 27  ? 10.461  5.786   38.311  1.00 20.00 ? 26   ASN C CB  1 
ATOM   2382 C  CG  . ASN C 1 27  ? 10.046  4.709   39.335  1.00 19.48 ? 26   ASN C CG  1 
ATOM   2383 O  OD1 . ASN C 1 27  ? 10.512  3.569   39.326  1.00 24.45 ? 26   ASN C OD1 1 
ATOM   2384 N  ND2 . ASN C 1 27  ? 9.127   5.085   40.211  1.00 24.84 ? 26   ASN C ND2 1 
ATOM   2385 N  N   . GLY C 1 28  ? 13.966  4.679   38.594  1.00 23.02 ? 27   GLY C N   1 
ATOM   2386 C  CA  . GLY C 1 28  ? 15.090  4.560   39.505  1.00 23.10 ? 27   GLY C CA  1 
ATOM   2387 C  C   . GLY C 1 28  ? 16.380  5.252   39.056  1.00 22.46 ? 27   GLY C C   1 
ATOM   2388 O  O   . GLY C 1 28  ? 16.474  5.855   37.995  1.00 23.71 ? 27   GLY C O   1 
ATOM   2389 N  N   . PRO C 1 29  ? 17.410  5.208   39.894  1.00 23.45 ? 28   PRO C N   1 
ATOM   2390 C  CA  . PRO C 1 29  ? 18.666  5.859   39.563  1.00 22.25 ? 28   PRO C CA  1 
ATOM   2391 C  C   . PRO C 1 29  ? 19.433  5.225   38.396  1.00 21.59 ? 28   PRO C C   1 
ATOM   2392 O  O   . PRO C 1 29  ? 19.255  4.064   38.019  1.00 23.94 ? 28   PRO C O   1 
ATOM   2393 C  CB  . PRO C 1 29  ? 19.460  5.706   40.860  1.00 21.83 ? 28   PRO C CB  1 
ATOM   2394 C  CG  . PRO C 1 29  ? 18.908  4.443   41.406  1.00 22.19 ? 28   PRO C CG  1 
ATOM   2395 C  CD  . PRO C 1 29  ? 17.447  4.603   41.239  1.00 22.39 ? 28   PRO C CD  1 
ATOM   2396 N  N   . VAL C 1 30  ? 20.292  6.019   37.817  1.00 22.29 ? 29   VAL C N   1 
ATOM   2397 C  CA  . VAL C 1 30  ? 21.189  5.545   36.780  1.00 20.70 ? 29   VAL C CA  1 
ATOM   2398 C  C   . VAL C 1 30  ? 22.565  5.329   37.410  1.00 21.06 ? 29   VAL C C   1 
ATOM   2399 O  O   . VAL C 1 30  ? 23.131  6.219   38.063  1.00 24.60 ? 29   VAL C O   1 
ATOM   2400 C  CB  . VAL C 1 30  ? 21.284  6.540   35.593  1.00 19.31 ? 29   VAL C CB  1 
ATOM   2401 C  CG1 . VAL C 1 30  ? 22.197  6.010   34.454  1.00 16.24 ? 29   VAL C CG1 1 
ATOM   2402 C  CG2 . VAL C 1 30  ? 19.893  6.984   35.073  1.00 24.27 ? 29   VAL C CG2 1 
ATOM   2403 N  N   . LYS C 1 31  ? 23.109  4.140   37.254  1.00 21.48 ? 30   LYS C N   1 
ATOM   2404 C  CA  . LYS C 1 31  ? 24.505  3.891   37.604  1.00 21.79 ? 30   LYS C CA  1 
ATOM   2405 C  C   . LYS C 1 31  ? 25.381  4.257   36.399  1.00 21.16 ? 30   LYS C C   1 
ATOM   2406 O  O   . LYS C 1 31  ? 25.100  3.860   35.248  1.00 24.18 ? 30   LYS C O   1 
ATOM   2407 C  CB  . LYS C 1 31  ? 24.722  2.415   37.959  1.00 20.13 ? 30   LYS C CB  1 
ATOM   2408 C  CG  . LYS C 1 31  ? 23.889  1.822   39.082  1.00 23.39 ? 30   LYS C CG  1 
ATOM   2409 C  CD  . LYS C 1 31  ? 24.270  0.332   39.262  1.00 26.53 ? 30   LYS C CD  1 
ATOM   2410 C  CE  . LYS C 1 31  ? 23.028  -0.549  39.322  1.00 30.39 ? 30   LYS C CE  1 
ATOM   2411 N  NZ  . LYS C 1 31  ? 22.449  -0.837  37.985  1.00 32.51 ? 30   LYS C NZ  1 
ATOM   2412 N  N   . VAL C 1 32  ? 26.408  5.080   36.644  1.00 22.28 ? 31   VAL C N   1 
ATOM   2413 C  CA  . VAL C 1 32  ? 27.344  5.560   35.637  1.00 20.04 ? 31   VAL C CA  1 
ATOM   2414 C  C   . VAL C 1 32  ? 28.760  5.156   36.025  1.00 21.20 ? 31   VAL C C   1 
ATOM   2415 O  O   . VAL C 1 32  ? 29.283  5.576   37.061  1.00 24.35 ? 31   VAL C O   1 
ATOM   2416 C  CB  . VAL C 1 32  ? 27.286  7.149   35.442  1.00 17.40 ? 31   VAL C CB  1 
ATOM   2417 C  CG1 . VAL C 1 32  ? 28.259  7.608   34.307  1.00 16.48 ? 31   VAL C CG1 1 
ATOM   2418 C  CG2 . VAL C 1 32  ? 25.903  7.650   35.218  1.00 21.28 ? 31   VAL C CG2 1 
ATOM   2419 N  N   . TRP C 1 33  ? 29.435  4.398   35.175  1.00 22.78 ? 32   TRP C N   1 
ATOM   2420 C  CA  . TRP C 1 33  ? 30.771  3.928   35.512  1.00 21.21 ? 32   TRP C CA  1 
ATOM   2421 C  C   . TRP C 1 33  ? 31.651  3.588   34.336  1.00 21.56 ? 32   TRP C C   1 
ATOM   2422 O  O   . TRP C 1 33  ? 31.149  3.249   33.247  1.00 23.12 ? 32   TRP C O   1 
ATOM   2423 C  CB  . TRP C 1 33  ? 30.720  2.700   36.405  1.00 21.95 ? 32   TRP C CB  1 
ATOM   2424 C  CG  . TRP C 1 33  ? 30.480  1.425   35.671  1.00 21.06 ? 32   TRP C CG  1 
ATOM   2425 C  CD1 . TRP C 1 33  ? 31.406  0.512   35.304  1.00 23.58 ? 32   TRP C CD1 1 
ATOM   2426 C  CD2 . TRP C 1 33  ? 29.232  0.951   35.185  1.00 23.87 ? 32   TRP C CD2 1 
ATOM   2427 N  NE1 . TRP C 1 33  ? 30.812  -0.526  34.633  1.00 24.57 ? 32   TRP C NE1 1 
ATOM   2428 C  CE2 . TRP C 1 33  ? 29.468  -0.310  34.593  1.00 24.82 ? 32   TRP C CE2 1 
ATOM   2429 C  CE3 . TRP C 1 33  ? 27.912  1.411   35.284  1.00 22.62 ? 32   TRP C CE3 1 
ATOM   2430 C  CZ2 . TRP C 1 33  ? 28.455  -1.075  34.022  1.00 25.47 ? 32   TRP C CZ2 1 
ATOM   2431 C  CZ3 . TRP C 1 33  ? 26.909  0.671   34.700  1.00 27.19 ? 32   TRP C CZ3 1 
ATOM   2432 C  CH2 . TRP C 1 33  ? 27.187  -0.597  34.106  1.00 28.12 ? 32   TRP C CH2 1 
ATOM   2433 N  N   . GLY C 1 34  ? 32.963  3.653   34.569  1.00 21.91 ? 33   GLY C N   1 
ATOM   2434 C  CA  . GLY C 1 34  ? 33.966  3.325   33.561  1.00 22.61 ? 33   GLY C CA  1 
ATOM   2435 C  C   . GLY C 1 34  ? 35.335  3.904   33.852  1.00 22.92 ? 33   GLY C C   1 
ATOM   2436 O  O   . GLY C 1 34  ? 35.707  4.108   35.018  1.00 25.03 ? 33   GLY C O   1 
ATOM   2437 N  N   . SER C 1 35  ? 36.101  4.143   32.793  1.00 23.96 ? 34   SER C N   1 
ATOM   2438 C  CA  . SER C 1 35  ? 37.448  4.669   32.896  1.00 24.36 ? 34   SER C CA  1 
ATOM   2439 C  C   . SER C 1 35  ? 37.804  5.649   31.773  1.00 24.16 ? 34   SER C C   1 
ATOM   2440 O  O   . SER C 1 35  ? 37.483  5.411   30.596  1.00 25.32 ? 34   SER C O   1 
ATOM   2441 C  CB  . SER C 1 35  ? 38.426  3.510   32.874  1.00 22.90 ? 34   SER C CB  1 
ATOM   2442 O  OG  . SER C 1 35  ? 39.639  3.897   33.496  1.00 29.51 ? 34   SER C OG  1 
ATOM   2443 N  N   . ILE C 1 36  ? 38.490  6.732   32.138  1.00 24.67 ? 35   ILE C N   1 
ATOM   2444 C  CA  . ILE C 1 36  ? 39.012  7.711   31.195  1.00 23.65 ? 35   ILE C CA  1 
ATOM   2445 C  C   . ILE C 1 36  ? 40.514  7.999   31.433  1.00 23.93 ? 35   ILE C C   1 
ATOM   2446 O  O   . ILE C 1 36  ? 40.941  8.230   32.566  1.00 25.83 ? 35   ILE C O   1 
ATOM   2447 C  CB  . ILE C 1 36  ? 38.282  9.066   31.307  1.00 22.57 ? 35   ILE C CB  1 
ATOM   2448 C  CG1 . ILE C 1 36  ? 36.757  8.921   31.332  1.00 24.39 ? 35   ILE C CG1 1 
ATOM   2449 C  CG2 . ILE C 1 36  ? 38.859  10.034  30.225  1.00 20.03 ? 35   ILE C CG2 1 
ATOM   2450 C  CD1 . ILE C 1 36  ? 36.053  10.186  31.774  1.00 27.79 ? 35   ILE C CD1 1 
ATOM   2451 N  N   . LYS C 1 37  ? 41.295  8.031   30.360  1.00 25.19 ? 36   LYS C N   1 
ATOM   2452 C  CA  . LYS C 1 37  ? 42.726  8.323   30.423  1.00 24.95 ? 36   LYS C CA  1 
ATOM   2453 C  C   . LYS C 1 37  ? 43.199  9.506   29.573  1.00 24.92 ? 36   LYS C C   1 
ATOM   2454 O  O   . LYS C 1 37  ? 42.451  10.043  28.731  1.00 26.37 ? 36   LYS C O   1 
ATOM   2455 C  CB  . LYS C 1 37  ? 43.536  7.085   30.067  1.00 24.46 ? 36   LYS C CB  1 
ATOM   2456 C  CG  . LYS C 1 37  ? 43.291  6.507   28.684  1.00 25.50 ? 36   LYS C CG  1 
ATOM   2457 C  CD  . LYS C 1 37  ? 44.546  5.743   28.253  1.00 27.61 ? 36   LYS C CD  1 
ATOM   2458 C  CE  . LYS C 1 37  ? 44.334  4.499   27.356  1.00 28.15 ? 36   LYS C CE  1 
ATOM   2459 N  NZ  . LYS C 1 37  ? 45.677  3.802   27.142  1.00 28.65 ? 36   LYS C NZ  1 
ATOM   2460 N  N   . GLY C 1 38  ? 44.451  9.906   29.795  1.00 25.06 ? 37   GLY C N   1 
ATOM   2461 C  CA  . GLY C 1 38  ? 45.040  11.003  29.049  1.00 23.62 ? 37   GLY C CA  1 
ATOM   2462 C  C   . GLY C 1 38  ? 44.722  12.327  29.695  1.00 23.16 ? 37   GLY C C   1 
ATOM   2463 O  O   . GLY C 1 38  ? 44.962  13.382  29.091  1.00 24.50 ? 37   GLY C O   1 
ATOM   2464 N  N   . LEU C 1 39  ? 44.162  12.273  30.905  1.00 23.50 ? 38   LEU C N   1 
ATOM   2465 C  CA  . LEU C 1 39  ? 43.828  13.471  31.665  1.00 23.30 ? 38   LEU C CA  1 
ATOM   2466 C  C   . LEU C 1 39  ? 44.955  13.981  32.539  1.00 23.73 ? 38   LEU C C   1 
ATOM   2467 O  O   . LEU C 1 39  ? 45.773  13.208  33.052  1.00 24.79 ? 38   LEU C O   1 
ATOM   2468 C  CB  . LEU C 1 39  ? 42.652  13.198  32.622  1.00 21.88 ? 38   LEU C CB  1 
ATOM   2469 C  CG  . LEU C 1 39  ? 41.147  13.205  32.389  1.00 22.11 ? 38   LEU C CG  1 
ATOM   2470 C  CD1 . LEU C 1 39  ? 40.726  13.990  31.203  1.00 22.14 ? 38   LEU C CD1 1 
ATOM   2471 C  CD2 . LEU C 1 39  ? 40.663  11.759  32.298  1.00 22.90 ? 38   LEU C CD2 1 
ATOM   2472 N  N   . THR C 1 40  ? 45.009  15.295  32.736  1.00 24.98 ? 39   THR C N   1 
ATOM   2473 C  CA  . THR C 1 40  ? 45.901  15.842  33.744  1.00 24.90 ? 39   THR C CA  1 
ATOM   2474 C  C   . THR C 1 40  ? 45.371  15.475  35.138  1.00 25.66 ? 39   THR C C   1 
ATOM   2475 O  O   . THR C 1 40  ? 44.144  15.387  35.351  1.00 25.61 ? 39   THR C O   1 
ATOM   2476 C  CB  . THR C 1 40  ? 46.033  17.370  33.596  1.00 25.74 ? 39   THR C CB  1 
ATOM   2477 O  OG1 . THR C 1 40  ? 44.726  17.961  33.649  1.00 27.82 ? 39   THR C OG1 1 
ATOM   2478 C  CG2 . THR C 1 40  ? 46.522  17.737  32.188  1.00 23.51 ? 39   THR C CG2 1 
ATOM   2479 N  N   . GLU C 1 41  ? 46.292  15.190  36.059  1.00 25.85 ? 40   GLU C N   1 
ATOM   2480 C  CA  . GLU C 1 41  ? 45.915  14.803  37.414  1.00 26.35 ? 40   GLU C CA  1 
ATOM   2481 C  C   . GLU C 1 41  ? 44.979  15.851  37.996  1.00 26.46 ? 40   GLU C C   1 
ATOM   2482 O  O   . GLU C 1 41  ? 45.216  17.052  37.849  1.00 26.74 ? 40   GLU C O   1 
ATOM   2483 C  CB  . GLU C 1 41  ? 47.133  14.609  38.316  1.00 26.50 ? 40   GLU C CB  1 
ATOM   2484 C  CG  . GLU C 1 41  ? 46.823  14.323  39.789  1.00 27.58 ? 40   GLU C CG  1 
ATOM   2485 C  CD  . GLU C 1 41  ? 48.064  13.957  40.626  1.00 28.42 ? 40   GLU C CD  1 
ATOM   2486 O  OE1 . GLU C 1 41  ? 49.206  13.964  40.091  1.00 30.61 ? 40   GLU C OE1 1 
ATOM   2487 O  OE2 . GLU C 1 41  ? 47.895  13.647  41.837  1.00 30.15 ? 40   GLU C OE2 1 
ATOM   2488 N  N   . GLY C 1 42  ? 43.912  15.379  38.622  1.00 25.39 ? 41   GLY C N   1 
ATOM   2489 C  CA  . GLY C 1 42  ? 42.953  16.255  39.270  1.00 25.52 ? 41   GLY C CA  1 
ATOM   2490 C  C   . GLY C 1 42  ? 41.523  16.140  38.763  1.00 25.03 ? 41   GLY C C   1 
ATOM   2491 O  O   . GLY C 1 42  ? 41.114  15.139  38.157  1.00 26.35 ? 41   GLY C O   1 
ATOM   2492 N  N   . LEU C 1 43  ? 40.759  17.196  39.042  1.00 24.55 ? 42   LEU C N   1 
ATOM   2493 C  CA  . LEU C 1 43  ? 39.347  17.262  38.758  1.00 22.92 ? 42   LEU C CA  1 
ATOM   2494 C  C   . LEU C 1 43  ? 39.014  17.809  37.389  1.00 22.23 ? 42   LEU C C   1 
ATOM   2495 O  O   . LEU C 1 43  ? 39.600  18.795  36.927  1.00 22.01 ? 42   LEU C O   1 
ATOM   2496 C  CB  . LEU C 1 43  ? 38.657  18.142  39.787  1.00 22.81 ? 42   LEU C CB  1 
ATOM   2497 C  CG  . LEU C 1 43  ? 37.783  17.723  40.968  1.00 22.72 ? 42   LEU C CG  1 
ATOM   2498 C  CD1 . LEU C 1 43  ? 37.675  16.239  41.199  1.00 24.50 ? 42   LEU C CD1 1 
ATOM   2499 C  CD2 . LEU C 1 43  ? 38.369  18.405  42.150  1.00 19.22 ? 42   LEU C CD2 1 
ATOM   2500 N  N   . HIS C 1 44  ? 38.024  17.164  36.790  1.00 22.95 ? 43   HIS C N   1 
ATOM   2501 C  CA  . HIS C 1 44  ? 37.501  17.487  35.472  1.00 21.87 ? 43   HIS C CA  1 
ATOM   2502 C  C   . HIS C 1 44  ? 35.981  17.462  35.401  1.00 21.44 ? 43   HIS C C   1 
ATOM   2503 O  O   . HIS C 1 44  ? 35.272  16.432  35.676  1.00 21.57 ? 43   HIS C O   1 
ATOM   2504 C  CB  . HIS C 1 44  ? 38.088  16.551  34.406  1.00 20.99 ? 43   HIS C CB  1 
ATOM   2505 C  CG  . HIS C 1 44  ? 39.577  16.634  34.287  1.00 22.66 ? 43   HIS C CG  1 
ATOM   2506 N  ND1 . HIS C 1 44  ? 40.214  17.665  33.637  1.00 22.25 ? 43   HIS C ND1 1 
ATOM   2507 C  CD2 . HIS C 1 44  ? 40.558  15.818  34.746  1.00 17.23 ? 43   HIS C CD2 1 
ATOM   2508 C  CE1 . HIS C 1 44  ? 41.516  17.466  33.675  1.00 23.49 ? 43   HIS C CE1 1 
ATOM   2509 N  NE2 . HIS C 1 44  ? 41.749  16.346  34.333  1.00 24.25 ? 43   HIS C NE2 1 
ATOM   2510 N  N   . GLY C 1 45  ? 35.426  18.577  34.945  1.00 22.01 ? 44   GLY C N   1 
ATOM   2511 C  CA  . GLY C 1 45  ? 33.984  18.571  34.722  1.00 22.24 ? 44   GLY C CA  1 
ATOM   2512 C  C   . GLY C 1 45  ? 33.448  17.382  33.890  1.00 21.84 ? 44   GLY C C   1 
ATOM   2513 O  O   . GLY C 1 45  ? 34.076  16.882  32.949  1.00 24.44 ? 44   GLY C O   1 
ATOM   2514 N  N   . PHE C 1 46  ? 32.256  16.946  34.232  1.00 21.18 ? 45   PHE C N   1 
ATOM   2515 C  CA  . PHE C 1 46  ? 31.633  15.756  33.592  1.00 19.77 ? 45   PHE C CA  1 
ATOM   2516 C  C   . PHE C 1 46  ? 30.154  16.058  33.393  1.00 20.04 ? 45   PHE C C   1 
ATOM   2517 O  O   . PHE C 1 46  ? 29.344  16.061  34.329  1.00 21.91 ? 45   PHE C O   1 
ATOM   2518 C  CB  . PHE C 1 46  ? 31.904  14.622  34.528  1.00 20.30 ? 45   PHE C CB  1 
ATOM   2519 C  CG  . PHE C 1 46  ? 31.662  13.269  33.970  1.00 18.71 ? 45   PHE C CG  1 
ATOM   2520 C  CD1 . PHE C 1 46  ? 32.283  12.860  32.802  1.00 24.42 ? 45   PHE C CD1 1 
ATOM   2521 C  CD2 . PHE C 1 46  ? 30.889  12.391  34.681  1.00 19.22 ? 45   PHE C CD2 1 
ATOM   2522 C  CE1 . PHE C 1 46  ? 32.104  11.567  32.313  1.00 20.98 ? 45   PHE C CE1 1 
ATOM   2523 C  CE2 . PHE C 1 46  ? 30.710  11.090  34.232  1.00 20.93 ? 45   PHE C CE2 1 
ATOM   2524 C  CZ  . PHE C 1 46  ? 31.304  10.694  33.019  1.00 24.59 ? 45   PHE C CZ  1 
ATOM   2525 N  N   . HIS C 1 47  ? 29.811  16.322  32.149  1.00 21.59 ? 46   HIS C N   1 
ATOM   2526 C  CA  . HIS C 1 47  ? 28.484  16.715  31.748  1.00 20.74 ? 46   HIS C CA  1 
ATOM   2527 C  C   . HIS C 1 47  ? 27.954  16.042  30.505  1.00 20.22 ? 46   HIS C C   1 
ATOM   2528 O  O   . HIS C 1 47  ? 28.664  15.765  29.483  1.00 22.91 ? 46   HIS C O   1 
ATOM   2529 C  CB  . HIS C 1 47  ? 28.428  18.246  31.468  1.00 20.57 ? 46   HIS C CB  1 
ATOM   2530 C  CG  . HIS C 1 47  ? 28.580  19.107  32.682  1.00 23.88 ? 46   HIS C CG  1 
ATOM   2531 N  ND1 . HIS C 1 47  ? 29.792  19.622  33.079  1.00 24.21 ? 46   HIS C ND1 1 
ATOM   2532 C  CD2 . HIS C 1 47  ? 27.668  19.559  33.575  1.00 23.52 ? 46   HIS C CD2 1 
ATOM   2533 C  CE1 . HIS C 1 47  ? 29.629  20.334  34.174  1.00 21.35 ? 46   HIS C CE1 1 
ATOM   2534 N  NE2 . HIS C 1 47  ? 28.345  20.325  34.489  1.00 24.77 ? 46   HIS C NE2 1 
ATOM   2535 N  N   . VAL C 1 48  ? 26.649  15.831  30.570  1.00 21.82 ? 47   VAL C N   1 
ATOM   2536 C  CA  . VAL C 1 48  ? 25.898  15.541  29.413  1.00 22.20 ? 47   VAL C CA  1 
ATOM   2537 C  C   . VAL C 1 48  ? 25.465  16.865  28.812  1.00 20.99 ? 47   VAL C C   1 
ATOM   2538 O  O   . VAL C 1 48  ? 24.912  17.726  29.496  1.00 24.27 ? 47   VAL C O   1 
ATOM   2539 C  CB  . VAL C 1 48  ? 24.686  14.714  29.724  1.00 20.39 ? 47   VAL C CB  1 
ATOM   2540 C  CG1 . VAL C 1 48  ? 23.819  14.598  28.491  1.00 20.34 ? 47   VAL C CG1 1 
ATOM   2541 C  CG2 . VAL C 1 48  ? 25.102  13.319  30.206  1.00 26.37 ? 47   VAL C CG2 1 
ATOM   2542 N  N   . HIS C 1 49  ? 25.697  17.007  27.514  1.00 23.53 ? 48   HIS C N   1 
ATOM   2543 C  CA  . HIS C 1 49  ? 25.287  18.175  26.764  1.00 23.57 ? 48   HIS C CA  1 
ATOM   2544 C  C   . HIS C 1 49  ? 24.128  17.757  25.868  1.00 23.52 ? 48   HIS C C   1 
ATOM   2545 O  O   . HIS C 1 49  ? 23.921  16.541  25.600  1.00 24.92 ? 48   HIS C O   1 
ATOM   2546 C  CB  . HIS C 1 49  ? 26.455  18.737  25.938  1.00 21.94 ? 48   HIS C CB  1 
ATOM   2547 C  CG  . HIS C 1 49  ? 27.559  19.279  26.774  1.00 20.83 ? 48   HIS C CG  1 
ATOM   2548 N  ND1 . HIS C 1 49  ? 27.918  20.620  26.758  1.00 19.02 ? 48   HIS C ND1 1 
ATOM   2549 C  CD2 . HIS C 1 49  ? 28.337  18.687  27.710  1.00 16.33 ? 48   HIS C CD2 1 
ATOM   2550 C  CE1 . HIS C 1 49  ? 28.907  20.804  27.606  1.00 16.25 ? 48   HIS C CE1 1 
ATOM   2551 N  NE2 . HIS C 1 49  ? 29.171  19.659  28.202  1.00 22.47 ? 48   HIS C NE2 1 
ATOM   2552 N  N   . GLU C 1 50  ? 23.370  18.777  25.467  1.00 23.35 ? 49   GLU C N   1 
ATOM   2553 C  CA  . GLU C 1 50  ? 22.106  18.665  24.759  1.00 23.53 ? 49   GLU C CA  1 
ATOM   2554 C  C   . GLU C 1 50  ? 22.075  17.908  23.419  1.00 22.67 ? 49   GLU C C   1 
ATOM   2555 O  O   . GLU C 1 50  ? 21.170  17.116  23.227  1.00 25.38 ? 49   GLU C O   1 
ATOM   2556 C  CB  . GLU C 1 50  ? 21.442  20.031  24.568  1.00 23.22 ? 49   GLU C CB  1 
ATOM   2557 C  CG  . GLU C 1 50  ? 20.012  19.953  24.003  1.00 20.68 ? 49   GLU C CG  1 
ATOM   2558 C  CD  . GLU C 1 50  ? 19.386  21.313  23.841  1.00 24.90 ? 49   GLU C CD  1 
ATOM   2559 O  OE1 . GLU C 1 50  ? 20.106  22.279  24.095  1.00 26.54 ? 49   GLU C OE1 1 
ATOM   2560 O  OE2 . GLU C 1 50  ? 18.212  21.425  23.455  1.00 29.45 ? 49   GLU C OE2 1 
ATOM   2561 N  N   . PHE C 1 51  ? 23.052  18.120  22.548  1.00 22.73 ? 50   PHE C N   1 
ATOM   2562 C  CA  . PHE C 1 51  ? 23.003  17.522  21.221  1.00 21.98 ? 50   PHE C CA  1 
ATOM   2563 C  C   . PHE C 1 51  ? 23.962  16.345  21.062  1.00 23.49 ? 50   PHE C C   1 
ATOM   2564 O  O   . PHE C 1 51  ? 25.097  16.372  21.586  1.00 24.72 ? 50   PHE C O   1 
ATOM   2565 C  CB  . PHE C 1 51  ? 23.157  18.605  20.135  1.00 21.63 ? 50   PHE C CB  1 
ATOM   2566 C  CG  . PHE C 1 51  ? 22.177  19.732  20.295  1.00 19.67 ? 50   PHE C CG  1 
ATOM   2567 C  CD1 . PHE C 1 51  ? 20.806  19.495  20.268  1.00 18.30 ? 50   PHE C CD1 1 
ATOM   2568 C  CD2 . PHE C 1 51  ? 22.634  21.062  20.489  1.00 19.08 ? 50   PHE C CD2 1 
ATOM   2569 C  CE1 . PHE C 1 51  ? 19.887  20.527  20.437  1.00 21.20 ? 50   PHE C CE1 1 
ATOM   2570 C  CE2 . PHE C 1 51  ? 21.737  22.064  20.694  1.00 19.57 ? 50   PHE C CE2 1 
ATOM   2571 C  CZ  . PHE C 1 51  ? 20.361  21.826  20.642  1.00 19.11 ? 50   PHE C CZ  1 
ATOM   2572 N  N   . GLY C 1 52  ? 23.455  15.261  20.454  1.00 24.15 ? 51   GLY C N   1 
ATOM   2573 C  CA  . GLY C 1 52  ? 24.268  14.136  20.067  1.00 23.31 ? 51   GLY C CA  1 
ATOM   2574 C  C   . GLY C 1 52  ? 24.872  14.482  18.720  1.00 23.79 ? 51   GLY C C   1 
ATOM   2575 O  O   . GLY C 1 52  ? 24.829  13.691  17.760  1.00 25.06 ? 51   GLY C O   1 
ATOM   2576 N  N   . ASP C 1 53  ? 25.376  15.722  18.629  1.00 24.81 ? 52   ASP C N   1 
ATOM   2577 C  CA  . ASP C 1 53  ? 25.968  16.279  17.405  1.00 23.29 ? 52   ASP C CA  1 
ATOM   2578 C  C   . ASP C 1 53  ? 27.467  16.494  17.592  1.00 23.79 ? 52   ASP C C   1 
ATOM   2579 O  O   . ASP C 1 53  ? 27.953  17.358  18.361  1.00 25.31 ? 52   ASP C O   1 
ATOM   2580 C  CB  . ASP C 1 53  ? 25.281  17.603  17.025  1.00 24.81 ? 52   ASP C CB  1 
ATOM   2581 C  CG  . ASP C 1 53  ? 25.732  18.202  15.638  1.00 21.02 ? 52   ASP C CG  1 
ATOM   2582 O  OD1 . ASP C 1 53  ? 26.898  18.075  15.160  1.00 23.27 ? 52   ASP C OD1 1 
ATOM   2583 O  OD2 . ASP C 1 53  ? 24.925  18.848  14.930  1.00 25.81 ? 52   ASP C OD2 1 
ATOM   2584 N  N   . ASN C 1 54  ? 28.240  15.709  16.883  1.00 24.70 ? 53   ASN C N   1 
ATOM   2585 C  CA  . ASN C 1 54  ? 29.665  15.909  16.935  1.00 25.35 ? 53   ASN C CA  1 
ATOM   2586 C  C   . ASN C 1 54  ? 30.283  16.295  15.559  1.00 24.44 ? 53   ASN C C   1 
ATOM   2587 O  O   . ASN C 1 54  ? 31.479  16.055  15.274  1.00 25.27 ? 53   ASN C O   1 
ATOM   2588 C  CB  . ASN C 1 54  ? 30.320  14.710  17.626  1.00 25.97 ? 53   ASN C CB  1 
ATOM   2589 C  CG  . ASN C 1 54  ? 29.996  14.645  19.192  1.00 28.39 ? 53   ASN C CG  1 
ATOM   2590 O  OD1 . ASN C 1 54  ? 30.037  13.569  19.814  1.00 31.32 ? 53   ASN C OD1 1 
ATOM   2591 N  ND2 . ASN C 1 54  ? 29.701  15.799  19.805  1.00 26.43 ? 53   ASN C ND2 1 
ATOM   2592 N  N   . THR C 1 55  ? 29.486  16.922  14.710  1.00 24.40 ? 54   THR C N   1 
ATOM   2593 C  CA  . THR C 1 55  ? 29.979  17.292  13.380  1.00 24.12 ? 54   THR C CA  1 
ATOM   2594 C  C   . THR C 1 55  ? 31.247  18.147  13.349  1.00 24.13 ? 54   THR C C   1 
ATOM   2595 O  O   . THR C 1 55  ? 32.059  18.004  12.459  1.00 25.10 ? 54   THR C O   1 
ATOM   2596 C  CB  . THR C 1 55  ? 28.882  17.925  12.481  1.00 23.33 ? 54   THR C CB  1 
ATOM   2597 O  OG1 . THR C 1 55  ? 28.233  18.991  13.181  1.00 25.59 ? 54   THR C OG1 1 
ATOM   2598 C  CG2 . THR C 1 55  ? 27.756  16.934  12.196  1.00 21.68 ? 54   THR C CG2 1 
ATOM   2599 N  N   . ALA C 1 56  ? 31.439  18.989  14.351  1.00 24.20 ? 55   ALA C N   1 
ATOM   2600 C  CA  . ALA C 1 56  ? 32.606  19.838  14.433  1.00 24.32 ? 55   ALA C CA  1 
ATOM   2601 C  C   . ALA C 1 56  ? 33.187  19.619  15.795  1.00 24.23 ? 55   ALA C C   1 
ATOM   2602 O  O   . ALA C 1 56  ? 33.512  20.569  16.515  1.00 25.57 ? 55   ALA C O   1 
ATOM   2603 C  CB  . ALA C 1 56  ? 32.224  21.292  14.257  1.00 22.17 ? 55   ALA C CB  1 
ATOM   2604 N  N   . GLY C 1 57  ? 33.285  18.354  16.174  1.00 24.44 ? 56   GLY C N   1 
ATOM   2605 C  CA  . GLY C 1 57  ? 33.838  18.044  17.463  1.00 22.78 ? 56   GLY C CA  1 
ATOM   2606 C  C   . GLY C 1 57  ? 32.851  18.253  18.585  1.00 23.12 ? 56   GLY C C   1 
ATOM   2607 O  O   . GLY C 1 57  ? 31.619  18.345  18.377  1.00 24.30 ? 56   GLY C O   1 
ATOM   2608 N  N   . CYS C 1 58  ? 33.429  18.311  19.773  1.00 22.60 ? 57   CYS C N   1 
ATOM   2609 C  CA  . CYS C 1 58  ? 32.737  18.404  21.035  1.00 23.22 ? 57   CYS C CA  1 
ATOM   2610 C  C   . CYS C 1 58  ? 31.930  19.693  21.154  1.00 23.22 ? 57   CYS C C   1 
ATOM   2611 O  O   . CYS C 1 58  ? 30.920  19.748  21.893  1.00 26.30 ? 57   CYS C O   1 
ATOM   2612 C  CB  . CYS C 1 58  ? 33.773  18.222  22.159  1.00 20.97 ? 57   CYS C CB  1 
ATOM   2613 S  SG  . CYS C 1 58  ? 34.433  16.524  22.211  1.00 27.29 ? 57   CYS C SG  1 
ATOM   2614 N  N   . THR C 1 59  ? 32.337  20.695  20.378  1.00 25.52 ? 58   THR C N   1 
ATOM   2615 C  CA  . THR C 1 59  ? 31.665  21.968  20.333  1.00 25.37 ? 58   THR C CA  1 
ATOM   2616 C  C   . THR C 1 59  ? 30.252  21.892  19.790  1.00 26.06 ? 58   THR C C   1 
ATOM   2617 O  O   . THR C 1 59  ? 29.390  22.637  20.231  1.00 26.29 ? 58   THR C O   1 
ATOM   2618 C  CB  . THR C 1 59  ? 32.494  22.956  19.496  1.00 25.62 ? 58   THR C CB  1 
ATOM   2619 O  OG1 . THR C 1 59  ? 33.791  23.088  20.094  1.00 28.42 ? 58   THR C OG1 1 
ATOM   2620 C  CG2 . THR C 1 59  ? 31.914  24.398  19.587  1.00 23.34 ? 58   THR C CG2 1 
ATOM   2621 N  N   . SER C 1 60  ? 29.985  20.996  18.852  1.00 26.57 ? 59   SER C N   1 
ATOM   2622 C  CA  . SER C 1 60  ? 28.639  20.930  18.297  1.00 25.89 ? 59   SER C CA  1 
ATOM   2623 C  C   . SER C 1 60  ? 27.583  20.387  19.265  1.00 24.99 ? 59   SER C C   1 
ATOM   2624 O  O   . SER C 1 60  ? 26.383  20.482  18.967  1.00 25.84 ? 59   SER C O   1 
ATOM   2625 C  CB  . SER C 1 60  ? 28.584  20.130  16.991  1.00 25.06 ? 59   SER C CB  1 
ATOM   2626 O  OG  . SER C 1 60  ? 29.846  20.064  16.389  1.00 29.37 ? 59   SER C OG  1 
ATOM   2627 N  N   . ALA C 1 61  ? 28.016  19.841  20.399  1.00 23.71 ? 60   ALA C N   1 
ATOM   2628 C  CA  . ALA C 1 61  ? 27.096  19.249  21.392  1.00 23.50 ? 60   ALA C CA  1 
ATOM   2629 C  C   . ALA C 1 61  ? 26.160  20.285  21.997  1.00 22.29 ? 60   ALA C C   1 
ATOM   2630 O  O   . ALA C 1 61  ? 25.185  19.947  22.653  1.00 22.95 ? 60   ALA C O   1 
ATOM   2631 C  CB  . ALA C 1 61  ? 27.888  18.586  22.471  1.00 21.68 ? 60   ALA C CB  1 
ATOM   2632 N  N   . GLY C 1 62  ? 26.510  21.565  21.850  1.00 22.40 ? 61   GLY C N   1 
ATOM   2633 C  CA  . GLY C 1 62  ? 25.705  22.597  22.465  1.00 21.34 ? 61   GLY C CA  1 
ATOM   2634 C  C   . GLY C 1 62  ? 25.979  22.704  23.947  1.00 20.16 ? 61   GLY C C   1 
ATOM   2635 O  O   . GLY C 1 62  ? 27.015  22.280  24.443  1.00 19.81 ? 61   GLY C O   1 
ATOM   2636 N  N   . PRO C 1 63  ? 25.035  23.282  24.655  1.00 21.34 ? 62   PRO C N   1 
ATOM   2637 C  CA  . PRO C 1 63  ? 25.144  23.513  26.100  1.00 22.31 ? 62   PRO C CA  1 
ATOM   2638 C  C   . PRO C 1 63  ? 24.811  22.286  26.938  1.00 23.11 ? 62   PRO C C   1 
ATOM   2639 O  O   . PRO C 1 63  ? 24.418  21.273  26.396  1.00 24.57 ? 62   PRO C O   1 
ATOM   2640 C  CB  . PRO C 1 63  ? 24.031  24.496  26.339  1.00 22.61 ? 62   PRO C CB  1 
ATOM   2641 C  CG  . PRO C 1 63  ? 23.032  24.111  25.364  1.00 20.44 ? 62   PRO C CG  1 
ATOM   2642 C  CD  . PRO C 1 63  ? 23.750  23.734  24.122  1.00 20.04 ? 62   PRO C CD  1 
ATOM   2643 N  N   . HIS C 1 64  ? 24.952  22.428  28.257  1.00 25.64 ? 63   HIS C N   1 
ATOM   2644 C  CA  . HIS C 1 64  ? 24.598  21.412  29.231  1.00 24.87 ? 63   HIS C CA  1 
ATOM   2645 C  C   . HIS C 1 64  ? 23.147  21.016  28.986  1.00 24.95 ? 63   HIS C C   1 
ATOM   2646 O  O   . HIS C 1 64  ? 22.275  21.874  28.816  1.00 25.18 ? 63   HIS C O   1 
ATOM   2647 C  CB  . HIS C 1 64  ? 24.750  21.937  30.687  1.00 25.19 ? 63   HIS C CB  1 
ATOM   2648 C  CG  . HIS C 1 64  ? 26.150  22.318  31.079  1.00 23.98 ? 63   HIS C CG  1 
ATOM   2649 N  ND1 . HIS C 1 64  ? 26.477  22.731  32.347  1.00 28.49 ? 63   HIS C ND1 1 
ATOM   2650 C  CD2 . HIS C 1 64  ? 27.306  22.345  30.371  1.00 27.31 ? 63   HIS C CD2 1 
ATOM   2651 C  CE1 . HIS C 1 64  ? 27.771  22.988  32.412  1.00 27.48 ? 63   HIS C CE1 1 
ATOM   2652 N  NE2 . HIS C 1 64  ? 28.299  22.759  31.224  1.00 27.42 ? 63   HIS C NE2 1 
ATOM   2653 N  N   . PHE C 1 65  ? 22.883  19.717  28.926  1.00 25.25 ? 64   PHE C N   1 
ATOM   2654 C  CA  . PHE C 1 65  ? 21.514  19.236  28.809  1.00 25.34 ? 64   PHE C CA  1 
ATOM   2655 C  C   . PHE C 1 65  ? 20.635  19.721  29.973  1.00 27.11 ? 64   PHE C C   1 
ATOM   2656 O  O   . PHE C 1 65  ? 20.948  19.506  31.160  1.00 28.48 ? 64   PHE C O   1 
ATOM   2657 C  CB  . PHE C 1 65  ? 21.511  17.699  28.755  1.00 22.98 ? 64   PHE C CB  1 
ATOM   2658 C  CG  . PHE C 1 65  ? 20.115  17.085  28.712  1.00 22.00 ? 64   PHE C CG  1 
ATOM   2659 C  CD1 . PHE C 1 65  ? 19.172  17.495  27.773  1.00 23.16 ? 64   PHE C CD1 1 
ATOM   2660 C  CD2 . PHE C 1 65  ? 19.779  16.034  29.576  1.00 24.64 ? 64   PHE C CD2 1 
ATOM   2661 C  CE1 . PHE C 1 65  ? 17.909  16.905  27.712  1.00 22.13 ? 64   PHE C CE1 1 
ATOM   2662 C  CE2 . PHE C 1 65  ? 18.502  15.412  29.508  1.00 20.89 ? 64   PHE C CE2 1 
ATOM   2663 C  CZ  . PHE C 1 65  ? 17.575  15.832  28.583  1.00 20.96 ? 64   PHE C CZ  1 
ATOM   2664 N  N   . ASN C 1 66  ? 19.527  20.369  29.625  1.00 29.17 ? 65   ASN C N   1 
ATOM   2665 C  CA  . ASN C 1 66  ? 18.601  20.928  30.607  1.00 32.32 ? 65   ASN C CA  1 
ATOM   2666 C  C   . ASN C 1 66  ? 17.232  21.165  30.019  1.00 33.67 ? 65   ASN C C   1 
ATOM   2667 O  O   . ASN C 1 66  ? 16.890  22.269  29.583  1.00 34.92 ? 65   ASN C O   1 
ATOM   2668 C  CB  . ASN C 1 66  ? 19.134  22.239  31.161  1.00 32.42 ? 65   ASN C CB  1 
ATOM   2669 C  CG  . ASN C 1 66  ? 18.693  22.465  32.571  1.00 34.32 ? 65   ASN C CG  1 
ATOM   2670 O  OD1 . ASN C 1 66  ? 18.503  21.493  33.332  1.00 37.36 ? 65   ASN C OD1 1 
ATOM   2671 N  ND2 . ASN C 1 66  ? 18.485  23.732  32.937  1.00 35.32 ? 65   ASN C ND2 1 
ATOM   2672 N  N   . PRO C 1 67  ? 16.421  20.126  30.070  1.00 34.93 ? 66   PRO C N   1 
ATOM   2673 C  CA  . PRO C 1 67  ? 15.120  20.100  29.410  1.00 36.37 ? 66   PRO C CA  1 
ATOM   2674 C  C   . PRO C 1 67  ? 14.113  21.184  29.812  1.00 37.49 ? 66   PRO C C   1 
ATOM   2675 O  O   . PRO C 1 67  ? 13.325  21.620  28.949  1.00 38.56 ? 66   PRO C O   1 
ATOM   2676 C  CB  . PRO C 1 67  ? 14.596  18.707  29.786  1.00 36.27 ? 66   PRO C CB  1 
ATOM   2677 C  CG  . PRO C 1 67  ? 15.287  18.431  31.058  1.00 35.37 ? 66   PRO C CG  1 
ATOM   2678 C  CD  . PRO C 1 67  ? 16.686  18.896  30.818  1.00 34.74 ? 66   PRO C CD  1 
ATOM   2679 N  N   . LEU C 1 68  ? 14.125  21.650  31.087  1.00 36.41 ? 67   LEU C N   1 
ATOM   2680 C  CA  . LEU C 1 68  ? 13.110  22.626  31.534  1.00 36.80 ? 67   LEU C CA  1 
ATOM   2681 C  C   . LEU C 1 68  ? 13.657  24.036  31.872  1.00 37.34 ? 67   LEU C C   1 
ATOM   2682 O  O   . LEU C 1 68  ? 13.267  25.022  31.238  1.00 37.99 ? 67   LEU C O   1 
ATOM   2683 C  CB  . LEU C 1 68  ? 12.296  21.980  32.663  1.00 36.21 ? 67   LEU C CB  1 
ATOM   2684 C  CG  . LEU C 1 68  ? 11.023  21.250  32.219  1.00 35.69 ? 67   LEU C CG  1 
ATOM   2685 C  CD1 . LEU C 1 68  ? 10.730  21.573  30.750  1.00 35.85 ? 67   LEU C CD1 1 
ATOM   2686 C  CD2 . LEU C 1 68  ? 11.145  19.745  32.412  1.00 34.22 ? 67   LEU C CD2 1 
ATOM   2687 N  N   . SER C 1 69  ? 14.543  24.187  32.816  1.00 37.70 ? 68   SER C N   1 
ATOM   2688 C  CA  . SER C 1 69  ? 15.051  25.530  33.065  1.00 37.72 ? 68   SER C CA  1 
ATOM   2689 C  CB  . SER C 1 69  ? 14.023  26.616  32.720  1.00 37.66 ? 68   SER C CB  1 
ATOM   2690 N  N   . ARG C 1 80  ? 20.673  22.064  39.995  1.00 32.07 ? 79   ARG C N   1 
ATOM   2691 C  CA  . ARG C 1 80  ? 21.600  21.769  38.905  1.00 32.06 ? 79   ARG C CA  1 
ATOM   2692 C  C   . ARG C 1 80  ? 20.905  21.517  37.588  1.00 31.72 ? 79   ARG C C   1 
ATOM   2693 O  O   . ARG C 1 80  ? 19.679  21.369  37.520  1.00 33.08 ? 79   ARG C O   1 
ATOM   2694 C  CB  . ARG C 1 80  ? 22.448  20.519  39.206  1.00 32.21 ? 79   ARG C CB  1 
ATOM   2695 C  CG  . ARG C 1 80  ? 21.628  19.284  39.557  1.00 32.22 ? 79   ARG C CG  1 
ATOM   2696 C  CD  . ARG C 1 80  ? 21.947  18.075  38.704  1.00 35.63 ? 79   ARG C CD  1 
ATOM   2697 N  NE  . ARG C 1 80  ? 22.074  16.860  39.503  1.00 37.08 ? 79   ARG C NE  1 
ATOM   2698 C  CZ  . ARG C 1 80  ? 22.301  15.650  38.995  1.00 34.75 ? 79   ARG C CZ  1 
ATOM   2699 N  NH1 . ARG C 1 80  ? 22.423  15.481  37.682  1.00 33.76 ? 79   ARG C NH1 1 
ATOM   2700 N  NH2 . ARG C 1 80  ? 22.415  14.608  39.821  1.00 33.60 ? 79   ARG C NH2 1 
ATOM   2701 N  N   . HIS C 1 81  ? 21.710  21.448  36.536  1.00 31.26 ? 80   HIS C N   1 
ATOM   2702 C  CA  . HIS C 1 81  ? 21.224  21.051  35.225  1.00 29.57 ? 80   HIS C CA  1 
ATOM   2703 C  C   . HIS C 1 81  ? 21.089  19.521  35.226  1.00 28.91 ? 80   HIS C C   1 
ATOM   2704 O  O   . HIS C 1 81  ? 21.818  18.818  35.926  1.00 29.20 ? 80   HIS C O   1 
ATOM   2705 C  CB  . HIS C 1 81  ? 22.194  21.511  34.117  1.00 29.19 ? 80   HIS C CB  1 
ATOM   2706 N  N   . VAL C 1 82  ? 20.148  19.012  34.449  1.00 28.88 ? 81   VAL C N   1 
ATOM   2707 C  CA  . VAL C 1 82  ? 19.972  17.566  34.333  1.00 28.12 ? 81   VAL C CA  1 
ATOM   2708 C  C   . VAL C 1 82  ? 21.275  16.899  33.928  1.00 28.64 ? 81   VAL C C   1 
ATOM   2709 O  O   . VAL C 1 82  ? 21.694  15.940  34.556  1.00 31.75 ? 81   VAL C O   1 
ATOM   2710 C  CB  . VAL C 1 82  ? 18.822  17.189  33.397  1.00 27.35 ? 81   VAL C CB  1 
ATOM   2711 C  CG1 . VAL C 1 82  ? 18.774  15.675  33.200  1.00 26.45 ? 81   VAL C CG1 1 
ATOM   2712 C  CG2 . VAL C 1 82  ? 17.478  17.638  33.989  1.00 27.61 ? 81   VAL C CG2 1 
ATOM   2713 N  N   . GLY C 1 83  ? 21.942  17.405  32.907  1.00 29.36 ? 82   GLY C N   1 
ATOM   2714 C  CA  . GLY C 1 83  ? 23.255  16.895  32.514  1.00 29.21 ? 82   GLY C CA  1 
ATOM   2715 C  C   . GLY C 1 83  ? 24.464  16.954  33.471  1.00 28.37 ? 82   GLY C C   1 
ATOM   2716 O  O   . GLY C 1 83  ? 25.507  16.345  33.166  1.00 29.99 ? 82   GLY C O   1 
ATOM   2717 N  N   . ASP C 1 84  ? 24.332  17.654  34.603  1.00 27.17 ? 83   ASP C N   1 
ATOM   2718 C  CA  . ASP C 1 84  ? 25.441  17.871  35.553  1.00 25.79 ? 83   ASP C CA  1 
ATOM   2719 C  C   . ASP C 1 84  ? 25.828  16.650  36.393  1.00 24.62 ? 83   ASP C C   1 
ATOM   2720 O  O   . ASP C 1 84  ? 25.208  16.375  37.382  1.00 26.78 ? 83   ASP C O   1 
ATOM   2721 C  CB  . ASP C 1 84  ? 25.119  19.078  36.442  1.00 25.69 ? 83   ASP C CB  1 
ATOM   2722 C  CG  . ASP C 1 84  ? 26.252  19.451  37.409  1.00 25.92 ? 83   ASP C CG  1 
ATOM   2723 O  OD1 . ASP C 1 84  ? 27.258  18.707  37.530  0.50 27.04 ? 83   ASP C OD1 1 
ATOM   2724 O  OD2 . ASP C 1 84  ? 26.198  20.494  38.115  0.50 27.23 ? 83   ASP C OD2 1 
ATOM   2725 N  N   . LEU C 1 85  ? 26.877  15.943  35.999  1.00 23.69 ? 84   LEU C N   1 
ATOM   2726 C  CA  . LEU C 1 85  ? 27.330  14.763  36.708  1.00 22.84 ? 84   LEU C CA  1 
ATOM   2727 C  C   . LEU C 1 85  ? 28.590  15.047  37.577  1.00 23.15 ? 84   LEU C C   1 
ATOM   2728 O  O   . LEU C 1 85  ? 29.376  14.161  37.872  1.00 26.28 ? 84   LEU C O   1 
ATOM   2729 C  CB  . LEU C 1 85  ? 27.555  13.630  35.674  1.00 21.44 ? 84   LEU C CB  1 
ATOM   2730 C  CG  . LEU C 1 85  ? 26.364  13.185  34.809  1.00 20.71 ? 84   LEU C CG  1 
ATOM   2731 C  CD1 . LEU C 1 85  ? 26.855  12.066  33.821  1.00 21.70 ? 84   LEU C CD1 1 
ATOM   2732 C  CD2 . LEU C 1 85  ? 25.207  12.793  35.699  1.00 27.18 ? 84   LEU C CD2 1 
ATOM   2733 N  N   . GLY C 1 86  ? 28.823  16.305  37.947  1.00 23.12 ? 85   GLY C N   1 
ATOM   2734 C  CA  . GLY C 1 86  ? 29.952  16.645  38.805  1.00 22.06 ? 85   GLY C CA  1 
ATOM   2735 C  C   . GLY C 1 86  ? 31.299  16.606  38.089  1.00 21.69 ? 85   GLY C C   1 
ATOM   2736 O  O   . GLY C 1 86  ? 31.434  17.052  36.935  1.00 22.81 ? 85   GLY C O   1 
ATOM   2737 N  N   . ASN C 1 87  ? 32.291  16.049  38.764  1.00 21.56 ? 86   ASN C N   1 
ATOM   2738 C  CA  . ASN C 1 87  ? 33.629  15.903  38.228  1.00 22.02 ? 86   ASN C CA  1 
ATOM   2739 C  C   . ASN C 1 87  ? 34.073  14.472  38.229  1.00 21.52 ? 86   ASN C C   1 
ATOM   2740 O  O   . ASN C 1 87  ? 33.540  13.642  38.952  1.00 24.69 ? 86   ASN C O   1 
ATOM   2741 C  CB  . ASN C 1 87  ? 34.678  16.656  39.041  1.00 21.42 ? 86   ASN C CB  1 
ATOM   2742 C  CG  . ASN C 1 87  ? 34.443  18.136  39.091  1.00 22.51 ? 86   ASN C CG  1 
ATOM   2743 O  OD1 . ASN C 1 87  ? 34.518  18.824  38.077  1.00 22.26 ? 86   ASN C OD1 1 
ATOM   2744 N  ND2 . ASN C 1 87  ? 34.187  18.645  40.288  1.00 26.31 ? 86   ASN C ND2 1 
ATOM   2745 N  N   . VAL C 1 88  ? 35.039  14.185  37.381  1.00 23.58 ? 87   VAL C N   1 
ATOM   2746 C  CA  . VAL C 1 88  ? 35.696  12.920  37.491  1.00 23.32 ? 87   VAL C CA  1 
ATOM   2747 C  C   . VAL C 1 88  ? 37.109  13.333  37.931  1.00 23.19 ? 87   VAL C C   1 
ATOM   2748 O  O   . VAL C 1 88  ? 37.542  14.498  37.756  1.00 26.04 ? 87   VAL C O   1 
ATOM   2749 C  CB  . VAL C 1 88  ? 35.584  12.025  36.206  1.00 20.98 ? 87   VAL C CB  1 
ATOM   2750 C  CG1 . VAL C 1 88  ? 34.037  11.581  35.901  1.00 21.05 ? 87   VAL C CG1 1 
ATOM   2751 C  CG2 . VAL C 1 88  ? 36.338  12.638  35.004  1.00 23.52 ? 87   VAL C CG2 1 
ATOM   2752 N  N   . THR C 1 89  ? 37.831  12.400  38.525  1.00 24.76 ? 88   THR C N   1 
ATOM   2753 C  CA  . THR C 1 89  ? 39.123  12.691  39.100  1.00 24.97 ? 88   THR C CA  1 
ATOM   2754 C  C   . THR C 1 89  ? 40.252  11.866  38.490  1.00 25.54 ? 88   THR C C   1 
ATOM   2755 O  O   . THR C 1 89  ? 40.264  10.631  38.582  1.00 27.11 ? 88   THR C O   1 
ATOM   2756 C  CB  . THR C 1 89  ? 39.099  12.475  40.623  1.00 25.43 ? 88   THR C CB  1 
ATOM   2757 O  OG1 . THR C 1 89  ? 37.989  13.163  41.219  1.00 25.49 ? 88   THR C OG1 1 
ATOM   2758 C  CG2 . THR C 1 89  ? 40.300  13.126  41.251  1.00 24.21 ? 88   THR C CG2 1 
ATOM   2759 N  N   . ALA C 1 90  ? 41.206  12.544  37.877  1.00 25.52 ? 89   ALA C N   1 
ATOM   2760 C  CA  . ALA C 1 90  ? 42.338  11.822  37.298  1.00 26.32 ? 89   ALA C CA  1 
ATOM   2761 C  C   . ALA C 1 90  ? 43.449  11.691  38.310  1.00 26.54 ? 89   ALA C C   1 
ATOM   2762 O  O   . ALA C 1 90  ? 43.812  12.667  38.980  1.00 26.67 ? 89   ALA C O   1 
ATOM   2763 C  CB  . ALA C 1 90  ? 42.862  12.524  36.046  1.00 26.29 ? 89   ALA C CB  1 
ATOM   2764 N  N   . ASP C 1 91  ? 43.994  10.479  38.417  1.00 27.29 ? 90   ASP C N   1 
ATOM   2765 C  CA  . ASP C 1 91  ? 45.152  10.224  39.269  1.00 26.98 ? 90   ASP C CA  1 
ATOM   2766 C  C   . ASP C 1 91  ? 46.474  10.726  38.657  1.00 27.30 ? 90   ASP C C   1 
ATOM   2767 O  O   . ASP C 1 91  ? 46.489  11.464  37.654  1.00 27.33 ? 90   ASP C O   1 
ATOM   2768 C  CB  . ASP C 1 91  ? 45.249  8.741   39.679  1.00 26.69 ? 90   ASP C CB  1 
ATOM   2769 C  CG  . ASP C 1 91  ? 45.540  7.807   38.505  1.00 27.20 ? 90   ASP C CG  1 
ATOM   2770 O  OD1 . ASP C 1 91  ? 45.997  8.285   37.452  1.00 25.64 ? 90   ASP C OD1 1 
ATOM   2771 O  OD2 . ASP C 1 91  ? 45.347  6.565   38.540  1.00 28.94 ? 90   ASP C OD2 1 
ATOM   2772 N  N   . LYS C 1 92  ? 47.580  10.325  39.268  1.00 27.23 ? 91   LYS C N   1 
ATOM   2773 C  CA  . LYS C 1 92  ? 48.883  10.794  38.829  1.00 27.17 ? 91   LYS C CA  1 
ATOM   2774 C  C   . LYS C 1 92  ? 49.212  10.295  37.432  1.00 27.29 ? 91   LYS C C   1 
ATOM   2775 O  O   . LYS C 1 92  ? 49.919  10.951  36.681  1.00 27.95 ? 91   LYS C O   1 
ATOM   2776 C  CB  . LYS C 1 92  ? 49.991  10.490  39.862  1.00 26.88 ? 91   LYS C CB  1 
ATOM   2777 C  CG  . LYS C 1 92  ? 50.009  9.075   40.481  1.00 27.09 ? 91   LYS C CG  1 
ATOM   2778 C  CD  . LYS C 1 92  ? 50.670  8.059   39.526  1.00 26.25 ? 91   LYS C CD  1 
ATOM   2779 N  N   . ASP C 1 93  ? 48.657  9.146   37.073  1.00 27.89 ? 92   ASP C N   1 
ATOM   2780 C  CA  . ASP C 1 93  ? 48.895  8.585   35.750  1.00 27.72 ? 92   ASP C CA  1 
ATOM   2781 C  C   . ASP C 1 93  ? 47.827  8.929   34.707  1.00 26.79 ? 92   ASP C C   1 
ATOM   2782 O  O   . ASP C 1 93  ? 47.629  8.163   33.762  1.00 26.98 ? 92   ASP C O   1 
ATOM   2783 C  CB  . ASP C 1 93  ? 49.057  7.068   35.856  1.00 28.57 ? 92   ASP C CB  1 
ATOM   2784 C  CG  . ASP C 1 93  ? 50.368  6.670   36.478  1.00 31.17 ? 92   ASP C CG  1 
ATOM   2785 O  OD1 . ASP C 1 93  ? 51.318  7.503   36.490  1.00 34.68 ? 92   ASP C OD1 1 
ATOM   2786 O  OD2 . ASP C 1 93  ? 50.554  5.532   36.979  1.00 34.33 ? 92   ASP C OD2 1 
ATOM   2787 N  N   . GLY C 1 94  ? 47.129  10.060  34.879  1.00 25.72 ? 93   GLY C N   1 
ATOM   2788 C  CA  . GLY C 1 94  ? 46.118  10.523  33.932  1.00 24.51 ? 93   GLY C CA  1 
ATOM   2789 C  C   . GLY C 1 94  ? 44.838  9.694   33.852  1.00 23.56 ? 93   GLY C C   1 
ATOM   2790 O  O   . GLY C 1 94  ? 44.000  9.871   32.955  1.00 24.98 ? 93   GLY C O   1 
ATOM   2791 N  N   . VAL C 1 95  ? 44.682  8.792   34.807  1.00 23.14 ? 94   VAL C N   1 
ATOM   2792 C  CA  . VAL C 1 95  ? 43.547  7.893   34.794  1.00 22.36 ? 94   VAL C CA  1 
ATOM   2793 C  C   . VAL C 1 95  ? 42.469  8.205   35.823  1.00 23.36 ? 94   VAL C C   1 
ATOM   2794 O  O   . VAL C 1 95  ? 42.712  8.210   37.037  1.00 24.66 ? 94   VAL C O   1 
ATOM   2795 C  CB  . VAL C 1 95  ? 43.965  6.426   34.919  1.00 21.90 ? 94   VAL C CB  1 
ATOM   2796 C  CG1 . VAL C 1 95  ? 42.732  5.546   34.755  1.00 19.10 ? 94   VAL C CG1 1 
ATOM   2797 C  CG2 . VAL C 1 95  ? 45.011  6.070   33.863  1.00 21.41 ? 94   VAL C CG2 1 
ATOM   2798 N  N   . ALA C 1 96  ? 41.273  8.469   35.311  1.00 24.28 ? 95   ALA C N   1 
ATOM   2799 C  CA  . ALA C 1 96  ? 40.126  8.703   36.143  1.00 25.22 ? 95   ALA C CA  1 
ATOM   2800 C  C   . ALA C 1 96  ? 39.215  7.494   36.118  1.00 25.47 ? 95   ALA C C   1 
ATOM   2801 O  O   . ALA C 1 96  ? 38.707  7.112   35.050  1.00 27.79 ? 95   ALA C O   1 
ATOM   2802 C  CB  . ALA C 1 96  ? 39.365  9.954   35.677  1.00 24.02 ? 95   ALA C CB  1 
ATOM   2803 N  N   . ASP C 1 97  ? 39.016  6.871   37.279  1.00 26.75 ? 96   ASP C N   1 
ATOM   2804 C  CA  . ASP C 1 97  ? 37.966  5.854   37.372  1.00 26.90 ? 96   ASP C CA  1 
ATOM   2805 C  C   . ASP C 1 97  ? 36.643  6.453   37.828  1.00 26.28 ? 96   ASP C C   1 
ATOM   2806 O  O   . ASP C 1 97  ? 36.558  7.260   38.798  1.00 26.96 ? 96   ASP C O   1 
ATOM   2807 C  CB  . ASP C 1 97  ? 38.367  4.650   38.211  1.00 27.88 ? 96   ASP C CB  1 
ATOM   2808 C  CG  . ASP C 1 97  ? 39.251  3.693   37.443  1.00 30.52 ? 96   ASP C CG  1 
ATOM   2809 O  OD1 . ASP C 1 97  ? 40.442  3.568   37.789  1.00 35.36 ? 96   ASP C OD1 1 
ATOM   2810 O  OD2 . ASP C 1 97  ? 38.843  3.039   36.461  1.00 35.60 ? 96   ASP C OD2 1 
ATOM   2811 N  N   . VAL C 1 98  ? 35.593  6.069   37.124  1.00 25.07 ? 97   VAL C N   1 
ATOM   2812 C  CA  . VAL C 1 98  ? 34.325  6.687   37.374  1.00 24.01 ? 97   VAL C CA  1 
ATOM   2813 C  C   . VAL C 1 98  ? 33.365  5.704   37.936  1.00 24.25 ? 97   VAL C C   1 
ATOM   2814 O  O   . VAL C 1 98  ? 33.278  4.588   37.463  1.00 26.92 ? 97   VAL C O   1 
ATOM   2815 C  CB  . VAL C 1 98  ? 33.758  7.347   36.080  1.00 22.14 ? 97   VAL C CB  1 
ATOM   2816 C  CG1 . VAL C 1 98  ? 32.339  7.961   36.307  1.00 22.70 ? 97   VAL C CG1 1 
ATOM   2817 C  CG2 . VAL C 1 98  ? 34.786  8.388   35.475  1.00 22.91 ? 97   VAL C CG2 1 
ATOM   2818 N  N   . SER C 1 99  ? 32.699  6.119   39.002  1.00 25.33 ? 98   SER C N   1 
ATOM   2819 C  CA  . SER C 1 99  ? 31.558  5.420   39.558  1.00 25.88 ? 98   SER C CA  1 
ATOM   2820 C  C   . SER C 1 99  ? 30.654  6.430   40.233  1.00 25.52 ? 98   SER C C   1 
ATOM   2821 O  O   . SER C 1 99  ? 30.959  6.919   41.330  1.00 27.02 ? 98   SER C O   1 
ATOM   2822 C  CB  . SER C 1 99  ? 31.970  4.341   40.553  1.00 25.18 ? 98   SER C CB  1 
ATOM   2823 O  OG  . SER C 1 99  ? 30.849  3.809   41.229  1.00 29.03 ? 98   SER C OG  1 
ATOM   2824 N  N   . ILE C 1 100 ? 29.525  6.676   39.583  1.00 26.20 ? 99   ILE C N   1 
ATOM   2825 C  CA  . ILE C 1 100 ? 28.539  7.646   39.996  1.00 25.34 ? 99   ILE C CA  1 
ATOM   2826 C  C   . ILE C 1 100 ? 27.131  7.051   39.939  1.00 25.87 ? 99   ILE C C   1 
ATOM   2827 O  O   . ILE C 1 100 ? 26.772  6.308   39.002  1.00 26.47 ? 99   ILE C O   1 
ATOM   2828 C  CB  . ILE C 1 100 ? 28.551  8.804   39.000  1.00 25.24 ? 99   ILE C CB  1 
ATOM   2829 C  CG1 . ILE C 1 100 ? 29.850  9.624   39.107  1.00 23.85 ? 99   ILE C CG1 1 
ATOM   2830 C  CG2 . ILE C 1 100 ? 27.282  9.615   39.166  1.00 24.57 ? 99   ILE C CG2 1 
ATOM   2831 C  CD1 . ILE C 1 100 ? 30.152  10.431  37.850  1.00 20.82 ? 99   ILE C CD1 1 
ATOM   2832 N  N   . GLU C 1 101 ? 26.324  7.405   40.937  1.00 26.30 ? 100  GLU C N   1 
ATOM   2833 C  CA  . GLU C 1 101 ? 24.906  7.142   40.892  1.00 25.79 ? 100  GLU C CA  1 
ATOM   2834 C  C   . GLU C 1 101 ? 24.145  8.470   40.780  1.00 26.18 ? 100  GLU C C   1 
ATOM   2835 O  O   . GLU C 1 101 ? 24.336  9.393   41.571  1.00 27.87 ? 100  GLU C O   1 
ATOM   2836 C  CB  . GLU C 1 101 ? 24.428  6.310   42.086  1.00 25.07 ? 100  GLU C CB  1 
ATOM   2837 C  CG  . GLU C 1 101 ? 22.912  6.254   42.217  1.00 25.43 ? 100  GLU C CG  1 
ATOM   2838 C  CD  . GLU C 1 101 ? 22.399  5.163   43.148  0.50 25.27 ? 100  GLU C CD  1 
ATOM   2839 O  OE1 . GLU C 1 101 ? 22.950  4.033   43.125  0.50 25.46 ? 100  GLU C OE1 1 
ATOM   2840 O  OE2 . GLU C 1 101 ? 21.438  5.445   43.904  0.50 24.44 ? 100  GLU C OE2 1 
ATOM   2841 N  N   . ASP C 1 102 ? 23.281  8.559   39.786  1.00 26.39 ? 101  ASP C N   1 
ATOM   2842 C  CA  . ASP C 1 102 ? 22.499  9.780   39.604  1.00 26.33 ? 101  ASP C CA  1 
ATOM   2843 C  C   . ASP C 1 102 ? 20.984  9.522   39.435  1.00 25.68 ? 101  ASP C C   1 
ATOM   2844 O  O   . ASP C 1 102 ? 20.549  8.635   38.682  1.00 26.52 ? 101  ASP C O   1 
ATOM   2845 C  CB  . ASP C 1 102 ? 23.070  10.613  38.462  1.00 26.02 ? 101  ASP C CB  1 
ATOM   2846 C  CG  . ASP C 1 102 ? 22.549  12.013  38.475  1.00 26.46 ? 101  ASP C CG  1 
ATOM   2847 O  OD1 . ASP C 1 102 ? 23.074  12.794  39.259  1.00 31.33 ? 101  ASP C OD1 1 
ATOM   2848 O  OD2 . ASP C 1 102 ? 21.567  12.387  37.808  1.00 31.07 ? 101  ASP C OD2 1 
ATOM   2849 N  N   . SER C 1 103 ? 20.192  10.352  40.093  1.00 25.53 ? 102  SER C N   1 
ATOM   2850 C  CA  . SER C 1 103 ? 18.752  10.188  40.099  1.00 25.29 ? 102  SER C CA  1 
ATOM   2851 C  C   . SER C 1 103 ? 18.004  11.249  39.318  1.00 24.62 ? 102  SER C C   1 
ATOM   2852 O  O   . SER C 1 103 ? 16.784  11.399  39.454  1.00 26.36 ? 102  SER C O   1 
ATOM   2853 C  CB  . SER C 1 103 ? 18.264  10.161  41.537  1.00 24.64 ? 102  SER C CB  1 
ATOM   2854 O  OG  . SER C 1 103 ? 18.448  8.867   42.109  1.00 28.96 ? 102  SER C OG  1 
ATOM   2855 N  N   . VAL C 1 104 ? 18.738  12.004  38.526  1.00 25.34 ? 103  VAL C N   1 
ATOM   2856 C  CA  . VAL C 1 104 ? 18.141  13.076  37.760  1.00 23.22 ? 103  VAL C CA  1 
ATOM   2857 C  C   . VAL C 1 104 ? 18.135  12.695  36.307  1.00 22.02 ? 103  VAL C C   1 
ATOM   2858 O  O   . VAL C 1 104 ? 17.096  12.790  35.661  1.00 25.40 ? 103  VAL C O   1 
ATOM   2859 C  CB  . VAL C 1 104 ? 18.864  14.388  37.997  1.00 21.92 ? 103  VAL C CB  1 
ATOM   2860 C  CG1 . VAL C 1 104 ? 18.207  15.479  37.142  1.00 21.98 ? 103  VAL C CG1 1 
ATOM   2861 C  CG2 . VAL C 1 104 ? 18.778  14.740  39.475  1.00 24.84 ? 103  VAL C CG2 1 
ATOM   2862 N  N   . ILE C 1 105 ? 19.269  12.242  35.804  1.00 23.74 ? 104  ILE C N   1 
ATOM   2863 C  CA  . ILE C 1 105 ? 19.359  11.741  34.446  1.00 22.78 ? 104  ILE C CA  1 
ATOM   2864 C  C   . ILE C 1 105 ? 18.546  10.463  34.393  1.00 23.13 ? 104  ILE C C   1 
ATOM   2865 O  O   . ILE C 1 105 ? 18.324  9.845   35.415  1.00 24.56 ? 104  ILE C O   1 
ATOM   2866 C  CB  . ILE C 1 105 ? 20.820  11.432  33.983  1.00 23.17 ? 104  ILE C CB  1 
ATOM   2867 C  CG1 . ILE C 1 105 ? 21.514  10.401  34.924  1.00 16.75 ? 104  ILE C CG1 1 
ATOM   2868 C  CG2 . ILE C 1 105 ? 21.574  12.771  33.715  1.00 19.21 ? 104  ILE C CG2 1 
ATOM   2869 C  CD1 . ILE C 1 105 ? 22.705  9.728   34.317  1.00 20.65 ? 104  ILE C CD1 1 
ATOM   2870 N  N   . SER C 1 106 ? 18.104  10.112  33.195  1.00 23.55 ? 105  SER C N   1 
ATOM   2871 C  CA  . SER C 1 106 ? 17.433  8.858   32.922  1.00 23.44 ? 105  SER C CA  1 
ATOM   2872 C  C   . SER C 1 106 ? 17.869  8.280   31.569  1.00 22.77 ? 105  SER C C   1 
ATOM   2873 O  O   . SER C 1 106 ? 18.448  8.988   30.709  1.00 26.84 ? 105  SER C O   1 
ATOM   2874 C  CB  . SER C 1 106 ? 15.897  9.053   33.011  1.00 20.04 ? 105  SER C CB  1 
ATOM   2875 O  OG  . SER C 1 106 ? 15.203  7.823   33.009  1.00 26.31 ? 105  SER C OG  1 
ATOM   2876 N  N   . LEU C 1 107 ? 17.692  6.977   31.412  1.00 23.01 ? 106  LEU C N   1 
ATOM   2877 C  CA  . LEU C 1 107 ? 17.898  6.328   30.128  1.00 21.25 ? 106  LEU C CA  1 
ATOM   2878 C  C   . LEU C 1 107 ? 16.590  6.258   29.287  1.00 21.89 ? 106  LEU C C   1 
ATOM   2879 O  O   . LEU C 1 107 ? 16.577  5.684   28.183  1.00 24.36 ? 106  LEU C O   1 
ATOM   2880 C  CB  . LEU C 1 107 ? 18.549  4.935   30.335  1.00 19.44 ? 106  LEU C CB  1 
ATOM   2881 C  CG  . LEU C 1 107 ? 19.971  4.961   30.936  1.00 18.51 ? 106  LEU C CG  1 
ATOM   2882 C  CD1 . LEU C 1 107 ? 20.708  3.592   30.917  1.00 21.17 ? 106  LEU C CD1 1 
ATOM   2883 C  CD2 . LEU C 1 107 ? 20.902  5.998   30.303  1.00 22.60 ? 106  LEU C CD2 1 
ATOM   2884 N  N   . SER C 1 108 ? 15.492  6.837   29.789  1.00 23.01 ? 107  SER C N   1 
ATOM   2885 C  CA  . SER C 1 108 ? 14.227  6.927   29.031  1.00 23.69 ? 107  SER C CA  1 
ATOM   2886 C  C   . SER C 1 108 ? 13.409  8.125   29.503  1.00 23.85 ? 107  SER C C   1 
ATOM   2887 O  O   . SER C 1 108 ? 13.800  8.801   30.447  1.00 25.65 ? 107  SER C O   1 
ATOM   2888 C  CB  . SER C 1 108 ? 13.380  5.622   29.136  1.00 21.64 ? 107  SER C CB  1 
ATOM   2889 O  OG  . SER C 1 108 ? 12.836  5.415   30.434  1.00 25.94 ? 107  SER C OG  1 
ATOM   2890 N  N   . GLY C 1 109 ? 12.283  8.393   28.847  1.00 26.02 ? 108  GLY C N   1 
ATOM   2891 C  CA  . GLY C 1 109 ? 11.447  9.532   29.188  1.00 26.30 ? 108  GLY C CA  1 
ATOM   2892 C  C   . GLY C 1 109 ? 12.073  10.901  28.935  1.00 26.99 ? 108  GLY C C   1 
ATOM   2893 O  O   . GLY C 1 109 ? 12.972  11.060  28.126  1.00 28.48 ? 108  GLY C O   1 
ATOM   2894 N  N   . ASP C 1 110 ? 11.591  11.899  29.667  1.00 28.66 ? 109  ASP C N   1 
ATOM   2895 C  CA  . ASP C 1 110 ? 11.950  13.301  29.437  1.00 28.13 ? 109  ASP C CA  1 
ATOM   2896 C  C   . ASP C 1 110 ? 13.360  13.695  29.852  1.00 27.60 ? 109  ASP C C   1 
ATOM   2897 O  O   . ASP C 1 110 ? 13.905  14.660  29.335  1.00 27.61 ? 109  ASP C O   1 
ATOM   2898 C  CB  . ASP C 1 110 ? 10.916  14.181  30.139  1.00 28.91 ? 109  ASP C CB  1 
ATOM   2899 C  CG  . ASP C 1 110 ? 11.233  15.669  30.056  1.00 31.45 ? 109  ASP C CG  1 
ATOM   2900 O  OD1 . ASP C 1 110 ? 11.173  16.242  28.940  1.00 35.36 ? 109  ASP C OD1 1 
ATOM   2901 O  OD2 . ASP C 1 110 ? 11.522  16.355  31.068  1.00 34.12 ? 109  ASP C OD2 1 
ATOM   2902 N  N   . HIS C 1 111 ? 13.972  12.939  30.757  1.00 27.54 ? 110  HIS C N   1 
ATOM   2903 C  CA  . HIS C 1 111 ? 15.335  13.241  31.146  1.00 27.01 ? 110  HIS C CA  1 
ATOM   2904 C  C   . HIS C 1 111 ? 16.301  12.292  30.437  1.00 26.91 ? 110  HIS C C   1 
ATOM   2905 O  O   . HIS C 1 111 ? 17.478  12.224  30.818  1.00 26.26 ? 110  HIS C O   1 
ATOM   2906 C  CB  . HIS C 1 111 ? 15.553  13.199  32.671  1.00 27.09 ? 110  HIS C CB  1 
ATOM   2907 C  CG  . HIS C 1 111 ? 14.905  14.321  33.425  1.00 25.37 ? 110  HIS C CG  1 
ATOM   2908 N  ND1 . HIS C 1 111 ? 15.149  14.541  34.763  1.00 28.21 ? 110  HIS C ND1 1 
ATOM   2909 C  CD2 . HIS C 1 111 ? 14.048  15.292  33.034  1.00 25.12 ? 110  HIS C CD2 1 
ATOM   2910 C  CE1 . HIS C 1 111 ? 14.464  15.596  35.167  1.00 27.99 ? 110  HIS C CE1 1 
ATOM   2911 N  NE2 . HIS C 1 111 ? 13.784  16.068  34.138  1.00 30.18 ? 110  HIS C NE2 1 
ATOM   2912 N  N   . CYS C 1 112 ? 15.797  11.600  29.401  1.00 27.28 ? 111  CYS C N   1 
ATOM   2913 C  CA  . CYS C 1 112 ? 16.600  10.654  28.643  1.00 25.86 ? 111  CYS C CA  1 
ATOM   2914 C  C   . CYS C 1 112 ? 17.865  11.295  27.998  1.00 23.67 ? 111  CYS C C   1 
ATOM   2915 O  O   . CYS C 1 112 ? 17.802  12.264  27.249  1.00 24.44 ? 111  CYS C O   1 
ATOM   2916 C  CB  . CYS C 1 112 ? 15.758  9.824   27.655  1.00 23.77 ? 111  CYS C CB  1 
ATOM   2917 S  SG  . CYS C 1 112 ? 16.684  8.691   26.581  1.00 30.89 ? 111  CYS C SG  1 
ATOM   2918 N  N   . ILE C 1 113 ? 18.992  10.688  28.282  1.00 23.43 ? 112  ILE C N   1 
ATOM   2919 C  CA  . ILE C 1 113 ? 20.306  11.160  27.804  1.00 22.55 ? 112  ILE C CA  1 
ATOM   2920 C  C   . ILE C 1 113 ? 20.823  10.349  26.597  1.00 22.79 ? 112  ILE C C   1 
ATOM   2921 O  O   . ILE C 1 113 ? 21.830  10.705  26.012  1.00 23.51 ? 112  ILE C O   1 
ATOM   2922 C  CB  . ILE C 1 113 ? 21.307  11.189  28.952  1.00 20.64 ? 112  ILE C CB  1 
ATOM   2923 C  CG1 . ILE C 1 113 ? 21.644  9.749   29.458  1.00 13.19 ? 112  ILE C CG1 1 
ATOM   2924 C  CG2 . ILE C 1 113 ? 20.826  12.127  30.105  1.00 18.36 ? 112  ILE C CG2 1 
ATOM   2925 C  CD1 . ILE C 1 113 ? 22.669  9.742   30.542  1.00 20.31 ? 112  ILE C CD1 1 
ATOM   2926 N  N   . ILE C 1 114 ? 20.155  9.226   26.269  1.00 23.94 ? 113  ILE C N   1 
ATOM   2927 C  CA  . ILE C 1 114 ? 20.478  8.539   25.032  1.00 23.18 ? 113  ILE C CA  1 
ATOM   2928 C  C   . ILE C 1 114 ? 20.343  9.412   23.753  1.00 22.18 ? 113  ILE C C   1 
ATOM   2929 O  O   . ILE C 1 114 ? 19.316  10.052  23.461  1.00 25.41 ? 113  ILE C O   1 
ATOM   2930 C  CB  . ILE C 1 114 ? 19.672  7.174   24.921  1.00 21.57 ? 113  ILE C CB  1 
ATOM   2931 C  CG1 . ILE C 1 114 ? 19.949  6.321   26.184  1.00 22.95 ? 113  ILE C CG1 1 
ATOM   2932 C  CG2 . ILE C 1 114 ? 19.923  6.597   23.519  1.00 23.39 ? 113  ILE C CG2 1 
ATOM   2933 C  CD1 . ILE C 1 114 ? 19.358  4.978   26.159  1.00 21.54 ? 113  ILE C CD1 1 
ATOM   2934 N  N   . GLY C 1 115 ? 21.427  9.488   22.985  1.00 23.14 ? 114  GLY C N   1 
ATOM   2935 C  CA  . GLY C 1 115 ? 21.462  10.238  21.753  1.00 22.62 ? 114  GLY C CA  1 
ATOM   2936 C  C   . GLY C 1 115 ? 22.018  11.620  22.074  1.00 19.44 ? 114  GLY C C   1 
ATOM   2937 O  O   . GLY C 1 115 ? 22.161  12.469  21.234  1.00 22.53 ? 114  GLY C O   1 
ATOM   2938 N  N   . ARG C 1 116 ? 22.401  11.855  23.320  1.00 22.58 ? 115  ARG C N   1 
ATOM   2939 C  CA  . ARG C 1 116 ? 22.950  13.118  23.592  1.00 21.87 ? 115  ARG C CA  1 
ATOM   2940 C  C   . ARG C 1 116 ? 24.473  12.803  23.735  1.00 22.49 ? 115  ARG C C   1 
ATOM   2941 O  O   . ARG C 1 116 ? 24.907  11.633  23.561  1.00 25.85 ? 115  ARG C O   1 
ATOM   2942 C  CB  . ARG C 1 116 ? 22.264  13.730  24.843  1.00 20.44 ? 115  ARG C CB  1 
ATOM   2943 C  CG  . ARG C 1 116 ? 20.768  13.875  24.625  1.00 17.25 ? 115  ARG C CG  1 
ATOM   2944 C  CD  . ARG C 1 116 ? 20.028  14.795  25.619  1.00 23.21 ? 115  ARG C CD  1 
ATOM   2945 N  NE  . ARG C 1 116 ? 18.578  14.727  25.440  1.00 21.83 ? 115  ARG C NE  1 
ATOM   2946 C  CZ  . ARG C 1 116 ? 17.882  15.577  24.685  1.00 20.14 ? 115  ARG C CZ  1 
ATOM   2947 N  NH1 . ARG C 1 116 ? 18.492  16.562  24.035  1.00 25.94 ? 115  ARG C NH1 1 
ATOM   2948 N  NH2 . ARG C 1 116 ? 16.563  15.458  24.569  1.00 23.40 ? 115  ARG C NH2 1 
ATOM   2949 N  N   . THR C 1 117 ? 25.268  13.810  24.011  1.00 21.26 ? 116  THR C N   1 
ATOM   2950 C  CA  . THR C 1 117 ? 26.725  13.733  24.216  1.00 19.98 ? 116  THR C CA  1 
ATOM   2951 C  C   . THR C 1 117 ? 27.206  13.846  25.683  1.00 20.12 ? 116  THR C C   1 
ATOM   2952 O  O   . THR C 1 117 ? 26.880  14.794  26.466  1.00 24.10 ? 116  THR C O   1 
ATOM   2953 C  CB  . THR C 1 117 ? 27.398  14.882  23.348  1.00 17.87 ? 116  THR C CB  1 
ATOM   2954 O  OG1 . THR C 1 117 ? 27.100  14.694  21.971  1.00 21.83 ? 116  THR C OG1 1 
ATOM   2955 C  CG2 . THR C 1 117 ? 28.967  15.010  23.473  1.00 15.68 ? 116  THR C CG2 1 
ATOM   2956 N  N   . LEU C 1 118 ? 28.000  12.870  26.076  1.00 20.17 ? 117  LEU C N   1 
ATOM   2957 C  CA  . LEU C 1 118 ? 28.792  12.982  27.290  1.00 18.98 ? 117  LEU C CA  1 
ATOM   2958 C  C   . LEU C 1 118 ? 30.130  13.703  26.980  1.00 19.25 ? 117  LEU C C   1 
ATOM   2959 O  O   . LEU C 1 118 ? 30.802  13.412  25.956  1.00 21.56 ? 117  LEU C O   1 
ATOM   2960 C  CB  . LEU C 1 118 ? 29.063  11.587  27.783  1.00 16.42 ? 117  LEU C CB  1 
ATOM   2961 C  CG  . LEU C 1 118 ? 29.820  11.503  29.126  1.00 14.89 ? 117  LEU C CG  1 
ATOM   2962 C  CD1 . LEU C 1 118 ? 28.986  12.057  30.260  1.00 22.01 ? 117  LEU C CD1 1 
ATOM   2963 C  CD2 . LEU C 1 118 ? 30.229  10.012  29.391  1.00 17.70 ? 117  LEU C CD2 1 
ATOM   2964 N  N   . VAL C 1 119 ? 30.517  14.660  27.820  1.00 19.97 ? 118  VAL C N   1 
ATOM   2965 C  CA  . VAL C 1 119 ? 31.740  15.484  27.667  1.00 19.06 ? 118  VAL C CA  1 
ATOM   2966 C  C   . VAL C 1 119 ? 32.541  15.592  28.976  1.00 17.72 ? 118  VAL C C   1 
ATOM   2967 O  O   . VAL C 1 119 ? 32.013  15.903  30.073  1.00 21.23 ? 118  VAL C O   1 
ATOM   2968 C  CB  . VAL C 1 119 ? 31.394  17.015  27.278  1.00 15.62 ? 118  VAL C CB  1 
ATOM   2969 C  CG1 . VAL C 1 119 ? 32.658  17.877  27.202  1.00 18.95 ? 118  VAL C CG1 1 
ATOM   2970 C  CG2 . VAL C 1 119 ? 30.617  17.125  25.955  1.00 20.41 ? 118  VAL C CG2 1 
ATOM   2971 N  N   . VAL C 1 120 ? 33.804  15.264  28.896  1.00 19.76 ? 119  VAL C N   1 
ATOM   2972 C  CA  . VAL C 1 120 ? 34.746  15.504  29.948  1.00 19.62 ? 119  VAL C CA  1 
ATOM   2973 C  C   . VAL C 1 120 ? 35.529  16.806  29.683  1.00 19.88 ? 119  VAL C C   1 
ATOM   2974 O  O   . VAL C 1 120 ? 36.280  16.951  28.680  1.00 21.58 ? 119  VAL C O   1 
ATOM   2975 C  CB  . VAL C 1 120 ? 35.697  14.344  30.120  1.00 18.48 ? 119  VAL C CB  1 
ATOM   2976 C  CG1 . VAL C 1 120 ? 36.449  14.036  28.844  1.00 22.03 ? 119  VAL C CG1 1 
ATOM   2977 C  CG2 . VAL C 1 120 ? 36.614  14.620  31.260  1.00 19.58 ? 119  VAL C CG2 1 
ATOM   2978 N  N   . HIS C 1 121 ? 35.376  17.742  30.608  1.00 22.02 ? 120  HIS C N   1 
ATOM   2979 C  CA  . HIS C 1 121 ? 35.984  19.060  30.457  1.00 20.18 ? 120  HIS C CA  1 
ATOM   2980 C  C   . HIS C 1 121 ? 37.445  19.281  30.918  1.00 21.62 ? 120  HIS C C   1 
ATOM   2981 O  O   . HIS C 1 121 ? 38.003  18.546  31.740  1.00 23.38 ? 120  HIS C O   1 
ATOM   2982 C  CB  . HIS C 1 121 ? 35.083  20.092  31.097  1.00 20.06 ? 120  HIS C CB  1 
ATOM   2983 C  CG  . HIS C 1 121 ? 33.790  20.307  30.371  1.00 20.92 ? 120  HIS C CG  1 
ATOM   2984 N  ND1 . HIS C 1 121 ? 33.519  21.457  29.658  1.00 23.94 ? 120  HIS C ND1 1 
ATOM   2985 C  CD2 . HIS C 1 121 ? 32.683  19.536  30.280  1.00 21.12 ? 120  HIS C CD2 1 
ATOM   2986 C  CE1 . HIS C 1 121 ? 32.301  21.377  29.153  1.00 21.28 ? 120  HIS C CE1 1 
ATOM   2987 N  NE2 . HIS C 1 121 ? 31.767  20.226  29.529  1.00 21.95 ? 120  HIS C NE2 1 
ATOM   2988 N  N   . GLU C 1 122 ? 38.059  20.340  30.408  1.00 23.54 ? 121  GLU C N   1 
ATOM   2989 C  CA  . GLU C 1 122 ? 39.438  20.687  30.806  1.00 23.41 ? 121  GLU C CA  1 
ATOM   2990 C  C   . GLU C 1 122 ? 39.603  20.942  32.307  1.00 23.86 ? 121  GLU C C   1 
ATOM   2991 O  O   . GLU C 1 122 ? 40.436  20.310  32.967  1.00 24.41 ? 121  GLU C O   1 
ATOM   2992 C  CB  . GLU C 1 122 ? 39.973  21.895  30.036  1.00 22.52 ? 121  GLU C CB  1 
ATOM   2993 C  CG  . GLU C 1 122 ? 41.467  22.101  30.245  1.00 26.36 ? 121  GLU C CG  1 
ATOM   2994 C  CD  . GLU C 1 122 ? 42.057  23.125  29.299  1.00 32.22 ? 121  GLU C CD  1 
ATOM   2995 O  OE1 . GLU C 1 122 ? 43.270  23.013  29.004  1.00 37.56 ? 121  GLU C OE1 1 
ATOM   2996 O  OE2 . GLU C 1 122 ? 41.318  24.040  28.848  1.00 32.79 ? 121  GLU C OE2 1 
ATOM   2997 N  N   . LYS C 1 123 ? 38.809  21.857  32.852  1.00 24.12 ? 122  LYS C N   1 
ATOM   2998 C  CA  . LYS C 1 123 ? 38.925  22.218  34.255  1.00 24.18 ? 122  LYS C CA  1 
ATOM   2999 C  C   . LYS C 1 123 ? 37.806  21.643  35.118  1.00 25.24 ? 122  LYS C C   1 
ATOM   3000 O  O   . LYS C 1 123 ? 36.728  21.304  34.607  1.00 26.33 ? 122  LYS C O   1 
ATOM   3001 C  CB  . LYS C 1 123 ? 38.881  23.739  34.397  1.00 23.51 ? 122  LYS C CB  1 
ATOM   3002 C  CG  . LYS C 1 123 ? 39.619  24.572  33.355  1.00 23.04 ? 122  LYS C CG  1 
ATOM   3003 N  N   . ALA C 1 124 ? 38.055  21.532  36.423  1.00 26.57 ? 123  ALA C N   1 
ATOM   3004 C  CA  . ALA C 1 124 ? 37.020  21.141  37.376  1.00 27.55 ? 123  ALA C CA  1 
ATOM   3005 C  C   . ALA C 1 124 ? 35.773  22.031  37.291  1.00 28.62 ? 123  ALA C C   1 
ATOM   3006 O  O   . ALA C 1 124 ? 35.867  23.226  36.963  1.00 29.23 ? 123  ALA C O   1 
ATOM   3007 C  CB  . ALA C 1 124 ? 37.562  21.169  38.767  1.00 27.12 ? 123  ALA C CB  1 
ATOM   3008 N  N   . ASP C 1 125 ? 34.615  21.423  37.558  1.00 29.87 ? 124  ASP C N   1 
ATOM   3009 C  CA  . ASP C 1 125 ? 33.327  22.113  37.638  1.00 30.72 ? 124  ASP C CA  1 
ATOM   3010 C  C   . ASP C 1 125 ? 33.467  23.211  38.683  1.00 31.27 ? 124  ASP C C   1 
ATOM   3011 O  O   . ASP C 1 125 ? 33.924  22.961  39.819  1.00 32.48 ? 124  ASP C O   1 
ATOM   3012 C  CB  . ASP C 1 125 ? 32.250  21.147  38.129  1.00 30.88 ? 124  ASP C CB  1 
ATOM   3013 C  CG  . ASP C 1 125 ? 31.023  21.154  37.266  1.00 31.90 ? 124  ASP C CG  1 
ATOM   3014 O  OD1 . ASP C 1 125 ? 31.166  21.538  36.092  1.00 35.16 ? 124  ASP C OD1 1 
ATOM   3015 O  OD2 . ASP C 1 125 ? 29.883  20.751  37.655  1.00 34.14 ? 124  ASP C OD2 1 
ATOM   3016 N  N   . GLY C 1 142 ? 35.754  23.965  31.676  1.00 32.84 ? 141  GLY C N   1 
ATOM   3017 C  CA  . GLY C 1 142 ? 36.975  23.862  30.906  1.00 31.01 ? 141  GLY C CA  1 
ATOM   3018 C  C   . GLY C 1 142 ? 36.664  23.651  29.440  1.00 31.06 ? 141  GLY C C   1 
ATOM   3019 O  O   . GLY C 1 142 ? 35.495  23.393  29.095  1.00 31.34 ? 141  GLY C O   1 
ATOM   3020 N  N   . SER C 1 143 ? 37.688  23.826  28.581  1.00 30.31 ? 142  SER C N   1 
ATOM   3021 C  CA  . SER C 1 143 ? 37.568  23.570  27.159  1.00 28.39 ? 142  SER C CA  1 
ATOM   3022 C  C   . SER C 1 143 ? 37.097  22.104  27.113  1.00 26.61 ? 142  SER C C   1 
ATOM   3023 O  O   . SER C 1 143 ? 37.068  21.442  28.148  1.00 27.37 ? 142  SER C O   1 
ATOM   3024 C  CB  . SER C 1 143 ? 38.904  23.814  26.437  1.00 28.55 ? 142  SER C CB  1 
ATOM   3025 O  OG  . SER C 1 143 ? 39.513  22.612  25.969  1.00 30.32 ? 142  SER C OG  1 
ATOM   3026 N  N   . ARG C 1 144 ? 36.671  21.614  25.959  1.00 25.73 ? 143  ARG C N   1 
ATOM   3027 C  CA  . ARG C 1 144 ? 36.113  20.248  25.920  1.00 24.51 ? 143  ARG C CA  1 
ATOM   3028 C  C   . ARG C 1 144 ? 37.148  19.256  25.458  1.00 24.70 ? 143  ARG C C   1 
ATOM   3029 O  O   . ARG C 1 144 ? 37.420  19.160  24.266  1.00 26.65 ? 143  ARG C O   1 
ATOM   3030 C  CB  . ARG C 1 144 ? 34.863  20.192  25.027  1.00 23.86 ? 143  ARG C CB  1 
ATOM   3031 C  CG  . ARG C 1 144 ? 33.745  21.068  25.556  1.00 22.40 ? 143  ARG C CG  1 
ATOM   3032 C  CD  . ARG C 1 144 ? 32.601  21.297  24.572  1.00 22.52 ? 143  ARG C CD  1 
ATOM   3033 N  NE  . ARG C 1 144 ? 31.638  22.249  25.123  1.00 26.15 ? 143  ARG C NE  1 
ATOM   3034 C  CZ  . ARG C 1 144 ? 30.398  22.390  24.695  1.00 22.12 ? 143  ARG C CZ  1 
ATOM   3035 N  NH1 . ARG C 1 144 ? 29.916  21.613  23.719  1.00 27.01 ? 143  ARG C NH1 1 
ATOM   3036 N  NH2 . ARG C 1 144 ? 29.629  23.310  25.260  1.00 23.86 ? 143  ARG C NH2 1 
ATOM   3037 N  N   . LEU C 1 145 ? 37.652  18.467  26.397  1.00 25.01 ? 144  LEU C N   1 
ATOM   3038 C  CA  . LEU C 1 145 ? 38.694  17.469  26.150  1.00 24.64 ? 144  LEU C CA  1 
ATOM   3039 C  C   . LEU C 1 145 ? 38.371  16.237  25.277  1.00 24.81 ? 144  LEU C C   1 
ATOM   3040 O  O   . LEU C 1 145 ? 39.161  15.904  24.383  1.00 25.78 ? 144  LEU C O   1 
ATOM   3041 C  CB  . LEU C 1 145 ? 39.309  17.029  27.486  1.00 24.13 ? 144  LEU C CB  1 
ATOM   3042 C  CG  . LEU C 1 145 ? 39.863  18.181  28.348  1.00 22.90 ? 144  LEU C CG  1 
ATOM   3043 C  CD1 . LEU C 1 145 ? 40.590  17.648  29.558  1.00 19.99 ? 144  LEU C CD1 1 
ATOM   3044 C  CD2 . LEU C 1 145 ? 40.754  19.088  27.566  1.00 18.92 ? 144  LEU C CD2 1 
ATOM   3045 N  N   . ALA C 1 146 ? 37.240  15.583  25.542  1.00 23.90 ? 145  ALA C N   1 
ATOM   3046 C  CA  . ALA C 1 146 ? 36.775  14.412  24.804  1.00 22.37 ? 145  ALA C CA  1 
ATOM   3047 C  C   . ALA C 1 146 ? 35.273  14.296  25.000  1.00 22.29 ? 145  ALA C C   1 
ATOM   3048 O  O   . ALA C 1 146 ? 34.733  14.777  26.036  1.00 25.55 ? 145  ALA C O   1 
ATOM   3049 C  CB  . ALA C 1 146 ? 37.472  13.160  25.302  1.00 18.16 ? 145  ALA C CB  1 
ATOM   3050 N  N   . CYS C 1 147 ? 34.606  13.671  24.030  1.00 22.88 ? 146  CYS C N   1 
ATOM   3051 C  CA  . CYS C 1 147 ? 33.175  13.394  24.018  1.00 22.62 ? 146  CYS C CA  1 
ATOM   3052 C  C   . CYS C 1 147 ? 32.796  12.192  23.163  1.00 21.49 ? 146  CYS C C   1 
ATOM   3053 O  O   . CYS C 1 147 ? 33.646  11.628  22.431  1.00 22.80 ? 146  CYS C O   1 
ATOM   3054 C  CB  . CYS C 1 147 ? 32.371  14.617  23.535  1.00 20.71 ? 146  CYS C CB  1 
ATOM   3055 S  SG  . CYS C 1 147 ? 32.825  15.240  21.921  1.00 26.09 ? 146  CYS C SG  1 
ATOM   3056 N  N   . GLY C 1 148 ? 31.492  11.914  23.148  1.00 22.58 ? 147  GLY C N   1 
ATOM   3057 C  CA  . GLY C 1 148 ? 30.870  10.761  22.480  1.00 20.69 ? 147  GLY C CA  1 
ATOM   3058 C  C   . GLY C 1 148 ? 29.389  10.862  22.625  1.00 18.53 ? 147  GLY C C   1 
ATOM   3059 O  O   . GLY C 1 148 ? 28.872  11.405  23.667  1.00 22.88 ? 147  GLY C O   1 
ATOM   3060 N  N   . VAL C 1 149 ? 28.683  10.369  21.627  1.00 20.60 ? 148  VAL C N   1 
ATOM   3061 C  CA  . VAL C 1 149 ? 27.235  10.314  21.696  1.00 18.96 ? 148  VAL C CA  1 
ATOM   3062 C  C   . VAL C 1 149 ? 26.860  9.085   22.611  1.00 19.87 ? 148  VAL C C   1 
ATOM   3063 O  O   . VAL C 1 149 ? 27.425  8.027   22.483  1.00 23.88 ? 148  VAL C O   1 
ATOM   3064 C  CB  . VAL C 1 149 ? 26.617  10.230  20.282  1.00 17.13 ? 148  VAL C CB  1 
ATOM   3065 C  CG1 . VAL C 1 149 ? 25.010  10.252  20.304  1.00 17.43 ? 148  VAL C CG1 1 
ATOM   3066 C  CG2 . VAL C 1 149 ? 27.259  11.277  19.239  1.00 21.64 ? 148  VAL C CG2 1 
ATOM   3067 N  N   . ILE C 1 150 ? 25.938  9.215   23.542  1.00 20.31 ? 149  ILE C N   1 
ATOM   3068 C  CA  . ILE C 1 150 ? 25.476  8.045   24.338  1.00 20.19 ? 149  ILE C CA  1 
ATOM   3069 C  C   . ILE C 1 150 ? 24.560  7.126   23.526  1.00 18.98 ? 149  ILE C C   1 
ATOM   3070 O  O   . ILE C 1 150 ? 23.457  7.486   23.017  1.00 21.49 ? 149  ILE C O   1 
ATOM   3071 C  CB  . ILE C 1 150 ? 24.818  8.577   25.583  1.00 18.18 ? 149  ILE C CB  1 
ATOM   3072 C  CG1 . ILE C 1 150 ? 25.732  9.557   26.351  1.00 23.45 ? 149  ILE C CG1 1 
ATOM   3073 C  CG2 . ILE C 1 150 ? 24.352  7.462   26.523  1.00 18.22 ? 149  ILE C CG2 1 
ATOM   3074 C  CD1 . ILE C 1 150 ? 24.991  10.307  27.482  1.00 17.97 ? 149  ILE C CD1 1 
ATOM   3075 N  N   . GLY C 1 151 ? 24.967  5.870   23.388  1.00 20.03 ? 150  GLY C N   1 
ATOM   3076 C  CA  . GLY C 1 151 ? 24.204  4.966   22.562  1.00 19.65 ? 150  GLY C CA  1 
ATOM   3077 C  C   . GLY C 1 151 ? 23.698  3.803   23.404  1.00 20.40 ? 150  GLY C C   1 
ATOM   3078 O  O   . GLY C 1 151 ? 24.226  3.568   24.464  1.00 22.28 ? 150  GLY C O   1 
ATOM   3079 N  N   . ILE C 1 152 ? 22.604  3.236   22.934  1.00 22.76 ? 151  ILE C N   1 
ATOM   3080 C  CA  . ILE C 1 152 ? 21.868  2.101   23.495  1.00 21.43 ? 151  ILE C CA  1 
ATOM   3081 C  C   . ILE C 1 152 ? 22.810  0.923   23.436  1.00 21.40 ? 151  ILE C C   1 
ATOM   3082 O  O   . ILE C 1 152 ? 23.503  0.720   22.445  1.00 22.58 ? 151  ILE C O   1 
ATOM   3083 C  CB  . ILE C 1 152 ? 20.630  1.831   22.678  1.00 21.08 ? 151  ILE C CB  1 
ATOM   3084 C  CG1 . ILE C 1 152 ? 19.593  2.916   22.938  1.00 21.64 ? 151  ILE C CG1 1 
ATOM   3085 C  CG2 . ILE C 1 152 ? 20.015  0.476   23.105  1.00 19.98 ? 151  ILE C CG2 1 
ATOM   3086 C  CD1 . ILE C 1 152 ? 18.531  2.964   21.874  1.00 26.70 ? 151  ILE C CD1 1 
ATOM   3087 N  N   . ALA C 1 153 ? 22.925  0.250   24.560  1.00 22.18 ? 152  ALA C N   1 
ATOM   3088 C  CA  . ALA C 1 153 ? 23.863  -0.840  24.696  1.00 21.62 ? 152  ALA C CA  1 
ATOM   3089 C  C   . ALA C 1 153 ? 23.145  -2.181  24.927  1.00 22.00 ? 152  ALA C C   1 
ATOM   3090 O  O   . ALA C 1 153 ? 21.995  -2.231  25.363  1.00 23.89 ? 152  ALA C O   1 
ATOM   3091 C  CB  . ALA C 1 153 ? 24.825  -0.538  25.801  1.00 20.51 ? 152  ALA C CB  1 
ATOM   3092 N  N   . GLN C 1 154 ? 23.821  -3.270  24.630  1.00 23.58 ? 153  GLN C N   1 
ATOM   3093 C  CA  . GLN C 1 154 ? 23.205  -4.568  24.817  1.00 24.39 ? 153  GLN C CA  1 
ATOM   3094 C  C   . GLN C 1 154 ? 23.048  -4.870  26.326  1.00 25.76 ? 153  GLN C C   1 
ATOM   3095 O  O   . GLN C 1 154 ? 23.976  -4.614  27.125  1.00 27.20 ? 153  GLN C O   1 
ATOM   3096 C  CB  . GLN C 1 154 ? 23.975  -5.660  24.038  1.00 23.69 ? 153  GLN C CB  1 
ATOM   3097 C  CG  . GLN C 1 154 ? 23.348  -7.098  24.077  1.00 25.45 ? 153  GLN C CG  1 
ATOM   3098 C  CD  . GLN C 1 154 ? 23.939  -8.055  22.998  1.00 26.26 ? 153  GLN C CD  1 
ATOM   3099 O  OE1 . GLN C 1 154 ? 25.148  -8.350  23.010  1.00 29.16 ? 153  GLN C OE1 1 
ATOM   3100 N  NE2 . GLN C 1 154 ? 23.088  -8.534  22.080  1.00 26.23 ? 153  GLN C NE2 1 
ATOM   3101 O  OXT . GLN C 1 154 ? 21.967  -5.335  26.745  1.00 25.46 ? 153  GLN C OXT 1 
ATOM   3102 N  N   . ALA D 1 2   ? 11.956  13.654  19.065  1.00 31.97 ? 1    ALA D N   1 
ATOM   3103 C  CA  . ALA D 1 2   ? 12.915  14.402  18.190  1.00 30.51 ? 1    ALA D CA  1 
ATOM   3104 C  C   . ALA D 1 2   ? 12.462  14.518  16.733  1.00 29.70 ? 1    ALA D C   1 
ATOM   3105 O  O   . ALA D 1 2   ? 11.883  13.595  16.175  1.00 31.09 ? 1    ALA D O   1 
ATOM   3106 C  CB  . ALA D 1 2   ? 14.298  13.752  18.261  1.00 31.18 ? 1    ALA D CB  1 
ATOM   3107 N  N   . THR D 1 3   ? 12.720  15.652  16.103  1.00 28.08 ? 2    THR D N   1 
ATOM   3108 C  CA  . THR D 1 3   ? 12.427  15.758  14.678  1.00 26.23 ? 2    THR D CA  1 
ATOM   3109 C  C   . THR D 1 3   ? 13.711  15.735  13.844  1.00 24.30 ? 2    THR D C   1 
ATOM   3110 O  O   . THR D 1 3   ? 13.663  15.621  12.613  1.00 24.73 ? 2    THR D O   1 
ATOM   3111 C  CB  . THR D 1 3   ? 11.600  16.992  14.373  1.00 25.87 ? 2    THR D CB  1 
ATOM   3112 O  OG1 . THR D 1 3   ? 12.410  18.165  14.562  1.00 30.45 ? 2    THR D OG1 1 
ATOM   3113 C  CG2 . THR D 1 3   ? 10.465  17.141  15.382  1.00 26.44 ? 2    THR D CG2 1 
ATOM   3114 N  N   . LYS D 1 4   ? 14.850  15.867  14.513  1.00 22.63 ? 3    LYS D N   1 
ATOM   3115 C  CA  . LYS D 1 4   ? 16.159  15.825  13.852  1.00 22.10 ? 3    LYS D CA  1 
ATOM   3116 C  C   . LYS D 1 4   ? 17.271  15.042  14.577  1.00 20.54 ? 3    LYS D C   1 
ATOM   3117 O  O   . LYS D 1 4   ? 17.465  15.131  15.792  1.00 22.36 ? 3    LYS D O   1 
ATOM   3118 C  CB  . LYS D 1 4   ? 16.670  17.249  13.582  1.00 21.26 ? 3    LYS D CB  1 
ATOM   3119 C  CG  . LYS D 1 4   ? 16.221  17.853  12.264  1.00 23.73 ? 3    LYS D CG  1 
ATOM   3120 C  CD  . LYS D 1 4   ? 16.255  19.384  12.348  1.00 26.55 ? 3    LYS D CD  1 
ATOM   3121 C  CE  . LYS D 1 4   ? 15.112  19.998  11.579  1.00 30.45 ? 3    LYS D CE  1 
ATOM   3122 N  NZ  . LYS D 1 4   ? 15.393  21.445  11.388  1.00 33.29 ? 3    LYS D NZ  1 
ATOM   3123 N  N   . ALA D 1 5   ? 18.067  14.342  13.791  1.00 21.72 ? 4    ALA D N   1 
ATOM   3124 C  CA  . ALA D 1 5   ? 19.195  13.623  14.282  1.00 19.94 ? 4    ALA D CA  1 
ATOM   3125 C  C   . ALA D 1 5   ? 20.311  13.810  13.258  1.00 19.88 ? 4    ALA D C   1 
ATOM   3126 O  O   . ALA D 1 5   ? 20.066  14.227  12.116  1.00 23.09 ? 4    ALA D O   1 
ATOM   3127 C  CB  . ALA D 1 5   ? 18.810  12.075  14.472  1.00 17.64 ? 4    ALA D CB  1 
ATOM   3128 N  N   . VAL D 1 6   ? 21.517  13.459  13.678  1.00 21.00 ? 5    VAL D N   1 
ATOM   3129 C  CA  . VAL D 1 6   ? 22.736  13.517  12.921  1.00 20.81 ? 5    VAL D CA  1 
ATOM   3130 C  C   . VAL D 1 6   ? 23.687  12.417  13.365  1.00 21.20 ? 5    VAL D C   1 
ATOM   3131 O  O   . VAL D 1 6   ? 23.674  11.976  14.531  1.00 24.91 ? 5    VAL D O   1 
ATOM   3132 C  CB  . VAL D 1 6   ? 23.450  14.909  13.134  1.00 17.64 ? 5    VAL D CB  1 
ATOM   3133 C  CG1 . VAL D 1 6   ? 24.229  14.980  14.515  1.00 16.91 ? 5    VAL D CG1 1 
ATOM   3134 C  CG2 . VAL D 1 6   ? 24.416  15.195  12.028  1.00 22.17 ? 5    VAL D CG2 1 
ATOM   3135 N  N   . CYS D 1 7   ? 24.548  11.991  12.459  1.00 22.74 ? 6    CYS D N   1 
ATOM   3136 C  CA  . CYS D 1 7   ? 25.498  10.926  12.717  1.00 22.78 ? 6    CYS D CA  1 
ATOM   3137 C  C   . CYS D 1 7   ? 26.810  11.211  11.999  1.00 21.95 ? 6    CYS D C   1 
ATOM   3138 O  O   . CYS D 1 7   ? 26.807  11.448  10.794  1.00 24.55 ? 6    CYS D O   1 
ATOM   3139 C  CB  . CYS D 1 7   ? 24.938  9.602   12.201  1.00 22.94 ? 6    CYS D CB  1 
ATOM   3140 S  SG  . CYS D 1 7   ? 26.141  8.294   12.411  1.00 29.60 ? 6    CYS D SG  1 
ATOM   3141 N  N   . VAL D 1 8   ? 27.902  11.228  12.751  1.00 22.40 ? 7    VAL D N   1 
ATOM   3142 C  CA  . VAL D 1 8   ? 29.250  11.293  12.184  1.00 20.90 ? 7    VAL D CA  1 
ATOM   3143 C  C   . VAL D 1 8   ? 29.803  9.879   11.958  1.00 21.11 ? 7    VAL D C   1 
ATOM   3144 O  O   . VAL D 1 8   ? 29.907  9.110   12.890  1.00 22.94 ? 7    VAL D O   1 
ATOM   3145 C  CB  . VAL D 1 8   ? 30.213  12.143  13.017  1.00 21.14 ? 7    VAL D CB  1 
ATOM   3146 C  CG1 . VAL D 1 8   ? 31.588  12.349  12.298  1.00 17.85 ? 7    VAL D CG1 1 
ATOM   3147 C  CG2 . VAL D 1 8   ? 29.580  13.531  13.298  1.00 20.96 ? 7    VAL D CG2 1 
ATOM   3148 N  N   . LEU D 1 9   ? 30.197  9.597   10.713  1.00 22.62 ? 8    LEU D N   1 
ATOM   3149 C  CA  . LEU D 1 9   ? 30.756  8.259   10.354  1.00 22.05 ? 8    LEU D CA  1 
ATOM   3150 C  C   . LEU D 1 9   ? 32.290  8.242   10.297  1.00 21.89 ? 8    LEU D C   1 
ATOM   3151 O  O   . LEU D 1 9   ? 32.938  9.016   9.543   1.00 22.63 ? 8    LEU D O   1 
ATOM   3152 C  CB  . LEU D 1 9   ? 30.206  7.753   9.003   1.00 20.73 ? 8    LEU D CB  1 
ATOM   3153 C  CG  . LEU D 1 9   ? 28.722  7.671   8.576   1.00 23.40 ? 8    LEU D CG  1 
ATOM   3154 C  CD1 . LEU D 1 9   ? 27.848  8.793   9.103   1.00 29.23 ? 8    LEU D CD1 1 
ATOM   3155 C  CD2 . LEU D 1 9   ? 28.598  7.548   7.042   1.00 24.44 ? 8    LEU D CD2 1 
ATOM   3156 N  N   . LYS D 1 10  ? 32.877  7.331   11.066  1.00 21.97 ? 9    LYS D N   1 
ATOM   3157 C  CA  . LYS D 1 10  ? 34.314  7.115   11.012  1.00 22.99 ? 9    LYS D CA  1 
ATOM   3158 C  C   . LYS D 1 10  ? 34.669  5.642   11.185  1.00 23.27 ? 9    LYS D C   1 
ATOM   3159 O  O   . LYS D 1 10  ? 33.920  4.887   11.824  1.00 24.33 ? 9    LYS D O   1 
ATOM   3160 C  CB  . LYS D 1 10  ? 35.049  7.967   12.052  1.00 20.90 ? 9    LYS D CB  1 
ATOM   3161 C  CG  . LYS D 1 10  ? 35.157  9.456   11.701  1.00 22.70 ? 9    LYS D CG  1 
ATOM   3162 C  CD  . LYS D 1 10  ? 35.706  10.245  12.916  1.00 28.39 ? 9    LYS D CD  1 
ATOM   3163 C  CE  . LYS D 1 10  ? 36.330  11.604  12.562  1.00 31.14 ? 9    LYS D CE  1 
ATOM   3164 N  NZ  . LYS D 1 10  ? 35.443  12.727  12.980  1.00 36.62 ? 9    LYS D NZ  1 
ATOM   3165 N  N   . GLY D 1 11  ? 35.793  5.259   10.588  1.00 25.66 ? 10   GLY D N   1 
ATOM   3166 C  CA  . GLY D 1 11  ? 36.306  3.904   10.676  1.00 27.38 ? 10   GLY D CA  1 
ATOM   3167 C  C   . GLY D 1 11  ? 37.807  3.777   10.883  1.00 28.95 ? 10   GLY D C   1 
ATOM   3168 O  O   . GLY D 1 11  ? 38.538  4.744   11.178  1.00 29.99 ? 10   GLY D O   1 
ATOM   3169 N  N   . ASP D 1 12  ? 38.276  2.537   10.751  1.00 30.28 ? 11   ASP D N   1 
ATOM   3170 C  CA  . ASP D 1 12  ? 39.690  2.222   10.854  1.00 31.34 ? 11   ASP D CA  1 
ATOM   3171 C  C   . ASP D 1 12  ? 40.450  2.869   9.700   1.00 30.84 ? 11   ASP D C   1 
ATOM   3172 O  O   . ASP D 1 12  ? 41.633  3.212   9.839   1.00 31.91 ? 11   ASP D O   1 
ATOM   3173 C  CB  . ASP D 1 12  ? 39.889  0.704   10.793  1.00 32.08 ? 11   ASP D CB  1 
ATOM   3174 C  CG  . ASP D 1 12  ? 39.351  -0.013  12.030  1.00 35.70 ? 11   ASP D CG  1 
ATOM   3175 O  OD1 . ASP D 1 12  ? 38.590  -1.010  11.866  1.00 39.61 ? 11   ASP D OD1 1 
ATOM   3176 O  OD2 . ASP D 1 12  ? 39.640  0.340   13.203  1.00 38.17 ? 11   ASP D OD2 1 
ATOM   3177 N  N   . GLY D 1 13  ? 39.757  3.032   8.569   1.00 30.38 ? 12   GLY D N   1 
ATOM   3178 C  CA  . GLY D 1 13  ? 40.334  3.560   7.349   1.00 29.52 ? 12   GLY D CA  1 
ATOM   3179 C  C   . GLY D 1 13  ? 39.962  4.977   6.966   1.00 29.03 ? 12   GLY D C   1 
ATOM   3180 O  O   . GLY D 1 13  ? 39.718  5.820   7.822   1.00 29.75 ? 12   GLY D O   1 
ATOM   3181 N  N   . PRO D 1 14  ? 39.876  5.230   5.667   1.00 28.78 ? 13   PRO D N   1 
ATOM   3182 C  CA  . PRO D 1 14  ? 39.663  6.586   5.150   1.00 28.73 ? 13   PRO D CA  1 
ATOM   3183 C  C   . PRO D 1 14  ? 38.196  7.000   5.024   1.00 28.44 ? 13   PRO D C   1 
ATOM   3184 O  O   . PRO D 1 14  ? 37.957  8.189   4.794   1.00 29.18 ? 13   PRO D O   1 
ATOM   3185 C  CB  . PRO D 1 14  ? 40.273  6.518   3.746   1.00 28.38 ? 13   PRO D CB  1 
ATOM   3186 C  CG  . PRO D 1 14  ? 40.688  5.057   3.557   1.00 28.79 ? 13   PRO D CG  1 
ATOM   3187 C  CD  . PRO D 1 14  ? 39.971  4.251   4.581   1.00 28.12 ? 13   PRO D CD  1 
ATOM   3188 N  N   . VAL D 1 15  ? 37.254  6.067   5.137   1.00 27.46 ? 14   VAL D N   1 
ATOM   3189 C  CA  . VAL D 1 15  ? 35.833  6.400   4.998   1.00 26.73 ? 14   VAL D CA  1 
ATOM   3190 C  C   . VAL D 1 15  ? 35.340  7.326   6.110   1.00 26.65 ? 14   VAL D C   1 
ATOM   3191 O  O   . VAL D 1 15  ? 35.516  7.039   7.308   1.00 27.76 ? 14   VAL D O   1 
ATOM   3192 C  CB  . VAL D 1 15  ? 34.933  5.146   4.971   1.00 26.01 ? 14   VAL D CB  1 
ATOM   3193 C  CG1 . VAL D 1 15  ? 33.440  5.548   4.808   1.00 23.57 ? 14   VAL D CG1 1 
ATOM   3194 C  CG2 . VAL D 1 15  ? 35.378  4.204   3.870   1.00 25.81 ? 14   VAL D CG2 1 
ATOM   3195 N  N   . GLN D 1 16  ? 34.759  8.457   5.721   1.00 27.14 ? 15   GLN D N   1 
ATOM   3196 C  CA  . GLN D 1 16  ? 34.190  9.391   6.690   1.00 26.27 ? 15   GLN D CA  1 
ATOM   3197 C  C   . GLN D 1 16  ? 33.092  10.230  6.075   1.00 24.68 ? 15   GLN D C   1 
ATOM   3198 O  O   . GLN D 1 16  ? 33.070  10.399  4.868   1.00 27.15 ? 15   GLN D O   1 
ATOM   3199 C  CB  . GLN D 1 16  ? 35.258  10.275  7.347   1.00 25.81 ? 15   GLN D CB  1 
ATOM   3200 C  CG  . GLN D 1 16  ? 35.921  11.286  6.425   1.00 28.00 ? 15   GLN D CG  1 
ATOM   3201 C  CD  . GLN D 1 16  ? 37.124  11.971  7.076   1.00 30.41 ? 15   GLN D CD  1 
ATOM   3202 O  OE1 . GLN D 1 16  ? 37.076  12.359  8.255   1.00 34.89 ? 15   GLN D OE1 1 
ATOM   3203 N  NE2 . GLN D 1 16  ? 38.204  12.104  6.318   1.00 33.31 ? 15   GLN D NE2 1 
ATOM   3204 N  N   . GLY D 1 17  ? 32.184  10.735  6.906   1.00 24.63 ? 16   GLY D N   1 
ATOM   3205 C  CA  . GLY D 1 17  ? 31.065  11.536  6.443   1.00 23.78 ? 16   GLY D CA  1 
ATOM   3206 C  C   . GLY D 1 17  ? 30.084  12.002  7.511   1.00 22.17 ? 16   GLY D C   1 
ATOM   3207 O  O   . GLY D 1 17  ? 30.306  11.843  8.712   1.00 24.71 ? 16   GLY D O   1 
ATOM   3208 N  N   . ILE D 1 18  ? 29.011  12.645  7.081   1.00 21.57 ? 17   ILE D N   1 
ATOM   3209 C  CA  . ILE D 1 18  ? 28.024  13.207  7.992   1.00 19.48 ? 17   ILE D CA  1 
ATOM   3210 C  C   . ILE D 1 18  ? 26.668  12.995  7.396   1.00 19.35 ? 17   ILE D C   1 
ATOM   3211 O  O   . ILE D 1 18  ? 26.406  13.425  6.259   1.00 21.43 ? 17   ILE D O   1 
ATOM   3212 C  CB  . ILE D 1 18  ? 28.235  14.755  8.183   1.00 18.34 ? 17   ILE D CB  1 
ATOM   3213 C  CG1 . ILE D 1 18  ? 29.581  15.028  8.827   1.00 17.10 ? 17   ILE D CG1 1 
ATOM   3214 C  CG2 . ILE D 1 18  ? 27.120  15.309  9.089   1.00 18.86 ? 17   ILE D CG2 1 
ATOM   3215 C  CD1 . ILE D 1 18  ? 29.876  16.526  8.960   1.00 15.43 ? 17   ILE D CD1 1 
ATOM   3216 N  N   . ILE D 1 19  ? 25.794  12.339  8.146   1.00 21.11 ? 18   ILE D N   1 
ATOM   3217 C  CA  . ILE D 1 19  ? 24.447  12.075  7.689   1.00 19.62 ? 18   ILE D CA  1 
ATOM   3218 C  C   . ILE D 1 19  ? 23.388  12.747  8.560   1.00 20.82 ? 18   ILE D C   1 
ATOM   3219 O  O   . ILE D 1 19  ? 23.442  12.644  9.799   1.00 23.75 ? 18   ILE D O   1 
ATOM   3220 C  CB  . ILE D 1 19  ? 24.260  10.513  7.632   1.00 17.93 ? 18   ILE D CB  1 
ATOM   3221 C  CG1 . ILE D 1 19  ? 25.176  9.896   6.585   1.00 15.98 ? 18   ILE D CG1 1 
ATOM   3222 C  CG2 . ILE D 1 19  ? 22.803  10.132  7.425   1.00 20.61 ? 18   ILE D CG2 1 
ATOM   3223 C  CD1 . ILE D 1 19  ? 24.974  10.394  5.138   1.00 14.21 ? 18   ILE D CD1 1 
ATOM   3224 N  N   . ASN D 1 20  ? 22.456  13.455  7.932   1.00 22.31 ? 19   ASN D N   1 
ATOM   3225 C  CA  . ASN D 1 20  ? 21.364  14.084  8.635   1.00 22.54 ? 19   ASN D CA  1 
ATOM   3226 C  C   . ASN D 1 20  ? 20.046  13.328  8.523   1.00 23.40 ? 19   ASN D C   1 
ATOM   3227 O  O   . ASN D 1 20  ? 19.751  12.683  7.513   1.00 25.63 ? 19   ASN D O   1 
ATOM   3228 C  CB  . ASN D 1 20  ? 21.163  15.535  8.185   1.00 21.40 ? 19   ASN D CB  1 
ATOM   3229 C  CG  . ASN D 1 20  ? 22.483  16.303  8.063   1.00 21.34 ? 19   ASN D CG  1 
ATOM   3230 O  OD1 . ASN D 1 20  ? 23.035  16.450  6.963   1.00 25.56 ? 19   ASN D OD1 1 
ATOM   3231 N  ND2 . ASN D 1 20  ? 23.014  16.760  9.202   1.00 19.11 ? 19   ASN D ND2 1 
ATOM   3232 N  N   . PHE D 1 21  ? 19.261  13.414  9.577   1.00 24.80 ? 20   PHE D N   1 
ATOM   3233 C  CA  . PHE D 1 21  ? 17.926  12.842  9.589   1.00 25.18 ? 20   PHE D CA  1 
ATOM   3234 C  C   . PHE D 1 21  ? 16.918  13.901  10.022  1.00 25.14 ? 20   PHE D C   1 
ATOM   3235 O  O   . PHE D 1 21  ? 17.141  14.618  10.994  1.00 27.04 ? 20   PHE D O   1 
ATOM   3236 C  CB  . PHE D 1 21  ? 17.802  11.663  10.560  1.00 24.20 ? 20   PHE D CB  1 
ATOM   3237 C  CG  . PHE D 1 21  ? 18.752  10.500  10.321  1.00 22.71 ? 20   PHE D CG  1 
ATOM   3238 C  CD1 . PHE D 1 21  ? 20.004  10.483  10.898  1.00 20.51 ? 20   PHE D CD1 1 
ATOM   3239 C  CD2 . PHE D 1 21  ? 18.359  9.382   9.591   1.00 25.13 ? 20   PHE D CD2 1 
ATOM   3240 C  CE1 . PHE D 1 21  ? 20.879  9.399   10.732  1.00 23.87 ? 20   PHE D CE1 1 
ATOM   3241 C  CE2 . PHE D 1 21  ? 19.231  8.317   9.399   1.00 21.71 ? 20   PHE D CE2 1 
ATOM   3242 C  CZ  . PHE D 1 21  ? 20.499  8.316   10.001  1.00 22.01 ? 20   PHE D CZ  1 
ATOM   3243 N  N   . GLU D 1 22  ? 15.786  13.976  9.334   1.00 24.97 ? 21   GLU D N   1 
ATOM   3244 C  CA  . GLU D 1 22  ? 14.715  14.889  9.716   1.00 25.09 ? 21   GLU D CA  1 
ATOM   3245 C  C   . GLU D 1 22  ? 13.372  14.221  9.521   1.00 24.13 ? 21   GLU D C   1 
ATOM   3246 O  O   . GLU D 1 22  ? 13.098  13.636  8.468   1.00 26.11 ? 21   GLU D O   1 
ATOM   3247 C  CB  . GLU D 1 22  ? 14.791  16.195  8.916   1.00 23.86 ? 21   GLU D CB  1 
ATOM   3248 C  CG  . GLU D 1 22  ? 13.774  17.247  9.311   1.00 27.35 ? 21   GLU D CG  1 
ATOM   3249 C  CD  . GLU D 1 22  ? 13.983  18.566  8.571   1.00 29.67 ? 21   GLU D CD  1 
ATOM   3250 O  OE1 . GLU D 1 22  ? 15.136  19.080  8.555   1.00 34.02 ? 21   GLU D OE1 1 
ATOM   3251 O  OE2 . GLU D 1 22  ? 13.005  19.103  7.998   1.00 31.32 ? 21   GLU D OE2 1 
ATOM   3252 N  N   . GLN D 1 23  ? 12.566  14.254  10.566  1.00 24.71 ? 22   GLN D N   1 
ATOM   3253 C  CA  . GLN D 1 23  ? 11.207  13.727  10.529  1.00 25.06 ? 22   GLN D CA  1 
ATOM   3254 C  C   . GLN D 1 23  ? 10.238  14.811  10.970  1.00 25.68 ? 22   GLN D C   1 
ATOM   3255 O  O   . GLN D 1 23  ? 10.207  15.219  12.135  1.00 26.01 ? 22   GLN D O   1 
ATOM   3256 C  CB  . GLN D 1 23  ? 11.082  12.500  11.424  1.00 24.02 ? 22   GLN D CB  1 
ATOM   3257 C  CG  . GLN D 1 23  ? 9.870   11.623  11.151  1.00 22.82 ? 22   GLN D CG  1 
ATOM   3258 C  CD  . GLN D 1 23  ? 9.826   10.432  12.126  1.00 23.65 ? 22   GLN D CD  1 
ATOM   3259 O  OE1 . GLN D 1 23  ? 10.474  10.478  13.163  1.00 25.77 ? 22   GLN D OE1 1 
ATOM   3260 N  NE2 . GLN D 1 23  ? 9.049   9.385   11.799  1.00 24.13 ? 22   GLN D NE2 1 
ATOM   3261 N  N   . LYS D 1 24  ? 9.424   15.249  10.025  1.00 27.19 ? 23   LYS D N   1 
ATOM   3262 C  CA  . LYS D 1 24  ? 8.466   16.334  10.243  1.00 28.16 ? 23   LYS D CA  1 
ATOM   3263 C  C   . LYS D 1 24  ? 7.334   15.954  11.188  1.00 29.03 ? 23   LYS D C   1 
ATOM   3264 O  O   . LYS D 1 24  ? 6.956   16.737  12.053  1.00 29.06 ? 23   LYS D O   1 
ATOM   3265 C  CB  . LYS D 1 24  ? 7.910   16.803  8.906   1.00 28.24 ? 23   LYS D CB  1 
ATOM   3266 C  CG  . LYS D 1 24  ? 8.975   16.929  7.812   1.00 29.29 ? 23   LYS D CG  1 
ATOM   3267 C  CD  . LYS D 1 24  ? 8.574   17.916  6.719   1.00 31.68 ? 23   LYS D CD  1 
ATOM   3268 C  CE  . LYS D 1 24  ? 9.449   19.173  6.736   1.00 32.27 ? 23   LYS D CE  1 
ATOM   3269 N  NZ  . LYS D 1 24  ? 9.431   19.869  5.400   1.00 31.97 ? 23   LYS D NZ  1 
ATOM   3270 N  N   . GLU D 1 25  ? 6.800   14.745  11.036  1.00 30.07 ? 24   GLU D N   1 
ATOM   3271 C  CA  . GLU D 1 25  ? 5.720   14.295  11.913  1.00 31.08 ? 24   GLU D CA  1 
ATOM   3272 C  C   . GLU D 1 25  ? 5.934   12.859  12.380  1.00 31.17 ? 24   GLU D C   1 
ATOM   3273 O  O   . GLU D 1 25  ? 6.572   12.050  11.699  1.00 31.56 ? 24   GLU D O   1 
ATOM   3274 C  CB  . GLU D 1 25  ? 4.322   14.522  11.294  1.00 31.40 ? 24   GLU D CB  1 
ATOM   3275 C  CG  . GLU D 1 25  ? 4.293   14.599  9.768   1.00 33.55 ? 24   GLU D CG  1 
ATOM   3276 C  CD  . GLU D 1 25  ? 2.904   14.890  9.199   1.00 35.47 ? 24   GLU D CD  1 
ATOM   3277 O  OE1 . GLU D 1 25  ? 1.967   15.139  9.995   1.00 36.63 ? 24   GLU D OE1 1 
ATOM   3278 O  OE2 . GLU D 1 25  ? 2.742   14.875  7.947   1.00 36.82 ? 24   GLU D OE2 1 
ATOM   3279 N  N   . SER D 1 26  ? 5.423   12.572  13.569  1.00 31.64 ? 25   SER D N   1 
ATOM   3280 C  CA  . SER D 1 26  ? 5.602   11.280  14.223  1.00 32.02 ? 25   SER D CA  1 
ATOM   3281 C  C   . SER D 1 26  ? 5.247   10.091  13.322  1.00 32.10 ? 25   SER D C   1 
ATOM   3282 O  O   . SER D 1 26  ? 5.970   9.094   13.277  1.00 32.36 ? 25   SER D O   1 
ATOM   3283 C  CB  . SER D 1 26  ? 4.814   11.274  15.548  1.00 32.48 ? 25   SER D CB  1 
ATOM   3284 O  OG  . SER D 1 26  ? 4.046   10.090  15.740  1.00 33.66 ? 25   SER D OG  1 
ATOM   3285 N  N   . ASN D 1 27  ? 4.149   10.206  12.583  1.00 32.18 ? 26   ASN D N   1 
ATOM   3286 C  CA  . ASN D 1 27  ? 3.744   9.132   11.677  1.00 32.30 ? 26   ASN D CA  1 
ATOM   3287 C  C   . ASN D 1 27  ? 4.364   9.264   10.282  1.00 32.04 ? 26   ASN D C   1 
ATOM   3288 O  O   . ASN D 1 27  ? 4.025   8.507   9.360   1.00 32.63 ? 26   ASN D O   1 
ATOM   3289 C  CB  . ASN D 1 27  ? 2.222   9.110   11.553  1.00 32.35 ? 26   ASN D CB  1 
ATOM   3290 C  CG  . ASN D 1 27  ? 1.539   8.829   12.875  1.00 33.19 ? 26   ASN D CG  1 
ATOM   3291 O  OD1 . ASN D 1 27  ? 0.649   9.567   13.307  1.00 33.69 ? 26   ASN D OD1 1 
ATOM   3292 N  ND2 . ASN D 1 27  ? 1.963   7.755   13.533  1.00 34.96 ? 26   ASN D ND2 1 
ATOM   3293 N  N   . GLY D 1 28  ? 5.276   10.215  10.128  1.00 31.28 ? 27   GLY D N   1 
ATOM   3294 C  CA  . GLY D 1 28  ? 5.833   10.500  8.821   1.00 29.81 ? 27   GLY D CA  1 
ATOM   3295 C  C   . GLY D 1 28  ? 7.130   9.821   8.456   1.00 28.45 ? 27   GLY D C   1 
ATOM   3296 O  O   . GLY D 1 28  ? 7.767   9.137   9.260   1.00 28.89 ? 27   GLY D O   1 
ATOM   3297 N  N   . PRO D 1 29  ? 7.491   10.020  7.192   1.00 27.88 ? 28   PRO D N   1 
ATOM   3298 C  CA  . PRO D 1 29  ? 8.753   9.557   6.620   1.00 26.93 ? 28   PRO D CA  1 
ATOM   3299 C  C   . PRO D 1 29  ? 9.940   10.394  7.122   1.00 25.86 ? 28   PRO D C   1 
ATOM   3300 O  O   . PRO D 1 29  ? 9.777   11.568  7.497   1.00 26.85 ? 28   PRO D O   1 
ATOM   3301 C  CB  . PRO D 1 29  ? 8.570   9.789   5.119   1.00 26.36 ? 28   PRO D CB  1 
ATOM   3302 C  CG  . PRO D 1 29  ? 7.137   10.188  4.936   1.00 27.71 ? 28   PRO D CG  1 
ATOM   3303 C  CD  . PRO D 1 29  ? 6.663   10.748  6.219   1.00 27.43 ? 28   PRO D CD  1 
ATOM   3304 N  N   . VAL D 1 30  ? 11.119  9.777   7.122   1.00 25.25 ? 29   VAL D N   1 
ATOM   3305 C  CA  . VAL D 1 30  ? 12.350  10.418  7.558   1.00 23.46 ? 29   VAL D CA  1 
ATOM   3306 C  C   . VAL D 1 30  ? 13.223  10.712  6.371   1.00 23.34 ? 29   VAL D C   1 
ATOM   3307 O  O   . VAL D 1 30  ? 13.542  9.844   5.560   1.00 25.00 ? 29   VAL D O   1 
ATOM   3308 C  CB  . VAL D 1 30  ? 13.161  9.534   8.544   1.00 21.92 ? 29   VAL D CB  1 
ATOM   3309 C  CG1 . VAL D 1 30  ? 14.434  10.274  9.062   1.00 20.33 ? 29   VAL D CG1 1 
ATOM   3310 C  CG2 . VAL D 1 30  ? 12.257  9.043   9.682   1.00 24.59 ? 29   VAL D CG2 1 
ATOM   3311 N  N   . LYS D 1 31  ? 13.614  11.962  6.242   1.00 23.55 ? 30   LYS D N   1 
ATOM   3312 C  CA  . LYS D 1 31  ? 14.547  12.307  5.194   1.00 23.83 ? 30   LYS D CA  1 
ATOM   3313 C  C   . LYS D 1 31  ? 15.966  12.107  5.711   1.00 23.29 ? 30   LYS D C   1 
ATOM   3314 O  O   . LYS D 1 31  ? 16.311  12.557  6.809   1.00 26.26 ? 30   LYS D O   1 
ATOM   3315 C  CB  . LYS D 1 31  ? 14.297  13.740  4.781   1.00 22.38 ? 30   LYS D CB  1 
ATOM   3316 C  CG  . LYS D 1 31  ? 13.003  13.883  3.997   1.00 26.19 ? 30   LYS D CG  1 
ATOM   3317 C  CD  . LYS D 1 31  ? 12.080  14.978  4.553   1.00 29.46 ? 30   LYS D CD  1 
ATOM   3318 C  CE  . LYS D 1 31  ? 11.905  14.869  6.094   1.00 29.85 ? 30   LYS D CE  1 
ATOM   3319 N  NZ  . LYS D 1 31  ? 10.802  13.988  6.615   1.00 29.72 ? 30   LYS D NZ  1 
ATOM   3320 N  N   . VAL D 1 32  ? 16.764  11.360  4.964   1.00 24.27 ? 31   VAL D N   1 
ATOM   3321 C  CA  . VAL D 1 32  ? 18.172  11.179  5.275   1.00 22.87 ? 31   VAL D CA  1 
ATOM   3322 C  C   . VAL D 1 32  ? 19.069  11.673  4.124   1.00 24.18 ? 31   VAL D C   1 
ATOM   3323 O  O   . VAL D 1 32  ? 18.844  11.395  2.940   1.00 24.42 ? 31   VAL D O   1 
ATOM   3324 C  CB  . VAL D 1 32  ? 18.527  9.767   5.894   1.00 23.27 ? 31   VAL D CB  1 
ATOM   3325 C  CG1 . VAL D 1 32  ? 17.360  8.797   5.832   1.00 23.29 ? 31   VAL D CG1 1 
ATOM   3326 C  CG2 . VAL D 1 32  ? 19.907  9.200   5.470   1.00 21.12 ? 31   VAL D CG2 1 
ATOM   3327 N  N   . TRP D 1 33  ? 20.071  12.459  4.497   1.00 24.09 ? 32   TRP D N   1 
ATOM   3328 C  CA  . TRP D 1 33  ? 20.947  13.081  3.538   1.00 23.27 ? 32   TRP D CA  1 
ATOM   3329 C  C   . TRP D 1 33  ? 22.241  13.562  4.145   1.00 22.19 ? 32   TRP D C   1 
ATOM   3330 O  O   . TRP D 1 33  ? 22.327  13.836  5.344   1.00 22.79 ? 32   TRP D O   1 
ATOM   3331 C  CB  . TRP D 1 33  ? 20.263  14.272  2.882   1.00 22.42 ? 32   TRP D CB  1 
ATOM   3332 C  CG  . TRP D 1 33  ? 20.272  15.496  3.690   1.00 23.85 ? 32   TRP D CG  1 
ATOM   3333 C  CD1 . TRP D 1 33  ? 21.091  16.568  3.529   1.00 23.93 ? 32   TRP D CD1 1 
ATOM   3334 C  CD2 . TRP D 1 33  ? 19.420  15.809  4.793   1.00 24.88 ? 32   TRP D CD2 1 
ATOM   3335 N  NE1 . TRP D 1 33  ? 20.803  17.529  4.462   1.00 26.27 ? 32   TRP D NE1 1 
ATOM   3336 C  CE2 . TRP D 1 33  ? 19.764  17.100  5.234   1.00 24.39 ? 32   TRP D CE2 1 
ATOM   3337 C  CE3 . TRP D 1 33  ? 18.374  15.144  5.434   1.00 25.80 ? 32   TRP D CE3 1 
ATOM   3338 C  CZ2 . TRP D 1 33  ? 19.128  17.724  6.303   1.00 26.67 ? 32   TRP D CZ2 1 
ATOM   3339 C  CZ3 . TRP D 1 33  ? 17.747  15.760  6.503   1.00 26.21 ? 32   TRP D CZ3 1 
ATOM   3340 C  CH2 . TRP D 1 33  ? 18.119  17.044  6.917   1.00 28.40 ? 32   TRP D CH2 1 
ATOM   3341 N  N   . GLY D 1 34  ? 23.244  13.648  3.278   1.00 22.64 ? 33   GLY D N   1 
ATOM   3342 C  CA  . GLY D 1 34  ? 24.566  14.133  3.621   1.00 22.95 ? 33   GLY D CA  1 
ATOM   3343 C  C   . GLY D 1 34  ? 25.598  13.605  2.658   1.00 22.17 ? 33   GLY D C   1 
ATOM   3344 O  O   . GLY D 1 34  ? 25.319  13.389  1.489   1.00 24.95 ? 33   GLY D O   1 
ATOM   3345 N  N   . SER D 1 35  ? 26.795  13.376  3.160   1.00 23.62 ? 34   SER D N   1 
ATOM   3346 C  CA  . SER D 1 35  ? 27.922  13.072  2.317   1.00 24.78 ? 34   SER D CA  1 
ATOM   3347 C  C   . SER D 1 35  ? 28.918  12.115  2.973   1.00 25.12 ? 34   SER D C   1 
ATOM   3348 O  O   . SER D 1 35  ? 29.272  12.264  4.140   1.00 26.44 ? 34   SER D O   1 
ATOM   3349 C  CB  . SER D 1 35  ? 28.605  14.407  1.988   1.00 24.06 ? 34   SER D CB  1 
ATOM   3350 O  OG  . SER D 1 35  ? 29.392  14.309  0.831   1.00 29.01 ? 34   SER D OG  1 
ATOM   3351 N  N   . ILE D 1 36  ? 29.336  11.098  2.231   1.00 25.72 ? 35   ILE D N   1 
ATOM   3352 C  CA  . ILE D 1 36  ? 30.358  10.185  2.709   1.00 25.53 ? 35   ILE D CA  1 
ATOM   3353 C  C   . ILE D 1 36  ? 31.529  10.176  1.734   1.00 25.60 ? 35   ILE D C   1 
ATOM   3354 O  O   . ILE D 1 36  ? 31.335  10.080  0.528   1.00 26.62 ? 35   ILE D O   1 
ATOM   3355 C  CB  . ILE D 1 36  ? 29.840  8.730   2.834   1.00 24.30 ? 35   ILE D CB  1 
ATOM   3356 C  CG1 . ILE D 1 36  ? 28.532  8.636   3.622   1.00 24.80 ? 35   ILE D CG1 1 
ATOM   3357 C  CG2 . ILE D 1 36  ? 30.910  7.900   3.499   1.00 25.24 ? 35   ILE D CG2 1 
ATOM   3358 C  CD1 . ILE D 1 36  ? 27.738  7.335   3.357   1.00 28.76 ? 35   ILE D CD1 1 
ATOM   3359 N  N   . LYS D 1 37  ? 32.748  10.253  2.259   1.00 26.88 ? 36   LYS D N   1 
ATOM   3360 C  CA  . LYS D 1 37  ? 33.919  10.203  1.404   1.00 26.88 ? 36   LYS D CA  1 
ATOM   3361 C  C   . LYS D 1 37  ? 34.889  9.062   1.756   1.00 26.88 ? 36   LYS D C   1 
ATOM   3362 O  O   . LYS D 1 37  ? 34.726  8.376   2.777   1.00 27.23 ? 36   LYS D O   1 
ATOM   3363 C  CB  . LYS D 1 37  ? 34.619  11.579  1.305   1.00 27.44 ? 36   LYS D CB  1 
ATOM   3364 C  CG  . LYS D 1 37  ? 35.284  12.107  2.590   1.00 27.32 ? 36   LYS D CG  1 
ATOM   3365 C  CD  . LYS D 1 37  ? 36.081  13.391  2.303   1.00 31.82 ? 36   LYS D CD  1 
ATOM   3366 C  CE  . LYS D 1 37  ? 36.060  14.355  3.496   1.00 33.26 ? 36   LYS D CE  1 
ATOM   3367 N  NZ  . LYS D 1 37  ? 37.429  14.880  3.806   1.00 36.24 ? 36   LYS D NZ  1 
ATOM   3368 N  N   . GLY D 1 38  ? 35.865  8.842   0.872   1.00 26.85 ? 37   GLY D N   1 
ATOM   3369 C  CA  . GLY D 1 38  ? 36.879  7.818   1.057   1.00 26.07 ? 37   GLY D CA  1 
ATOM   3370 C  C   . GLY D 1 38  ? 36.390  6.459   0.617   1.00 26.14 ? 37   GLY D C   1 
ATOM   3371 O  O   . GLY D 1 38  ? 36.972  5.425   0.930   1.00 27.60 ? 37   GLY D O   1 
ATOM   3372 N  N   . LEU D 1 39  ? 35.310  6.458   -0.133  1.00 26.26 ? 38   LEU D N   1 
ATOM   3373 C  CA  . LEU D 1 39  ? 34.682  5.214   -0.542  1.00 25.75 ? 38   LEU D CA  1 
ATOM   3374 C  C   . LEU D 1 39  ? 35.147  4.719   -1.906  1.00 26.13 ? 38   LEU D C   1 
ATOM   3375 O  O   . LEU D 1 39  ? 35.388  5.523   -2.812  1.00 26.84 ? 38   LEU D O   1 
ATOM   3376 C  CB  . LEU D 1 39  ? 33.184  5.466   -0.617  1.00 24.31 ? 38   LEU D CB  1 
ATOM   3377 C  CG  . LEU D 1 39  ? 32.149  4.933   0.360   1.00 23.80 ? 38   LEU D CG  1 
ATOM   3378 C  CD1 . LEU D 1 39  ? 32.668  4.269   1.622   1.00 21.34 ? 38   LEU D CD1 1 
ATOM   3379 C  CD2 . LEU D 1 39  ? 31.117  6.005   0.652   1.00 23.16 ? 38   LEU D CD2 1 
ATOM   3380 N  N   . THR D 1 40  ? 35.286  3.398   -2.064  1.00 26.92 ? 39   THR D N   1 
ATOM   3381 C  CA  . THR D 1 40  ? 35.573  2.836   -3.389  1.00 26.65 ? 39   THR D CA  1 
ATOM   3382 C  C   . THR D 1 40  ? 34.324  2.999   -4.237  1.00 26.65 ? 39   THR D C   1 
ATOM   3383 O  O   . THR D 1 40  ? 33.209  2.826   -3.729  1.00 26.89 ? 39   THR D O   1 
ATOM   3384 C  CB  . THR D 1 40  ? 35.914  1.335   -3.330  1.00 26.74 ? 39   THR D CB  1 
ATOM   3385 O  OG1 . THR D 1 40  ? 34.847  0.638   -2.677  1.00 26.45 ? 39   THR D OG1 1 
ATOM   3386 C  CG2 . THR D 1 40  ? 37.134  1.068   -2.440  1.00 26.90 ? 39   THR D CG2 1 
ATOM   3387 N  N   . GLU D 1 41  ? 34.516  3.351   -5.507  1.00 26.95 ? 40   GLU D N   1 
ATOM   3388 C  CA  . GLU D 1 41  ? 33.410  3.592   -6.446  1.00 27.73 ? 40   GLU D CA  1 
ATOM   3389 C  C   . GLU D 1 41  ? 32.440  2.422   -6.492  1.00 27.81 ? 40   GLU D C   1 
ATOM   3390 O  O   . GLU D 1 41  ? 32.846  1.247   -6.544  1.00 28.01 ? 40   GLU D O   1 
ATOM   3391 C  CB  . GLU D 1 41  ? 33.889  3.939   -7.886  1.00 27.39 ? 40   GLU D CB  1 
ATOM   3392 C  CG  . GLU D 1 41  ? 32.794  4.607   -8.745  1.00 27.61 ? 40   GLU D CG  1 
ATOM   3393 C  CD  . GLU D 1 41  ? 33.054  4.597   -10.258 1.00 30.82 ? 40   GLU D CD  1 
ATOM   3394 O  OE1 . GLU D 1 41  ? 33.319  3.518   -10.825 1.00 32.03 ? 40   GLU D OE1 1 
ATOM   3395 O  OE2 . GLU D 1 41  ? 32.954  5.667   -10.906 1.00 31.35 ? 40   GLU D OE2 1 
ATOM   3396 N  N   . GLY D 1 42  ? 31.159  2.756   -6.485  1.00 27.75 ? 41   GLY D N   1 
ATOM   3397 C  CA  . GLY D 1 42  ? 30.123  1.736   -6.515  1.00 27.50 ? 41   GLY D CA  1 
ATOM   3398 C  C   . GLY D 1 42  ? 29.200  1.728   -5.303  1.00 26.79 ? 41   GLY D C   1 
ATOM   3399 O  O   . GLY D 1 42  ? 29.171  2.670   -4.494  1.00 27.91 ? 41   GLY D O   1 
ATOM   3400 N  N   . LEU D 1 43  ? 28.444  0.639   -5.202  1.00 26.05 ? 42   LEU D N   1 
ATOM   3401 C  CA  . LEU D 1 43  ? 27.430  0.438   -4.184  1.00 25.13 ? 42   LEU D CA  1 
ATOM   3402 C  C   . LEU D 1 43  ? 27.973  -0.001  -2.837  1.00 24.19 ? 42   LEU D C   1 
ATOM   3403 O  O   . LEU D 1 43  ? 28.803  -0.941  -2.730  1.00 24.83 ? 42   LEU D O   1 
ATOM   3404 C  CB  . LEU D 1 43  ? 26.433  -0.628  -4.642  1.00 24.93 ? 42   LEU D CB  1 
ATOM   3405 C  CG  . LEU D 1 43  ? 25.132  -0.278  -5.374  1.00 26.07 ? 42   LEU D CG  1 
ATOM   3406 C  CD1 . LEU D 1 43  ? 25.021  1.201   -5.672  1.00 26.05 ? 42   LEU D CD1 1 
ATOM   3407 C  CD2 . LEU D 1 43  ? 24.993  -1.117  -6.642  1.00 22.64 ? 42   LEU D CD2 1 
ATOM   3408 N  N   . HIS D 1 44  ? 27.449  0.663   -1.825  1.00 23.28 ? 43   HIS D N   1 
ATOM   3409 C  CA  . HIS D 1 44  ? 27.732  0.371   -0.431  1.00 22.83 ? 43   HIS D CA  1 
ATOM   3410 C  C   . HIS D 1 44  ? 26.478  0.272   0.419   1.00 22.24 ? 43   HIS D C   1 
ATOM   3411 O  O   . HIS D 1 44  ? 25.670  1.218   0.538   1.00 22.03 ? 43   HIS D O   1 
ATOM   3412 C  CB  . HIS D 1 44  ? 28.694  1.407   0.159   1.00 22.73 ? 43   HIS D CB  1 
ATOM   3413 C  CG  . HIS D 1 44  ? 30.030  1.409   -0.506  1.00 24.29 ? 43   HIS D CG  1 
ATOM   3414 N  ND1 . HIS D 1 44  ? 31.061  0.587   -0.102  1.00 25.75 ? 43   HIS D ND1 1 
ATOM   3415 C  CD2 . HIS D 1 44  ? 30.493  2.100   -1.574  1.00 21.10 ? 43   HIS D CD2 1 
ATOM   3416 C  CE1 . HIS D 1 44  ? 32.108  0.793   -0.878  1.00 23.99 ? 43   HIS D CE1 1 
ATOM   3417 N  NE2 . HIS D 1 44  ? 31.792  1.712   -1.772  1.00 26.39 ? 43   HIS D NE2 1 
ATOM   3418 N  N   . GLY D 1 45  ? 26.323  -0.897  1.025   1.00 22.31 ? 44   GLY D N   1 
ATOM   3419 C  CA  . GLY D 1 45  ? 25.286  -1.126  2.010   1.00 22.90 ? 44   GLY D CA  1 
ATOM   3420 C  C   . GLY D 1 45  ? 25.216  -0.121  3.141   1.00 21.72 ? 44   GLY D C   1 
ATOM   3421 O  O   . GLY D 1 45  ? 26.207  0.268   3.792   1.00 23.33 ? 44   GLY D O   1 
ATOM   3422 N  N   . PHE D 1 46  ? 23.998  0.299   3.389   1.00 21.40 ? 45   PHE D N   1 
ATOM   3423 C  CA  . PHE D 1 46  ? 23.758  1.372   4.314   1.00 20.48 ? 45   PHE D CA  1 
ATOM   3424 C  C   . PHE D 1 46  ? 22.702  0.923   5.287   1.00 19.92 ? 45   PHE D C   1 
ATOM   3425 O  O   . PHE D 1 46  ? 21.501  0.910   4.959   1.00 21.23 ? 45   PHE D O   1 
ATOM   3426 C  CB  . PHE D 1 46  ? 23.285  2.538   3.478   1.00 20.40 ? 45   PHE D CB  1 
ATOM   3427 C  CG  . PHE D 1 46  ? 23.409  3.879   4.122   1.00 19.41 ? 45   PHE D CG  1 
ATOM   3428 C  CD1 . PHE D 1 46  ? 24.610  4.302   4.693   1.00 24.09 ? 45   PHE D CD1 1 
ATOM   3429 C  CD2 . PHE D 1 46  ? 22.351  4.758   4.075   1.00 19.56 ? 45   PHE D CD2 1 
ATOM   3430 C  CE1 . PHE D 1 46  ? 24.747  5.622   5.219   1.00 24.22 ? 45   PHE D CE1 1 
ATOM   3431 C  CE2 . PHE D 1 46  ? 22.474  6.041   4.630   1.00 23.03 ? 45   PHE D CE2 1 
ATOM   3432 C  CZ  . PHE D 1 46  ? 23.696  6.444   5.226   1.00 21.82 ? 45   PHE D CZ  1 
ATOM   3433 N  N   . HIS D 1 47  ? 23.150  0.594   6.491   1.00 21.58 ? 46   HIS D N   1 
ATOM   3434 C  CA  . HIS D 1 47  ? 22.289  0.156   7.593   1.00 21.84 ? 46   HIS D CA  1 
ATOM   3435 C  C   . HIS D 1 47  ? 22.361  0.782   8.991   1.00 22.02 ? 46   HIS D C   1 
ATOM   3436 O  O   . HIS D 1 47  ? 23.446  1.193   9.526   1.00 23.97 ? 46   HIS D O   1 
ATOM   3437 C  CB  . HIS D 1 47  ? 22.460  -1.364  7.824   1.00 20.22 ? 46   HIS D CB  1 
ATOM   3438 C  CG  . HIS D 1 47  ? 22.215  -2.185  6.620   1.00 23.60 ? 46   HIS D CG  1 
ATOM   3439 N  ND1 . HIS D 1 47  ? 23.190  -2.440  5.688   1.00 23.92 ? 46   HIS D ND1 1 
ATOM   3440 C  CD2 . HIS D 1 47  ? 21.102  -2.816  6.191   1.00 20.33 ? 46   HIS D CD2 1 
ATOM   3441 C  CE1 . HIS D 1 47  ? 22.690  -3.189  4.727   1.00 25.28 ? 46   HIS D CE1 1 
ATOM   3442 N  NE2 . HIS D 1 47  ? 21.425  -3.435  5.008   1.00 27.12 ? 46   HIS D NE2 1 
ATOM   3443 N  N   . VAL D 1 48  ? 21.190  0.822   9.616   1.00 23.41 ? 47   VAL D N   1 
ATOM   3444 C  CA  . VAL D 1 48  ? 21.087  1.072   11.032  1.00 24.24 ? 47   VAL D CA  1 
ATOM   3445 C  C   . VAL D 1 48  ? 21.241  -0.271  11.768  1.00 23.46 ? 47   VAL D C   1 
ATOM   3446 O  O   . VAL D 1 48  ? 20.590  -1.259  11.434  1.00 27.09 ? 47   VAL D O   1 
ATOM   3447 C  CB  . VAL D 1 48  ? 19.777  1.822   11.445  1.00 23.04 ? 47   VAL D CB  1 
ATOM   3448 C  CG1 . VAL D 1 48  ? 19.859  2.174   12.914  1.00 21.77 ? 47   VAL D CG1 1 
ATOM   3449 C  CG2 . VAL D 1 48  ? 19.540  3.063   10.575  1.00 27.25 ? 47   VAL D CG2 1 
ATOM   3450 N  N   . HIS D 1 49  ? 22.152  -0.300  12.731  1.00 25.08 ? 48   HIS D N   1 
ATOM   3451 C  CA  . HIS D 1 49  ? 22.474  -1.465  13.522  1.00 24.35 ? 48   HIS D CA  1 
ATOM   3452 C  C   . HIS D 1 49  ? 21.972  -1.132  14.899  1.00 23.92 ? 48   HIS D C   1 
ATOM   3453 O  O   . HIS D 1 49  ? 21.815  0.050   15.294  1.00 24.71 ? 48   HIS D O   1 
ATOM   3454 C  CB  . HIS D 1 49  ? 23.975  -1.799  13.487  1.00 23.42 ? 48   HIS D CB  1 
ATOM   3455 C  CG  . HIS D 1 49  ? 24.431  -2.384  12.181  1.00 22.79 ? 48   HIS D CG  1 
ATOM   3456 N  ND1 . HIS D 1 49  ? 24.941  -3.663  12.063  1.00 25.62 ? 48   HIS D ND1 1 
ATOM   3457 C  CD2 . HIS D 1 49  ? 24.416  -1.874  10.925  1.00 21.66 ? 48   HIS D CD2 1 
ATOM   3458 C  CE1 . HIS D 1 49  ? 25.247  -3.906  10.802  1.00 18.28 ? 48   HIS D CE1 1 
ATOM   3459 N  NE2 . HIS D 1 49  ? 24.908  -2.852  10.083  1.00 24.60 ? 48   HIS D NE2 1 
ATOM   3460 N  N   . GLU D 1 50  ? 21.605  -2.189  15.574  1.00 23.34 ? 49   GLU D N   1 
ATOM   3461 C  CA  . GLU D 1 50  ? 20.909  -2.149  16.847  1.00 23.21 ? 49   GLU D CA  1 
ATOM   3462 C  C   . GLU D 1 50  ? 21.522  -1.336  17.988  1.00 22.45 ? 49   GLU D C   1 
ATOM   3463 O  O   . GLU D 1 50  ? 20.828  -0.574  18.625  1.00 25.21 ? 49   GLU D O   1 
ATOM   3464 C  CB  . GLU D 1 50  ? 20.633  -3.594  17.316  1.00 22.57 ? 49   GLU D CB  1 
ATOM   3465 C  CG  . GLU D 1 50  ? 19.740  -3.657  18.567  1.00 20.75 ? 49   GLU D CG  1 
ATOM   3466 C  CD  . GLU D 1 50  ? 19.380  -5.049  19.033  1.00 24.54 ? 49   GLU D CD  1 
ATOM   3467 O  OE1 . GLU D 1 50  ? 20.042  -6.000  18.611  1.00 26.38 ? 49   GLU D OE1 1 
ATOM   3468 O  OE2 . GLU D 1 50  ? 18.449  -5.182  19.864  1.00 26.69 ? 49   GLU D OE2 1 
ATOM   3469 N  N   . PHE D 1 51  ? 22.799  -1.513  18.252  1.00 21.85 ? 50   PHE D N   1 
ATOM   3470 C  CA  . PHE D 1 51  ? 23.430  -0.893  19.406  1.00 22.32 ? 50   PHE D CA  1 
ATOM   3471 C  C   . PHE D 1 51  ? 24.257  0.325   19.011  1.00 22.52 ? 50   PHE D C   1 
ATOM   3472 O  O   . PHE D 1 51  ? 24.954  0.280   17.988  1.00 23.29 ? 50   PHE D O   1 
ATOM   3473 C  CB  . PHE D 1 51  ? 24.284  -1.947  20.130  1.00 21.77 ? 50   PHE D CB  1 
ATOM   3474 C  CG  . PHE D 1 51  ? 23.493  -3.150  20.571  1.00 20.63 ? 50   PHE D CG  1 
ATOM   3475 C  CD1 . PHE D 1 51  ? 22.443  -3.023  21.465  1.00 19.31 ? 50   PHE D CD1 1 
ATOM   3476 C  CD2 . PHE D 1 51  ? 23.785  -4.427  20.086  1.00 19.80 ? 50   PHE D CD2 1 
ATOM   3477 C  CE1 . PHE D 1 51  ? 21.674  -4.160  21.862  1.00 19.86 ? 50   PHE D CE1 1 
ATOM   3478 C  CE2 . PHE D 1 51  ? 23.038  -5.526  20.493  1.00 20.71 ? 50   PHE D CE2 1 
ATOM   3479 C  CZ  . PHE D 1 51  ? 21.974  -5.384  21.388  1.00 17.44 ? 50   PHE D CZ  1 
ATOM   3480 N  N   . GLY D 1 52  ? 24.140  1.408   19.797  1.00 23.82 ? 51   GLY D N   1 
ATOM   3481 C  CA  . GLY D 1 52  ? 24.947  2.608   19.660  1.00 22.06 ? 51   GLY D CA  1 
ATOM   3482 C  C   . GLY D 1 52  ? 26.244  2.394   20.432  1.00 21.84 ? 51   GLY D C   1 
ATOM   3483 O  O   . GLY D 1 52  ? 26.631  3.180   21.264  1.00 22.94 ? 51   GLY D O   1 
ATOM   3484 N  N   . ASP D 1 53  ? 26.861  1.233   20.207  1.00 23.39 ? 52   ASP D N   1 
ATOM   3485 C  CA  . ASP D 1 53  ? 28.035  0.766   20.955  1.00 21.75 ? 52   ASP D CA  1 
ATOM   3486 C  C   . ASP D 1 53  ? 29.201  0.682   19.986  1.00 22.10 ? 52   ASP D C   1 
ATOM   3487 O  O   . ASP D 1 53  ? 29.210  -0.162  19.082  1.00 23.78 ? 52   ASP D O   1 
ATOM   3488 C  CB  . ASP D 1 53  ? 27.752  -0.629  21.565  1.00 22.87 ? 52   ASP D CB  1 
ATOM   3489 C  CG  . ASP D 1 53  ? 28.900  -1.160  22.488  1.00 20.49 ? 52   ASP D CG  1 
ATOM   3490 O  OD1 . ASP D 1 53  ? 30.116  -0.881  22.292  1.00 22.35 ? 52   ASP D OD1 1 
ATOM   3491 O  OD2 . ASP D 1 53  ? 28.668  -1.890  23.471  1.00 25.75 ? 52   ASP D OD2 1 
ATOM   3492 N  N   . ASN D 1 54  ? 30.175  1.562   20.190  1.00 22.61 ? 53   ASN D N   1 
ATOM   3493 C  CA  . ASN D 1 54  ? 31.400  1.654   19.418  1.00 23.52 ? 53   ASN D CA  1 
ATOM   3494 C  C   . ASN D 1 54  ? 32.631  1.186   20.175  1.00 23.02 ? 53   ASN D C   1 
ATOM   3495 O  O   . ASN D 1 54  ? 33.775  1.503   19.778  1.00 24.43 ? 53   ASN D O   1 
ATOM   3496 C  CB  . ASN D 1 54  ? 31.637  3.127   19.086  1.00 22.09 ? 53   ASN D CB  1 
ATOM   3497 C  CG  . ASN D 1 54  ? 32.644  3.318   17.958  1.00 28.06 ? 53   ASN D CG  1 
ATOM   3498 O  OD1 . ASN D 1 54  ? 32.383  2.927   16.822  1.00 30.85 ? 53   ASN D OD1 1 
ATOM   3499 N  ND2 . ASN D 1 54  ? 33.814  3.922   18.269  1.00 35.26 ? 53   ASN D ND2 1 
ATOM   3500 N  N   . THR D 1 55  ? 32.435  0.509   21.296  1.00 23.54 ? 54   THR D N   1 
ATOM   3501 C  CA  . THR D 1 55  ? 33.576  0.119   22.141  1.00 24.02 ? 54   THR D CA  1 
ATOM   3502 C  C   . THR D 1 55  ? 34.621  -0.729  21.403  1.00 24.50 ? 54   THR D C   1 
ATOM   3503 O  O   . THR D 1 55  ? 35.805  -0.565  21.618  1.00 24.75 ? 54   THR D O   1 
ATOM   3504 C  CB  . THR D 1 55  ? 33.154  -0.556  23.480  1.00 23.05 ? 54   THR D CB  1 
ATOM   3505 O  OG1 . THR D 1 55  ? 32.277  -1.660  23.220  1.00 24.53 ? 54   THR D OG1 1 
ATOM   3506 C  CG2 . THR D 1 55  ? 32.335  0.380   24.349  1.00 21.94 ? 54   THR D CG2 1 
ATOM   3507 N  N   . ALA D 1 56  ? 34.190  -1.581  20.484  1.00 26.23 ? 55   ALA D N   1 
ATOM   3508 C  CA  . ALA D 1 56  ? 35.143  -2.376  19.731  1.00 25.88 ? 55   ALA D CA  1 
ATOM   3509 C  C   . ALA D 1 56  ? 35.070  -1.940  18.287  1.00 25.83 ? 55   ALA D C   1 
ATOM   3510 O  O   . ALA D 1 56  ? 35.271  -2.722  17.363  1.00 27.51 ? 55   ALA D O   1 
ATOM   3511 C  CB  . ALA D 1 56  ? 34.835  -3.885  19.880  1.00 25.82 ? 55   ALA D CB  1 
ATOM   3512 N  N   . GLY D 1 57  ? 34.769  -0.673  18.072  1.00 26.59 ? 56   GLY D N   1 
ATOM   3513 C  CA  . GLY D 1 57  ? 34.636  -0.202  16.720  1.00 25.25 ? 56   GLY D CA  1 
ATOM   3514 C  C   . GLY D 1 57  ? 33.259  -0.560  16.251  1.00 25.30 ? 56   GLY D C   1 
ATOM   3515 O  O   . GLY D 1 57  ? 32.362  -0.817  17.076  1.00 26.40 ? 56   GLY D O   1 
ATOM   3516 N  N   . CYS D 1 58  ? 33.108  -0.598  14.929  1.00 24.69 ? 57   CYS D N   1 
ATOM   3517 C  CA  . CYS D 1 58  ? 31.823  -0.794  14.280  1.00 24.89 ? 57   CYS D CA  1 
ATOM   3518 C  C   . CYS D 1 58  ? 31.181  -2.160  14.591  1.00 24.44 ? 57   CYS D C   1 
ATOM   3519 O  O   . CYS D 1 58  ? 29.943  -2.284  14.599  1.00 24.34 ? 57   CYS D O   1 
ATOM   3520 C  CB  . CYS D 1 58  ? 31.962  -0.532  12.767  1.00 23.72 ? 57   CYS D CB  1 
ATOM   3521 S  SG  . CYS D 1 58  ? 32.338  1.203   12.445  1.00 28.03 ? 57   CYS D SG  1 
ATOM   3522 N  N   . THR D 1 59  ? 32.035  -3.138  14.900  1.00 25.59 ? 58   THR D N   1 
ATOM   3523 C  CA  . THR D 1 59  ? 31.627  -4.505  15.233  1.00 25.65 ? 58   THR D CA  1 
ATOM   3524 C  C   . THR D 1 59  ? 30.653  -4.597  16.438  1.00 25.49 ? 58   THR D C   1 
ATOM   3525 O  O   . THR D 1 59  ? 29.673  -5.362  16.410  1.00 26.65 ? 58   THR D O   1 
ATOM   3526 C  CB  . THR D 1 59  ? 32.908  -5.348  15.449  1.00 26.04 ? 58   THR D CB  1 
ATOM   3527 O  OG1 . THR D 1 59  ? 33.805  -5.150  14.333  1.00 29.17 ? 58   THR D OG1 1 
ATOM   3528 C  CG2 . THR D 1 59  ? 32.605  -6.812  15.399  1.00 24.50 ? 58   THR D CG2 1 
ATOM   3529 N  N   . SER D 1 60  ? 30.901  -3.813  17.479  1.00 26.08 ? 59   SER D N   1 
ATOM   3530 C  CA  . SER D 1 60  ? 30.028  -3.801  18.660  1.00 25.37 ? 59   SER D CA  1 
ATOM   3531 C  C   . SER D 1 60  ? 28.635  -3.175  18.475  1.00 24.21 ? 59   SER D C   1 
ATOM   3532 O  O   . SER D 1 60  ? 27.876  -3.102  19.430  1.00 24.84 ? 59   SER D O   1 
ATOM   3533 C  CB  . SER D 1 60  ? 30.733  -3.235  19.903  1.00 24.27 ? 59   SER D CB  1 
ATOM   3534 O  OG  . SER D 1 60  ? 31.673  -2.231  19.591  1.00 28.30 ? 59   SER D OG  1 
ATOM   3535 N  N   . ALA D 1 61  ? 28.307  -2.753  17.256  1.00 24.77 ? 60   ALA D N   1 
ATOM   3536 C  CA  . ALA D 1 61  ? 26.984  -2.195  16.935  1.00 24.01 ? 60   ALA D CA  1 
ATOM   3537 C  C   . ALA D 1 61  ? 25.927  -3.292  16.801  1.00 23.88 ? 60   ALA D C   1 
ATOM   3538 O  O   . ALA D 1 61  ? 24.706  -3.017  16.728  1.00 23.72 ? 60   ALA D O   1 
ATOM   3539 C  CB  . ALA D 1 61  ? 27.040  -1.377  15.674  1.00 24.29 ? 60   ALA D CB  1 
ATOM   3540 N  N   . GLY D 1 62  ? 26.414  -4.531  16.757  1.00 24.59 ? 61   GLY D N   1 
ATOM   3541 C  CA  . GLY D 1 62  ? 25.594  -5.725  16.645  1.00 24.61 ? 61   GLY D CA  1 
ATOM   3542 C  C   . GLY D 1 62  ? 25.005  -5.899  15.263  1.00 24.18 ? 61   GLY D C   1 
ATOM   3543 O  O   . GLY D 1 62  ? 25.616  -5.512  14.282  1.00 24.40 ? 61   GLY D O   1 
ATOM   3544 N  N   . PRO D 1 63  ? 23.817  -6.488  15.189  1.00 25.70 ? 62   PRO D N   1 
ATOM   3545 C  CA  . PRO D 1 63  ? 23.147  -6.755  13.911  1.00 26.49 ? 62   PRO D CA  1 
ATOM   3546 C  C   . PRO D 1 63  ? 22.295  -5.592  13.430  1.00 27.27 ? 62   PRO D C   1 
ATOM   3547 O  O   . PRO D 1 63  ? 22.173  -4.598  14.129  1.00 28.12 ? 62   PRO D O   1 
ATOM   3548 C  CB  . PRO D 1 63  ? 22.224  -7.947  14.241  1.00 26.20 ? 62   PRO D CB  1 
ATOM   3549 C  CG  . PRO D 1 63  ? 22.175  -8.027  15.746  1.00 25.13 ? 62   PRO D CG  1 
ATOM   3550 C  CD  . PRO D 1 63  ? 23.016  -6.950  16.330  1.00 25.33 ? 62   PRO D CD  1 
ATOM   3551 N  N   . HIS D 1 64  ? 21.700  -5.752  12.248  1.00 28.64 ? 63   HIS D N   1 
ATOM   3552 C  CA  . HIS D 1 64  ? 20.748  -4.784  11.726  1.00 28.84 ? 63   HIS D CA  1 
ATOM   3553 C  C   . HIS D 1 64  ? 19.601  -4.590  12.713  1.00 28.23 ? 63   HIS D C   1 
ATOM   3554 O  O   . HIS D 1 64  ? 19.120  -5.546  13.300  1.00 27.73 ? 63   HIS D O   1 
ATOM   3555 C  CB  . HIS D 1 64  ? 20.202  -5.231  10.371  1.00 28.81 ? 63   HIS D CB  1 
ATOM   3556 C  CG  . HIS D 1 64  ? 21.264  -5.480  9.349   1.00 30.75 ? 63   HIS D CG  1 
ATOM   3557 N  ND1 . HIS D 1 64  ? 20.999  -6.042  8.126   1.00 34.91 ? 63   HIS D ND1 1 
ATOM   3558 C  CD2 . HIS D 1 64  ? 22.596  -5.221  9.362   1.00 33.98 ? 63   HIS D CD2 1 
ATOM   3559 C  CE1 . HIS D 1 64  ? 22.114  -6.124  7.422   1.00 34.79 ? 63   HIS D CE1 1 
ATOM   3560 N  NE2 . HIS D 1 64  ? 23.102  -5.637  8.151   1.00 35.60 ? 63   HIS D NE2 1 
ATOM   3561 N  N   . PHE D 1 65  ? 19.218  -3.338  12.921  1.00 28.00 ? 64   PHE D N   1 
ATOM   3562 C  CA  . PHE D 1 65  ? 18.098  -2.980  13.782  1.00 27.61 ? 64   PHE D CA  1 
ATOM   3563 C  C   . PHE D 1 65  ? 16.846  -3.631  13.209  1.00 28.29 ? 64   PHE D C   1 
ATOM   3564 O  O   . PHE D 1 65  ? 16.470  -3.356  12.070  1.00 29.92 ? 64   PHE D O   1 
ATOM   3565 C  CB  . PHE D 1 65  ? 17.953  -1.453  13.798  1.00 25.66 ? 64   PHE D CB  1 
ATOM   3566 C  CG  . PHE D 1 65  ? 16.805  -0.947  14.642  1.00 23.63 ? 64   PHE D CG  1 
ATOM   3567 C  CD1 . PHE D 1 65  ? 16.557  -1.481  15.898  1.00 22.61 ? 64   PHE D CD1 1 
ATOM   3568 C  CD2 . PHE D 1 65  ? 16.031  0.131   14.194  1.00 24.40 ? 64   PHE D CD2 1 
ATOM   3569 C  CE1 . PHE D 1 65  ? 15.488  -1.036  16.700  1.00 20.31 ? 64   PHE D CE1 1 
ATOM   3570 C  CE2 . PHE D 1 65  ? 14.984  0.633   14.968  1.00 21.97 ? 64   PHE D CE2 1 
ATOM   3571 C  CZ  . PHE D 1 65  ? 14.697  0.062   16.238  1.00 21.11 ? 64   PHE D CZ  1 
ATOM   3572 N  N   . ASN D 1 66  ? 16.201  -4.485  14.004  1.00 29.03 ? 65   ASN D N   1 
ATOM   3573 C  CA  . ASN D 1 66  ? 15.027  -5.247  13.574  1.00 30.36 ? 65   ASN D CA  1 
ATOM   3574 C  C   . ASN D 1 66  ? 14.112  -5.583  14.733  1.00 30.73 ? 65   ASN D C   1 
ATOM   3575 O  O   . ASN D 1 66  ? 13.997  -6.750  15.124  1.00 30.80 ? 65   ASN D O   1 
ATOM   3576 C  CB  . ASN D 1 66  ? 15.463  -6.551  12.937  1.00 29.88 ? 65   ASN D CB  1 
ATOM   3577 C  CG  . ASN D 1 66  ? 14.454  -7.056  11.967  1.00 32.21 ? 65   ASN D CG  1 
ATOM   3578 O  OD1 . ASN D 1 66  ? 13.846  -6.262  11.230  1.00 36.44 ? 65   ASN D OD1 1 
ATOM   3579 N  ND2 . ASN D 1 66  ? 14.227  -8.365  11.966  1.00 29.69 ? 65   ASN D ND2 1 
ATOM   3580 N  N   . PRO D 1 67  ? 13.413  -4.563  15.219  1.00 31.69 ? 66   PRO D N   1 
ATOM   3581 C  CA  . PRO D 1 67  ? 12.667  -4.597  16.488  1.00 32.51 ? 66   PRO D CA  1 
ATOM   3582 C  C   . PRO D 1 67  ? 11.394  -5.450  16.584  1.00 34.12 ? 66   PRO D C   1 
ATOM   3583 O  O   . PRO D 1 67  ? 11.022  -5.859  17.718  1.00 35.70 ? 66   PRO D O   1 
ATOM   3584 C  CB  . PRO D 1 67  ? 12.351  -3.114  16.719  1.00 32.68 ? 66   PRO D CB  1 
ATOM   3585 C  CG  . PRO D 1 67  ? 12.295  -2.535  15.366  1.00 31.48 ? 66   PRO D CG  1 
ATOM   3586 C  CD  . PRO D 1 67  ? 13.281  -3.271  14.530  1.00 31.17 ? 66   PRO D CD  1 
ATOM   3587 N  N   . LEU D 1 68  ? 10.736  -5.722  15.450  1.00 34.46 ? 67   LEU D N   1 
ATOM   3588 C  CA  . LEU D 1 68  ? 9.590   -6.636  15.415  1.00 34.89 ? 67   LEU D CA  1 
ATOM   3589 C  C   . LEU D 1 68  ? 9.929   -7.806  14.492  1.00 34.93 ? 67   LEU D C   1 
ATOM   3590 O  O   . LEU D 1 68  ? 9.646   -8.969  14.797  1.00 35.76 ? 67   LEU D O   1 
ATOM   3591 C  CB  . LEU D 1 68  ? 8.314   -5.919  14.937  1.00 34.74 ? 67   LEU D CB  1 
ATOM   3592 C  CG  . LEU D 1 68  ? 7.390   -6.534  13.865  1.00 35.15 ? 67   LEU D CG  1 
ATOM   3593 C  CD1 . LEU D 1 68  ? 8.130   -6.818  12.559  1.00 36.48 ? 67   LEU D CD1 1 
ATOM   3594 C  CD2 . LEU D 1 68  ? 6.617   -7.787  14.319  1.00 37.06 ? 67   LEU D CD2 1 
ATOM   3595 N  N   . ARG D 1 80  ? 11.296  -6.079  4.650   1.00 35.19 ? 79   ARG D N   1 
ATOM   3596 C  CA  . ARG D 1 80  ? 12.621  -5.476  4.899   1.00 34.81 ? 79   ARG D CA  1 
ATOM   3597 C  C   . ARG D 1 80  ? 12.970  -5.271  6.385   1.00 33.44 ? 79   ARG D C   1 
ATOM   3598 O  O   . ARG D 1 80  ? 12.133  -4.830  7.175   1.00 33.97 ? 79   ARG D O   1 
ATOM   3599 C  CB  . ARG D 1 80  ? 12.795  -4.147  4.125   1.00 35.62 ? 79   ARG D CB  1 
ATOM   3600 C  CG  . ARG D 1 80  ? 12.198  -2.879  4.759   1.00 38.57 ? 79   ARG D CG  1 
ATOM   3601 C  CD  . ARG D 1 80  ? 13.107  -1.625  4.592   1.00 44.30 ? 79   ARG D CD  1 
ATOM   3602 N  NE  . ARG D 1 80  ? 12.403  -0.350  4.761   1.00 48.91 ? 79   ARG D NE  1 
ATOM   3603 C  CZ  . ARG D 1 80  ? 11.967  0.419   3.758   1.00 52.01 ? 79   ARG D CZ  1 
ATOM   3604 N  NH1 . ARG D 1 80  ? 12.147  0.057   2.485   1.00 53.04 ? 79   ARG D NH1 1 
ATOM   3605 N  NH2 . ARG D 1 80  ? 11.332  1.555   4.030   1.00 53.76 ? 79   ARG D NH2 1 
ATOM   3606 N  N   . HIS D 1 81  ? 14.187  -5.582  6.805   1.00 31.76 ? 80   HIS D N   1 
ATOM   3607 C  CA  . HIS D 1 81  ? 14.466  -5.237  8.189   1.00 29.71 ? 80   HIS D CA  1 
ATOM   3608 N  N   . VAL D 1 82  ? 13.920  -3.194  9.337   1.00 28.02 ? 81   VAL D N   1 
ATOM   3609 C  CA  . VAL D 1 82  ? 13.854  -1.752  9.592   1.00 27.20 ? 81   VAL D CA  1 
ATOM   3610 C  C   . VAL D 1 82  ? 15.142  -0.931  9.343   1.00 28.43 ? 81   VAL D C   1 
ATOM   3611 O  O   . VAL D 1 82  ? 15.099  0.110   8.700   1.00 30.15 ? 81   VAL D O   1 
ATOM   3612 C  CB  . VAL D 1 82  ? 13.323  -1.479  11.040  1.00 26.28 ? 81   VAL D CB  1 
ATOM   3613 C  CG1 . VAL D 1 82  ? 13.280  0.070   11.367  1.00 23.79 ? 81   VAL D CG1 1 
ATOM   3614 C  CG2 . VAL D 1 82  ? 11.959  -2.143  11.291  1.00 25.70 ? 81   VAL D CG2 1 
ATOM   3615 N  N   . GLY D 1 83  ? 16.289  -1.396  9.832   1.00 29.52 ? 82   GLY D N   1 
ATOM   3616 C  CA  . GLY D 1 83  ? 17.553  -0.683  9.653   1.00 29.19 ? 82   GLY D CA  1 
ATOM   3617 C  C   . GLY D 1 83  ? 18.144  -0.743  8.247   1.00 28.66 ? 82   GLY D C   1 
ATOM   3618 O  O   . GLY D 1 83  ? 19.156  -0.096  7.992   1.00 30.23 ? 82   GLY D O   1 
ATOM   3619 N  N   . ASP D 1 84  ? 17.519  -1.533  7.354   1.00 27.78 ? 83   ASP D N   1 
ATOM   3620 C  CA  . ASP D 1 84  ? 17.961  -1.672  5.953   1.00 26.33 ? 83   ASP D CA  1 
ATOM   3621 C  C   . ASP D 1 84  ? 17.593  -0.450  5.129   1.00 25.02 ? 83   ASP D C   1 
ATOM   3622 O  O   . ASP D 1 84  ? 16.468  -0.359  4.690   1.00 27.49 ? 83   ASP D O   1 
ATOM   3623 C  CB  . ASP D 1 84  ? 17.260  -2.865  5.282   1.00 25.92 ? 83   ASP D CB  1 
ATOM   3624 N  N   . LEU D 1 85  ? 18.519  0.479   4.907   1.00 25.10 ? 84   LEU D N   1 
ATOM   3625 C  CA  . LEU D 1 85  ? 18.213  1.671   4.122   1.00 23.22 ? 84   LEU D CA  1 
ATOM   3626 C  C   . LEU D 1 85  ? 18.717  1.543   2.671   1.00 23.28 ? 84   LEU D C   1 
ATOM   3627 O  O   . LEU D 1 85  ? 18.820  2.514   1.946   1.00 24.81 ? 84   LEU D O   1 
ATOM   3628 C  CB  . LEU D 1 85  ? 18.766  2.907   4.827   1.00 22.81 ? 84   LEU D CB  1 
ATOM   3629 C  CG  . LEU D 1 85  ? 18.286  3.299   6.224   1.00 21.41 ? 84   LEU D CG  1 
ATOM   3630 C  CD1 . LEU D 1 85  ? 19.208  4.406   6.778   1.00 22.23 ? 84   LEU D CD1 1 
ATOM   3631 C  CD2 . LEU D 1 85  ? 16.794  3.738   6.147   1.00 24.34 ? 84   LEU D CD2 1 
ATOM   3632 N  N   . GLY D 1 86  ? 19.036  0.328   2.241   1.00 22.77 ? 85   GLY D N   1 
ATOM   3633 C  CA  . GLY D 1 86  ? 19.547  0.116   0.902   1.00 22.21 ? 85   GLY D CA  1 
ATOM   3634 C  C   . GLY D 1 86  ? 21.026  0.422   0.811   1.00 21.16 ? 85   GLY D C   1 
ATOM   3635 O  O   . GLY D 1 86  ? 21.767  0.134   1.731   1.00 22.41 ? 85   GLY D O   1 
ATOM   3636 N  N   . ASN D 1 87  ? 21.434  1.030   -0.295  1.00 21.47 ? 86   ASN D N   1 
ATOM   3637 C  CA  . ASN D 1 87  ? 22.820  1.316   -0.580  1.00 21.61 ? 86   ASN D CA  1 
ATOM   3638 C  C   . ASN D 1 87  ? 23.060  2.776   -0.746  1.00 21.32 ? 86   ASN D C   1 
ATOM   3639 O  O   . ASN D 1 87  ? 22.140  3.539   -0.975  1.00 23.48 ? 86   ASN D O   1 
ATOM   3640 C  CB  . ASN D 1 87  ? 23.255  0.682   -1.888  1.00 20.87 ? 86   ASN D CB  1 
ATOM   3641 C  CG  . ASN D 1 87  ? 23.198  -0.810  -1.850  1.00 22.61 ? 86   ASN D CG  1 
ATOM   3642 O  OD1 . ASN D 1 87  ? 23.979  -1.453  -1.137  1.00 27.51 ? 86   ASN D OD1 1 
ATOM   3643 N  ND2 . ASN D 1 87  ? 22.283  -1.389  -2.622  1.00 26.62 ? 86   ASN D ND2 1 
ATOM   3644 N  N   . VAL D 1 88  ? 24.321  3.147   -0.634  1.00 23.28 ? 87   VAL D N   1 
ATOM   3645 C  CA  . VAL D 1 88  ? 24.746  4.490   -1.024  1.00 22.32 ? 87   VAL D CA  1 
ATOM   3646 C  C   . VAL D 1 88  ? 25.685  4.232   -2.206  1.00 23.66 ? 87   VAL D C   1 
ATOM   3647 O  O   . VAL D 1 88  ? 26.178  3.105   -2.405  1.00 25.56 ? 87   VAL D O   1 
ATOM   3648 C  CB  . VAL D 1 88  ? 25.365  5.337   0.133   1.00 20.73 ? 87   VAL D CB  1 
ATOM   3649 C  CG1 . VAL D 1 88  ? 24.342  5.515   1.328   1.00 20.31 ? 87   VAL D CG1 1 
ATOM   3650 C  CG2 . VAL D 1 88  ? 26.737  4.783   0.658   1.00 18.20 ? 87   VAL D CG2 1 
ATOM   3651 N  N   . THR D 1 89  ? 25.915  5.253   -3.004  1.00 25.03 ? 88   THR D N   1 
ATOM   3652 C  CA  . THR D 1 89  ? 26.676  5.107   -4.232  1.00 25.71 ? 88   THR D CA  1 
ATOM   3653 C  C   . THR D 1 89  ? 27.817  6.105   -4.301  1.00 26.20 ? 88   THR D C   1 
ATOM   3654 O  O   . THR D 1 89  ? 27.582  7.314   -4.373  1.00 27.24 ? 88   THR D O   1 
ATOM   3655 C  CB  . THR D 1 89  ? 25.722  5.342   -5.432  1.00 25.12 ? 88   THR D CB  1 
ATOM   3656 O  OG1 . THR D 1 89  ? 24.743  4.293   -5.493  1.00 27.25 ? 88   THR D OG1 1 
ATOM   3657 C  CG2 . THR D 1 89  ? 26.456  5.227   -6.779  1.00 25.52 ? 88   THR D CG2 1 
ATOM   3658 N  N   . ALA D 1 90  ? 29.055  5.622   -4.290  1.00 27.06 ? 89   ALA D N   1 
ATOM   3659 C  CA  . ALA D 1 90  ? 30.196  6.536   -4.423  1.00 27.37 ? 89   ALA D CA  1 
ATOM   3660 C  C   . ALA D 1 90  ? 30.579  6.755   -5.877  1.00 27.62 ? 89   ALA D C   1 
ATOM   3661 O  O   . ALA D 1 90  ? 30.513  5.825   -6.687  1.00 28.54 ? 89   ALA D O   1 
ATOM   3662 C  CB  . ALA D 1 90  ? 31.408  6.044   -3.612  1.00 27.19 ? 89   ALA D CB  1 
ATOM   3663 N  N   . ASP D 1 91  ? 30.949  7.991   -6.212  1.00 28.16 ? 90   ASP D N   1 
ATOM   3664 C  CA  . ASP D 1 91  ? 31.399  8.320   -7.552  1.00 27.72 ? 90   ASP D CA  1 
ATOM   3665 C  C   . ASP D 1 91  ? 32.869  7.965   -7.665  1.00 28.13 ? 90   ASP D C   1 
ATOM   3666 O  O   . ASP D 1 91  ? 33.467  7.478   -6.702  1.00 28.83 ? 90   ASP D O   1 
ATOM   3667 C  CB  . ASP D 1 91  ? 31.177  9.791   -7.872  1.00 27.77 ? 90   ASP D CB  1 
ATOM   3668 C  CG  . ASP D 1 91  ? 31.930  10.713  -6.947  1.00 28.50 ? 90   ASP D CG  1 
ATOM   3669 O  OD1 . ASP D 1 91  ? 32.932  10.290  -6.330  1.00 29.13 ? 90   ASP D OD1 1 
ATOM   3670 O  OD2 . ASP D 1 91  ? 31.582  11.898  -6.765  1.00 31.98 ? 90   ASP D OD2 1 
ATOM   3671 N  N   . LYS D 1 92  ? 33.434  8.227   -8.840  1.00 28.21 ? 91   LYS D N   1 
ATOM   3672 C  CA  . LYS D 1 92  ? 34.826  7.914   -9.168  1.00 27.75 ? 91   LYS D CA  1 
ATOM   3673 C  C   . LYS D 1 92  ? 35.839  8.477   -8.173  1.00 27.93 ? 91   LYS D C   1 
ATOM   3674 O  O   . LYS D 1 92  ? 36.959  7.966   -8.052  1.00 27.85 ? 91   LYS D O   1 
ATOM   3675 C  CB  . LYS D 1 92  ? 35.164  8.414   -10.588 1.00 27.90 ? 91   LYS D CB  1 
ATOM   3676 N  N   . ASP D 1 93  ? 35.454  9.539   -7.476  1.00 28.17 ? 92   ASP D N   1 
ATOM   3677 C  CA  . ASP D 1 93  ? 36.357  10.141  -6.515  1.00 28.27 ? 92   ASP D CA  1 
ATOM   3678 C  C   . ASP D 1 93  ? 36.101  9.628   -5.091  1.00 27.74 ? 92   ASP D C   1 
ATOM   3679 O  O   . ASP D 1 93  ? 36.615  10.196  -4.127  1.00 28.03 ? 92   ASP D O   1 
ATOM   3680 C  CB  . ASP D 1 93  ? 36.272  11.678  -6.565  1.00 28.96 ? 92   ASP D CB  1 
ATOM   3681 C  CG  . ASP D 1 93  ? 36.667  12.269  -7.922  1.00 30.33 ? 92   ASP D CG  1 
ATOM   3682 O  OD1 . ASP D 1 93  ? 37.825  12.072  -8.403  1.00 30.59 ? 92   ASP D OD1 1 
ATOM   3683 O  OD2 . ASP D 1 93  ? 35.880  13.002  -8.573  1.00 33.01 ? 92   ASP D OD2 1 
ATOM   3684 N  N   . GLY D 1 94  ? 35.318  8.552   -4.959  1.00 26.69 ? 93   GLY D N   1 
ATOM   3685 C  CA  . GLY D 1 94  ? 34.980  7.978   -3.664  1.00 26.42 ? 93   GLY D CA  1 
ATOM   3686 C  C   . GLY D 1 94  ? 33.981  8.778   -2.839  1.00 25.81 ? 93   GLY D C   1 
ATOM   3687 O  O   . GLY D 1 94  ? 33.901  8.616   -1.616  1.00 27.17 ? 93   GLY D O   1 
ATOM   3688 N  N   . VAL D 1 95  ? 33.210  9.620   -3.515  1.00 26.10 ? 94   VAL D N   1 
ATOM   3689 C  CA  . VAL D 1 95  ? 32.237  10.506  -2.876  1.00 25.64 ? 94   VAL D CA  1 
ATOM   3690 C  C   . VAL D 1 95  ? 30.806  10.109  -3.162  1.00 25.55 ? 94   VAL D C   1 
ATOM   3691 O  O   . VAL D 1 95  ? 30.378  10.037  -4.314  1.00 26.55 ? 94   VAL D O   1 
ATOM   3692 C  CB  . VAL D 1 95  ? 32.395  11.959  -3.353  1.00 25.95 ? 94   VAL D CB  1 
ATOM   3693 C  CG1 . VAL D 1 95  ? 31.607  12.908  -2.421  1.00 25.28 ? 94   VAL D CG1 1 
ATOM   3694 C  CG2 . VAL D 1 95  ? 33.852  12.341  -3.399  1.00 26.00 ? 94   VAL D CG2 1 
ATOM   3695 N  N   . ALA D 1 96  ? 30.076  9.865   -2.084  1.00 26.06 ? 95   ALA D N   1 
ATOM   3696 C  CA  . ALA D 1 96  ? 28.678  9.492   -2.142  1.00 26.36 ? 95   ALA D CA  1 
ATOM   3697 C  C   . ALA D 1 96  ? 27.817  10.566  -1.494  1.00 26.94 ? 95   ALA D C   1 
ATOM   3698 O  O   . ALA D 1 96  ? 27.845  10.732  -0.260  1.00 28.70 ? 95   ALA D O   1 
ATOM   3699 C  CB  . ALA D 1 96  ? 28.467  8.156   -1.435  1.00 25.04 ? 95   ALA D CB  1 
ATOM   3700 N  N   . ASP D 1 97  ? 27.052  11.274  -2.316  1.00 28.31 ? 96   ASP D N   1 
ATOM   3701 C  CA  . ASP D 1 97  ? 26.135  12.278  -1.796  1.00 29.88 ? 96   ASP D CA  1 
ATOM   3702 C  C   . ASP D 1 97  ? 24.776  11.622  -1.574  1.00 29.16 ? 96   ASP D C   1 
ATOM   3703 O  O   . ASP D 1 97  ? 24.100  11.204  -2.515  1.00 30.73 ? 96   ASP D O   1 
ATOM   3704 C  CB  . ASP D 1 97  ? 26.075  13.515  -2.676  1.00 30.44 ? 96   ASP D CB  1 
ATOM   3705 C  CG  . ASP D 1 97  ? 26.904  14.671  -2.102  1.00 34.82 ? 96   ASP D CG  1 
ATOM   3706 O  OD1 . ASP D 1 97  ? 28.080  14.830  -2.511  1.00 35.94 ? 96   ASP D OD1 1 
ATOM   3707 O  OD2 . ASP D 1 97  ? 26.469  15.464  -1.219  1.00 39.90 ? 96   ASP D OD2 1 
ATOM   3708 N  N   . VAL D 1 98  ? 24.398  11.519  -0.314  1.00 28.64 ? 97   VAL D N   1 
ATOM   3709 C  CA  . VAL D 1 98  ? 23.225  10.759  0.070   1.00 27.89 ? 97   VAL D CA  1 
ATOM   3710 C  C   . VAL D 1 98  ? 21.978  11.595  0.123   1.00 28.12 ? 97   VAL D C   1 
ATOM   3711 O  O   . VAL D 1 98  ? 21.975  12.691  0.672   1.00 29.19 ? 97   VAL D O   1 
ATOM   3712 C  CB  . VAL D 1 98  ? 23.416  10.091  1.466   1.00 26.98 ? 97   VAL D CB  1 
ATOM   3713 C  CG1 . VAL D 1 98  ? 22.186  9.227   1.852   1.00 25.62 ? 97   VAL D CG1 1 
ATOM   3714 C  CG2 . VAL D 1 98  ? 24.741  9.318   1.533   1.00 27.31 ? 97   VAL D CG2 1 
ATOM   3715 N  N   . SER D 1 99  ? 20.936  11.062  -0.506  1.00 29.00 ? 98   SER D N   1 
ATOM   3716 C  CA  . SER D 1 99  ? 19.580  11.577  -0.420  1.00 28.77 ? 98   SER D CA  1 
ATOM   3717 C  C   . SER D 1 99  ? 18.684  10.331  -0.447  1.00 28.60 ? 98   SER D C   1 
ATOM   3718 O  O   . SER D 1 99  ? 18.708  9.551   -1.410  1.00 29.35 ? 98   SER D O   1 
ATOM   3719 C  CB  . SER D 1 99  ? 19.253  12.529  -1.564  1.00 28.48 ? 98   SER D CB  1 
ATOM   3720 O  OG  . SER D 1 99  ? 17.927  13.047  -1.450  1.00 29.78 ? 98   SER D OG  1 
ATOM   3721 N  N   . ILE D 1 100 ? 17.906  10.161  0.615   1.00 28.61 ? 99   ILE D N   1 
ATOM   3722 C  CA  . ILE D 1 100 ? 17.013  9.018   0.792   1.00 28.26 ? 99   ILE D CA  1 
ATOM   3723 C  C   . ILE D 1 100 ? 15.782  9.456   1.595   1.00 29.03 ? 99   ILE D C   1 
ATOM   3724 O  O   . ILE D 1 100 ? 15.885  10.277  2.507   1.00 29.81 ? 99   ILE D O   1 
ATOM   3725 C  CB  . ILE D 1 100 ? 17.728  7.936   1.612   1.00 28.77 ? 99   ILE D CB  1 
ATOM   3726 C  CG1 . ILE D 1 100 ? 18.855  7.257   0.833   1.00 25.00 ? 99   ILE D CG1 1 
ATOM   3727 C  CG2 . ILE D 1 100 ? 16.715  6.891   2.150   1.00 27.27 ? 99   ILE D CG2 1 
ATOM   3728 C  CD1 . ILE D 1 100 ? 19.773  6.459   1.743   1.00 21.26 ? 99   ILE D CD1 1 
ATOM   3729 N  N   . GLU D 1 101 ? 14.626  8.897   1.255   1.00 29.03 ? 100  GLU D N   1 
ATOM   3730 C  CA  . GLU D 1 101 ? 13.396  9.046   2.035   1.00 28.57 ? 100  GLU D CA  1 
ATOM   3731 C  C   . GLU D 1 101 ? 12.970  7.658   2.512   1.00 28.18 ? 100  GLU D C   1 
ATOM   3732 O  O   . GLU D 1 101 ? 12.817  6.745   1.699   1.00 29.24 ? 100  GLU D O   1 
ATOM   3733 C  CB  . GLU D 1 101 ? 12.271  9.623   1.205   1.00 28.77 ? 100  GLU D CB  1 
ATOM   3734 C  CG  . GLU D 1 101 ? 12.066  11.122  1.374   1.00 31.54 ? 100  GLU D CG  1 
ATOM   3735 C  CD  . GLU D 1 101 ? 10.594  11.529  1.396   1.00 33.01 ? 100  GLU D CD  1 
ATOM   3736 O  OE1 . GLU D 1 101 ? 10.312  12.716  1.650   1.00 36.26 ? 100  GLU D OE1 1 
ATOM   3737 O  OE2 . GLU D 1 101 ? 9.714   10.673  1.161   1.00 35.87 ? 100  GLU D OE2 1 
ATOM   3738 N  N   . ASP D 1 102 ? 12.790  7.498   3.816   1.00 28.14 ? 101  ASP D N   1 
ATOM   3739 C  CA  . ASP D 1 102 ? 12.362  6.238   4.371   1.00 27.85 ? 101  ASP D CA  1 
ATOM   3740 C  C   . ASP D 1 102 ? 11.138  6.404   5.284   1.00 28.33 ? 101  ASP D C   1 
ATOM   3741 O  O   . ASP D 1 102 ? 11.036  7.390   6.044   1.00 29.75 ? 101  ASP D O   1 
ATOM   3742 C  CB  . ASP D 1 102 ? 13.500  5.540   5.114   1.00 27.74 ? 101  ASP D CB  1 
ATOM   3743 C  CG  . ASP D 1 102 ? 13.206  4.073   5.330   1.00 26.42 ? 101  ASP D CG  1 
ATOM   3744 O  OD1 . ASP D 1 102 ? 13.296  3.315   4.349   1.00 31.55 ? 101  ASP D OD1 1 
ATOM   3745 O  OD2 . ASP D 1 102 ? 12.826  3.606   6.413   1.00 28.75 ? 101  ASP D OD2 1 
ATOM   3746 N  N   . SER D 1 103 ? 10.231  5.431   5.226   1.00 28.27 ? 102  SER D N   1 
ATOM   3747 C  CA  . SER D 1 103 ? 8.977   5.486   5.983   1.00 28.20 ? 102  SER D CA  1 
ATOM   3748 C  C   . SER D 1 103 ? 8.855   4.344   6.980   1.00 28.05 ? 102  SER D C   1 
ATOM   3749 O  O   . SER D 1 103 ? 7.782   4.103   7.550   1.00 29.07 ? 102  SER D O   1 
ATOM   3750 C  CB  . SER D 1 103 ? 7.785   5.453   5.027   1.00 28.20 ? 102  SER D CB  1 
ATOM   3751 O  OG  . SER D 1 103 ? 8.000   6.280   3.887   1.00 30.55 ? 102  SER D OG  1 
ATOM   3752 N  N   . VAL D 1 104 ? 9.953   3.623   7.159   1.00 27.98 ? 103  VAL D N   1 
ATOM   3753 C  CA  . VAL D 1 104 ? 9.983   2.522   8.099   1.00 27.06 ? 103  VAL D CA  1 
ATOM   3754 C  C   . VAL D 1 104 ? 10.805  2.899   9.324   1.00 27.22 ? 103  VAL D C   1 
ATOM   3755 O  O   . VAL D 1 104 ? 10.452  2.506   10.430  1.00 28.76 ? 103  VAL D O   1 
ATOM   3756 C  CB  . VAL D 1 104 ? 10.448  1.198   7.453   1.00 26.22 ? 103  VAL D CB  1 
ATOM   3757 C  CG1 . VAL D 1 104 ? 10.937  0.240   8.518   1.00 26.13 ? 103  VAL D CG1 1 
ATOM   3758 C  CG2 . VAL D 1 104 ? 9.285   0.535   6.705   1.00 26.11 ? 103  VAL D CG2 1 
ATOM   3759 N  N   . ILE D 1 105 ? 11.881  3.666   9.123   1.00 26.92 ? 104  ILE D N   1 
ATOM   3760 C  CA  . ILE D 1 105 ? 12.655  4.216   10.238  1.00 25.41 ? 104  ILE D CA  1 
ATOM   3761 C  C   . ILE D 1 105 ? 11.906  5.387   10.879  1.00 25.83 ? 104  ILE D C   1 
ATOM   3762 O  O   . ILE D 1 105 ? 10.976  5.938   10.294  1.00 27.33 ? 104  ILE D O   1 
ATOM   3763 C  CB  . ILE D 1 105 ? 14.132  4.605   9.865   1.00 24.63 ? 104  ILE D CB  1 
ATOM   3764 C  CG1 . ILE D 1 105 ? 14.209  5.662   8.743   1.00 20.48 ? 104  ILE D CG1 1 
ATOM   3765 C  CG2 . ILE D 1 105 ? 14.936  3.362   9.583   1.00 24.78 ? 104  ILE D CG2 1 
ATOM   3766 C  CD1 . ILE D 1 105 ? 15.537  6.435   8.652   1.00 20.27 ? 104  ILE D CD1 1 
ATOM   3767 N  N   . SER D 1 106 ? 12.263  5.697   12.112  1.00 25.64 ? 105  SER D N   1 
ATOM   3768 C  CA  . SER D 1 106 ? 11.689  6.820   12.832  1.00 24.92 ? 105  SER D CA  1 
ATOM   3769 C  C   . SER D 1 106 ? 12.674  7.459   13.812  1.00 25.43 ? 105  SER D C   1 
ATOM   3770 O  O   . SER D 1 106 ? 13.717  6.879   14.183  1.00 26.79 ? 105  SER D O   1 
ATOM   3771 C  CB  . SER D 1 106 ? 10.430  6.358   13.577  1.00 24.05 ? 105  SER D CB  1 
ATOM   3772 O  OG  . SER D 1 106 ? 9.573   7.418   13.949  1.00 25.59 ? 105  SER D OG  1 
ATOM   3773 N  N   . LEU D 1 107 ? 12.329  8.674   14.240  1.00 26.48 ? 106  LEU D N   1 
ATOM   3774 C  CA  . LEU D 1 107 ? 13.104  9.388   15.241  1.00 25.62 ? 106  LEU D CA  1 
ATOM   3775 C  C   . LEU D 1 107 ? 12.352  9.334   16.576  1.00 26.71 ? 106  LEU D C   1 
ATOM   3776 O  O   . LEU D 1 107 ? 12.688  10.021  17.535  1.00 28.15 ? 106  LEU D O   1 
ATOM   3777 C  CB  . LEU D 1 107 ? 13.390  10.838  14.777  1.00 25.37 ? 106  LEU D CB  1 
ATOM   3778 C  CG  . LEU D 1 107 ? 14.226  10.932  13.481  1.00 23.18 ? 106  LEU D CG  1 
ATOM   3779 C  CD1 . LEU D 1 107 ? 14.602  12.364  13.138  1.00 22.49 ? 106  LEU D CD1 1 
ATOM   3780 C  CD2 . LEU D 1 107 ? 15.498  10.085  13.607  1.00 23.22 ? 106  LEU D CD2 1 
ATOM   3781 N  N   . SER D 1 108 ? 11.319  8.515   16.656  1.00 27.36 ? 107  SER D N   1 
ATOM   3782 C  CA  . SER D 1 108 ? 10.624  8.342   17.934  1.00 28.11 ? 107  SER D CA  1 
ATOM   3783 C  C   . SER D 1 108 ? 9.968   6.991   17.938  1.00 28.29 ? 107  SER D C   1 
ATOM   3784 O  O   . SER D 1 108 ? 9.881   6.360   16.904  1.00 29.72 ? 107  SER D O   1 
ATOM   3785 C  CB  . SER D 1 108 ? 9.555   9.434   18.185  1.00 27.93 ? 107  SER D CB  1 
ATOM   3786 O  OG  . SER D 1 108 ? 8.466   9.343   17.271  1.00 29.84 ? 107  SER D OG  1 
ATOM   3787 N  N   . GLY D 1 109 ? 9.512   6.565   19.108  1.00 28.76 ? 108  GLY D N   1 
ATOM   3788 C  CA  . GLY D 1 109 ? 8.766   5.334   19.282  1.00 27.78 ? 108  GLY D CA  1 
ATOM   3789 C  C   . GLY D 1 109 ? 9.466   4.015   19.007  1.00 27.46 ? 108  GLY D C   1 
ATOM   3790 O  O   . GLY D 1 109 ? 10.676  3.885   19.072  1.00 27.99 ? 108  GLY D O   1 
ATOM   3791 N  N   . ASP D 1 110 ? 8.629   3.041   18.704  1.00 26.83 ? 109  ASP D N   1 
ATOM   3792 C  CA  . ASP D 1 110 ? 8.969   1.649   18.424  1.00 26.43 ? 109  ASP D CA  1 
ATOM   3793 C  C   . ASP D 1 110 ? 10.157  1.488   17.497  1.00 24.64 ? 109  ASP D C   1 
ATOM   3794 O  O   . ASP D 1 110 ? 11.045  0.691   17.768  1.00 24.41 ? 109  ASP D O   1 
ATOM   3795 C  CB  . ASP D 1 110 ? 7.737   1.032   17.774  1.00 26.67 ? 109  ASP D CB  1 
ATOM   3796 C  CG  . ASP D 1 110 ? 7.854   -0.445  17.558  1.00 31.10 ? 109  ASP D CG  1 
ATOM   3797 O  OD1 . ASP D 1 110 ? 8.383   -1.134  18.468  1.00 36.65 ? 109  ASP D OD1 1 
ATOM   3798 O  OD2 . ASP D 1 110 ? 7.403   -1.013  16.530  1.00 34.82 ? 109  ASP D OD2 1 
ATOM   3799 N  N   . HIS D 1 111 ? 10.159  2.237   16.399  1.00 24.11 ? 110  HIS D N   1 
ATOM   3800 C  CA  . HIS D 1 111 ? 11.198  2.127   15.400  1.00 23.10 ? 110  HIS D CA  1 
ATOM   3801 C  C   . HIS D 1 111 ? 12.292  3.211   15.533  1.00 22.99 ? 110  HIS D C   1 
ATOM   3802 O  O   . HIS D 1 111 ? 13.041  3.466   14.571  1.00 24.46 ? 110  HIS D O   1 
ATOM   3803 C  CB  . HIS D 1 111 ? 10.561  2.201   14.010  1.00 22.51 ? 110  HIS D CB  1 
ATOM   3804 C  CG  . HIS D 1 111 ? 9.731   1.015   13.634  1.00 22.81 ? 110  HIS D CG  1 
ATOM   3805 N  ND1 . HIS D 1 111 ? 9.156   0.894   12.390  1.00 24.43 ? 110  HIS D ND1 1 
ATOM   3806 C  CD2 . HIS D 1 111 ? 9.391   -0.108  14.314  1.00 20.14 ? 110  HIS D CD2 1 
ATOM   3807 C  CE1 . HIS D 1 111 ? 8.512   -0.256  12.310  1.00 22.63 ? 110  HIS D CE1 1 
ATOM   3808 N  NE2 . HIS D 1 111 ? 8.635   -0.877  13.468  1.00 25.97 ? 110  HIS D NE2 1 
ATOM   3809 N  N   . CYS D 1 112 ? 12.398  3.835   16.711  1.00 23.52 ? 111  CYS D N   1 
ATOM   3810 C  CA  . CYS D 1 112 ? 13.382  4.898   16.955  1.00 23.01 ? 111  CYS D CA  1 
ATOM   3811 C  C   . CYS D 1 112 ? 14.822  4.471   16.660  1.00 21.45 ? 111  CYS D C   1 
ATOM   3812 O  O   . CYS D 1 112 ? 15.281  3.411   17.086  1.00 24.45 ? 111  CYS D O   1 
ATOM   3813 C  CB  . CYS D 1 112 ? 13.264  5.483   18.366  1.00 21.97 ? 111  CYS D CB  1 
ATOM   3814 S  SG  . CYS D 1 112 ? 14.190  7.040   18.602  1.00 28.21 ? 111  CYS D SG  1 
ATOM   3815 N  N   . ILE D 1 113 ? 15.554  5.323   15.971  1.00 23.04 ? 112  ILE D N   1 
ATOM   3816 C  CA  . ILE D 1 113 ? 16.919  4.974   15.584  1.00 21.70 ? 112  ILE D CA  1 
ATOM   3817 C  C   . ILE D 1 113 ? 17.962  5.810   16.283  1.00 22.13 ? 112  ILE D C   1 
ATOM   3818 O  O   . ILE D 1 113 ? 19.148  5.597   16.112  1.00 22.90 ? 112  ILE D O   1 
ATOM   3819 C  CB  . ILE D 1 113 ? 17.089  4.955   14.061  1.00 19.35 ? 112  ILE D CB  1 
ATOM   3820 C  CG1 . ILE D 1 113 ? 17.007  6.395   13.462  1.00 14.51 ? 112  ILE D CG1 1 
ATOM   3821 C  CG2 . ILE D 1 113 ? 16.106  3.990   13.402  1.00 17.80 ? 112  ILE D CG2 1 
ATOM   3822 C  CD1 . ILE D 1 113 ? 17.424  6.392   12.045  1.00 19.70 ? 112  ILE D CD1 1 
ATOM   3823 N  N   . ILE D 1 114 ? 17.506  6.798   17.055  1.00 24.20 ? 113  ILE D N   1 
ATOM   3824 C  CA  . ILE D 1 114 ? 18.408  7.578   17.873  1.00 23.93 ? 113  ILE D CA  1 
ATOM   3825 C  C   . ILE D 1 114 ? 19.051  6.724   18.988  1.00 22.37 ? 113  ILE D C   1 
ATOM   3826 O  O   . ILE D 1 114 ? 18.352  6.088   19.812  1.00 25.14 ? 113  ILE D O   1 
ATOM   3827 C  CB  . ILE D 1 114 ? 17.615  8.757   18.481  1.00 22.84 ? 113  ILE D CB  1 
ATOM   3828 C  CG1 . ILE D 1 114 ? 17.291  9.757   17.367  1.00 25.55 ? 113  ILE D CG1 1 
ATOM   3829 C  CG2 . ILE D 1 114 ? 18.369  9.363   19.670  1.00 23.88 ? 113  ILE D CG2 1 
ATOM   3830 C  CD1 . ILE D 1 114 ? 16.017  10.449  17.580  1.00 20.95 ? 113  ILE D CD1 1 
ATOM   3831 N  N   . GLY D 1 115 ? 20.395  6.689   18.988  1.00 23.41 ? 114  GLY D N   1 
ATOM   3832 C  CA  . GLY D 1 115 ? 21.168  5.992   19.998  1.00 22.35 ? 114  GLY D CA  1 
ATOM   3833 C  C   . GLY D 1 115 ? 21.570  4.653   19.437  1.00 20.29 ? 114  GLY D C   1 
ATOM   3834 O  O   . GLY D 1 115 ? 22.167  3.806   20.108  1.00 22.28 ? 114  GLY D O   1 
ATOM   3835 N  N   . ARG D 1 116 ? 21.194  4.427   18.189  1.00 22.52 ? 115  ARG D N   1 
ATOM   3836 C  CA  . ARG D 1 116 ? 21.667  3.257   17.499  1.00 21.22 ? 115  ARG D CA  1 
ATOM   3837 C  C   . ARG D 1 116 ? 22.829  3.786   16.598  1.00 21.97 ? 115  ARG D C   1 
ATOM   3838 O  O   . ARG D 1 116 ? 23.178  5.018   16.626  1.00 24.87 ? 115  ARG D O   1 
ATOM   3839 C  CB  . ARG D 1 116 ? 20.489  2.600   16.782  1.00 19.51 ? 115  ARG D CB  1 
ATOM   3840 C  CG  . ARG D 1 116 ? 19.373  2.199   17.812  1.00 18.19 ? 115  ARG D CG  1 
ATOM   3841 C  CD  . ARG D 1 116 ? 18.243  1.257   17.300  1.00 18.60 ? 115  ARG D CD  1 
ATOM   3842 N  NE  . ARG D 1 116 ? 17.152  1.203   18.278  1.00 20.71 ? 115  ARG D NE  1 
ATOM   3843 C  CZ  . ARG D 1 116 ? 17.067  0.312   19.275  1.00 16.73 ? 115  ARG D CZ  1 
ATOM   3844 N  NH1 . ARG D 1 116 ? 18.015  -0.580  19.439  1.00 20.75 ? 115  ARG D NH1 1 
ATOM   3845 N  NH2 . ARG D 1 116 ? 16.054  0.326   20.128  1.00 17.87 ? 115  ARG D NH2 1 
ATOM   3846 N  N   . THR D 1 117 ? 23.453  2.873   15.874  1.00 21.86 ? 116  THR D N   1 
ATOM   3847 C  CA  . THR D 1 117 ? 24.592  3.085   15.005  1.00 20.95 ? 116  THR D CA  1 
ATOM   3848 C  C   . THR D 1 117 ? 24.231  2.997   13.482  1.00 20.14 ? 116  THR D C   1 
ATOM   3849 O  O   . THR D 1 117 ? 23.644  2.007   12.942  1.00 24.03 ? 116  THR D O   1 
ATOM   3850 C  CB  . THR D 1 117 ? 25.718  2.055   15.386  1.00 17.94 ? 116  THR D CB  1 
ATOM   3851 O  OG1 . THR D 1 117 ? 26.268  2.334   16.667  1.00 21.29 ? 116  THR D OG1 1 
ATOM   3852 C  CG2 . THR D 1 117 ? 26.936  2.090   14.403  1.00 17.90 ? 116  THR D CG2 1 
ATOM   3853 N  N   . LEU D 1 118 ? 24.586  4.049   12.772  1.00 21.42 ? 117  LEU D N   1 
ATOM   3854 C  CA  . LEU D 1 118 ? 24.528  4.031   11.331  1.00 21.29 ? 117  LEU D CA  1 
ATOM   3855 C  C   . LEU D 1 118 ? 25.888  3.531   10.840  1.00 22.23 ? 117  LEU D C   1 
ATOM   3856 O  O   . LEU D 1 118 ? 26.938  4.028   11.314  1.00 24.46 ? 117  LEU D O   1 
ATOM   3857 C  CB  . LEU D 1 118 ? 24.295  5.458   10.810  1.00 19.34 ? 117  LEU D CB  1 
ATOM   3858 C  CG  . LEU D 1 118 ? 24.159  5.505   9.266   1.00 18.04 ? 117  LEU D CG  1 
ATOM   3859 C  CD1 . LEU D 1 118 ? 22.899  4.745   8.729   1.00 21.84 ? 117  LEU D CD1 1 
ATOM   3860 C  CD2 . LEU D 1 118 ? 24.136  6.960   8.804   1.00 20.42 ? 117  LEU D CD2 1 
ATOM   3861 N  N   . VAL D 1 119 ? 25.855  2.558   9.922   1.00 21.19 ? 118  VAL D N   1 
ATOM   3862 C  CA  . VAL D 1 119 ? 27.017  1.871   9.298   1.00 19.98 ? 118  VAL D CA  1 
ATOM   3863 C  C   . VAL D 1 119 ? 27.010  1.816   7.747   1.00 18.79 ? 118  VAL D C   1 
ATOM   3864 O  O   . VAL D 1 119 ? 25.994  1.586   7.100   1.00 22.61 ? 118  VAL D O   1 
ATOM   3865 C  CB  . VAL D 1 119 ? 27.100  0.353   9.746   1.00 17.19 ? 118  VAL D CB  1 
ATOM   3866 C  CG1 . VAL D 1 119 ? 28.370  -0.305  9.109   1.00 19.69 ? 118  VAL D CG1 1 
ATOM   3867 C  CG2 . VAL D 1 119 ? 26.995  0.137   11.271  1.00 16.57 ? 118  VAL D CG2 1 
ATOM   3868 N  N   . VAL D 1 120 ? 28.154  2.026   7.138   1.00 20.48 ? 119  VAL D N   1 
ATOM   3869 C  CA  . VAL D 1 120 ? 28.331  1.940   5.715   1.00 21.54 ? 119  VAL D CA  1 
ATOM   3870 C  C   . VAL D 1 120 ? 29.275  0.751   5.451   1.00 21.22 ? 119  VAL D C   1 
ATOM   3871 O  O   . VAL D 1 120 ? 30.421  0.679   5.948   1.00 23.23 ? 119  VAL D O   1 
ATOM   3872 C  CB  . VAL D 1 120 ? 28.839  3.269   5.164   1.00 20.59 ? 119  VAL D CB  1 
ATOM   3873 C  CG1 . VAL D 1 120 ? 30.189  3.568   5.730   1.00 20.83 ? 119  VAL D CG1 1 
ATOM   3874 C  CG2 . VAL D 1 120 ? 28.843  3.257   3.638   1.00 24.14 ? 119  VAL D CG2 1 
ATOM   3875 N  N   . HIS D 1 121 ? 28.758  -0.218  4.708   1.00 23.44 ? 120  HIS D N   1 
ATOM   3876 C  CA  . HIS D 1 121 ? 29.447  -1.484  4.512   1.00 22.94 ? 120  HIS D CA  1 
ATOM   3877 C  C   . HIS D 1 121 ? 30.329  -1.578  3.297   1.00 22.85 ? 120  HIS D C   1 
ATOM   3878 O  O   . HIS D 1 121 ? 30.131  -0.870  2.322   1.00 23.87 ? 120  HIS D O   1 
ATOM   3879 C  CB  . HIS D 1 121 ? 28.427  -2.599  4.440   1.00 22.34 ? 120  HIS D CB  1 
ATOM   3880 C  CG  . HIS D 1 121 ? 27.783  -2.912  5.753   1.00 21.17 ? 120  HIS D CG  1 
ATOM   3881 N  ND1 . HIS D 1 121 ? 27.937  -4.130  6.386   1.00 22.71 ? 120  HIS D ND1 1 
ATOM   3882 C  CD2 . HIS D 1 121 ? 26.960  -2.180  6.536   1.00 18.50 ? 120  HIS D CD2 1 
ATOM   3883 C  CE1 . HIS D 1 121 ? 27.253  -4.125  7.516   1.00 19.53 ? 120  HIS D CE1 1 
ATOM   3884 N  NE2 . HIS D 1 121 ? 26.638  -2.953  7.624   1.00 21.69 ? 120  HIS D NE2 1 
ATOM   3885 N  N   . GLU D 1 122 ? 31.271  -2.516  3.347   1.00 24.36 ? 121  GLU D N   1 
ATOM   3886 C  CA  . GLU D 1 122 ? 32.192  -2.768  2.243   1.00 23.75 ? 121  GLU D CA  1 
ATOM   3887 C  C   . GLU D 1 122 ? 31.471  -3.108  0.938   1.00 24.44 ? 121  GLU D C   1 
ATOM   3888 O  O   . GLU D 1 122 ? 31.639  -2.420  -0.062  1.00 25.02 ? 121  GLU D O   1 
ATOM   3889 C  CB  . GLU D 1 122 ? 33.198  -3.874  2.612   1.00 24.27 ? 121  GLU D CB  1 
ATOM   3890 C  CG  . GLU D 1 122 ? 34.379  -3.990  1.660   1.00 24.18 ? 121  GLU D CG  1 
ATOM   3891 C  CD  . GLU D 1 122 ? 35.060  -5.347  1.716   1.00 27.81 ? 121  GLU D CD  1 
ATOM   3892 O  OE1 . GLU D 1 122 ? 34.946  -6.060  2.754   1.00 29.73 ? 121  GLU D OE1 1 
ATOM   3893 O  OE2 . GLU D 1 122 ? 35.726  -5.706  0.718   1.00 30.48 ? 121  GLU D OE2 1 
ATOM   3894 N  N   . LYS D 1 123 ? 30.656  -4.154  0.942   1.00 25.26 ? 122  LYS D N   1 
ATOM   3895 C  CA  . LYS D 1 123 ? 29.959  -4.566  -0.270  1.00 25.97 ? 122  LYS D CA  1 
ATOM   3896 C  C   . LYS D 1 123 ? 28.578  -3.946  -0.407  1.00 26.97 ? 122  LYS D C   1 
ATOM   3897 O  O   . LYS D 1 123 ? 28.028  -3.388  0.553   1.00 26.96 ? 122  LYS D O   1 
ATOM   3898 C  CB  . LYS D 1 123 ? 29.820  -6.085  -0.311  1.00 25.73 ? 122  LYS D CB  1 
ATOM   3899 C  CG  . LYS D 1 123 ? 31.149  -6.816  -0.189  1.00 26.17 ? 122  LYS D CG  1 
ATOM   3900 C  CD  . LYS D 1 123 ? 31.115  -8.216  -0.797  1.00 27.55 ? 122  LYS D CD  1 
ATOM   3901 C  CE  . LYS D 1 123 ? 32.417  -8.970  -0.517  1.00 28.90 ? 122  LYS D CE  1 
ATOM   3902 N  NZ  . LYS D 1 123 ? 32.303  -10.473 -0.735  1.00 29.69 ? 122  LYS D NZ  1 
ATOM   3903 N  N   . ALA D 1 124 ? 28.030  -4.056  -1.617  1.00 28.00 ? 123  ALA D N   1 
ATOM   3904 C  CA  . ALA D 1 124 ? 26.663  -3.642  -1.914  1.00 28.28 ? 123  ALA D CA  1 
ATOM   3905 C  C   . ALA D 1 124 ? 25.708  -4.493  -1.085  1.00 28.92 ? 123  ALA D C   1 
ATOM   3906 O  O   . ALA D 1 124 ? 26.025  -5.643  -0.737  1.00 29.63 ? 123  ALA D O   1 
ATOM   3907 C  CB  . ALA D 1 124 ? 26.377  -3.836  -3.401  1.00 27.27 ? 123  ALA D CB  1 
ATOM   3908 N  N   . ASP D 1 125 ? 24.541  -3.939  -0.775  1.00 28.99 ? 124  ASP D N   1 
ATOM   3909 C  CA  . ASP D 1 125 ? 23.533  -4.650  0.007   1.00 29.36 ? 124  ASP D CA  1 
ATOM   3910 C  C   . ASP D 1 125 ? 23.308  -6.098  -0.447  1.00 28.97 ? 124  ASP D C   1 
ATOM   3911 O  O   . ASP D 1 125 ? 23.138  -6.396  -1.645  1.00 30.16 ? 124  ASP D O   1 
ATOM   3912 C  CB  . ASP D 1 125 ? 22.212  -3.877  -0.002  1.00 29.72 ? 124  ASP D CB  1 
ATOM   3913 C  CG  . ASP D 1 125 ? 21.434  -4.023  1.304   1.00 30.81 ? 124  ASP D CG  1 
ATOM   3914 O  OD1 . ASP D 1 125 ? 22.054  -4.448  2.298   1.00 34.30 ? 124  ASP D OD1 1 
ATOM   3915 O  OD2 . ASP D 1 125 ? 20.207  -3.745  1.430   1.00 31.97 ? 124  ASP D OD2 1 
ATOM   3916 N  N   . SER D 1 143 ? 32.514  -6.078  5.097   1.00 27.46 ? 142  SER D N   1 
ATOM   3917 C  CA  . SER D 1 143 ? 33.012  -5.563  6.371   1.00 27.40 ? 142  SER D CA  1 
ATOM   3918 C  C   . SER D 1 143 ? 32.465  -4.144  6.663   1.00 27.19 ? 142  SER D C   1 
ATOM   3919 O  O   . SER D 1 143 ? 31.802  -3.537  5.822   1.00 27.07 ? 142  SER D O   1 
ATOM   3920 C  CB  . SER D 1 143 ? 34.541  -5.594  6.428   1.00 27.54 ? 142  SER D CB  1 
ATOM   3921 O  OG  . SER D 1 143 ? 35.110  -4.436  5.846   1.00 30.27 ? 142  SER D OG  1 
ATOM   3922 N  N   . ARG D 1 144 ? 32.732  -3.625  7.855   1.00 27.28 ? 143  ARG D N   1 
ATOM   3923 C  CA  . ARG D 1 144 ? 32.155  -2.330  8.229   1.00 26.36 ? 143  ARG D CA  1 
ATOM   3924 C  C   . ARG D 1 144 ? 33.181  -1.241  8.074   1.00 26.23 ? 143  ARG D C   1 
ATOM   3925 O  O   . ARG D 1 144 ? 34.128  -1.140  8.856   1.00 27.96 ? 143  ARG D O   1 
ATOM   3926 C  CB  . ARG D 1 144 ? 31.582  -2.388  9.650   1.00 26.23 ? 143  ARG D CB  1 
ATOM   3927 C  CG  . ARG D 1 144 ? 30.418  -3.371  9.768   1.00 26.03 ? 143  ARG D CG  1 
ATOM   3928 C  CD  . ARG D 1 144 ? 30.041  -3.775  11.211  1.00 24.61 ? 143  ARG D CD  1 
ATOM   3929 N  NE  . ARG D 1 144 ? 28.991  -4.790  11.197  1.00 25.66 ? 143  ARG D NE  1 
ATOM   3930 C  CZ  . ARG D 1 144 ? 28.229  -5.111  12.239  1.00 25.01 ? 143  ARG D CZ  1 
ATOM   3931 N  NH1 . ARG D 1 144 ? 28.390  -4.502  13.408  1.00 28.65 ? 143  ARG D NH1 1 
ATOM   3932 N  NH2 . ARG D 1 144 ? 27.294  -6.061  12.114  1.00 28.57 ? 143  ARG D NH2 1 
ATOM   3933 N  N   . LEU D 1 145 ? 32.977  -0.418  7.064   1.00 26.24 ? 144  LEU D N   1 
ATOM   3934 C  CA  . LEU D 1 145 ? 33.934  0.614   6.708   1.00 25.11 ? 144  LEU D CA  1 
ATOM   3935 C  C   . LEU D 1 145 ? 33.961  1.816   7.630   1.00 25.15 ? 144  LEU D C   1 
ATOM   3936 O  O   . LEU D 1 145 ? 35.049  2.311   7.937   1.00 25.72 ? 144  LEU D O   1 
ATOM   3937 C  CB  . LEU D 1 145 ? 33.717  1.032   5.260   1.00 24.39 ? 144  LEU D CB  1 
ATOM   3938 C  CG  . LEU D 1 145 ? 34.012  -0.127  4.295   1.00 24.06 ? 144  LEU D CG  1 
ATOM   3939 C  CD1 . LEU D 1 145 ? 33.453  0.190   2.917   1.00 21.22 ? 144  LEU D CD1 1 
ATOM   3940 C  CD2 . LEU D 1 145 ? 35.500  -0.453  4.232   1.00 24.42 ? 144  LEU D CD2 1 
ATOM   3941 N  N   . ALA D 1 146 ? 32.779  2.281   8.041   1.00 24.38 ? 145  ALA D N   1 
ATOM   3942 C  CA  . ALA D 1 146 ? 32.639  3.380   8.987   1.00 22.98 ? 145  ALA D CA  1 
ATOM   3943 C  C   . ALA D 1 146 ? 31.254  3.303   9.610   1.00 21.75 ? 145  ALA D C   1 
ATOM   3944 O  O   . ALA D 1 146 ? 30.318  2.739   8.997   1.00 23.21 ? 145  ALA D O   1 
ATOM   3945 C  CB  . ALA D 1 146 ? 32.846  4.765   8.301   1.00 20.81 ? 145  ALA D CB  1 
ATOM   3946 N  N   . CYS D 1 147 ? 31.151  3.901   10.791  1.00 22.03 ? 146  CYS D N   1 
ATOM   3947 C  CA  . CYS D 1 147 ? 29.932  4.029   11.559  1.00 23.29 ? 146  CYS D CA  1 
ATOM   3948 C  C   . CYS D 1 147 ? 29.966  5.198   12.518  1.00 21.13 ? 146  CYS D C   1 
ATOM   3949 O  O   . CYS D 1 147 ? 31.030  5.822   12.751  1.00 23.94 ? 146  CYS D O   1 
ATOM   3950 C  CB  . CYS D 1 147 ? 29.691  2.762   12.393  1.00 20.36 ? 146  CYS D CB  1 
ATOM   3951 S  SG  . CYS D 1 147 ? 31.035  2.376   13.510  1.00 28.20 ? 146  CYS D SG  1 
ATOM   3952 N  N   . GLY D 1 148 ? 28.815  5.415   13.160  1.00 21.85 ? 147  GLY D N   1 
ATOM   3953 C  CA  . GLY D 1 148 ? 28.647  6.427   14.191  1.00 19.77 ? 147  GLY D CA  1 
ATOM   3954 C  C   . GLY D 1 148 ? 27.325  6.226   14.884  1.00 19.76 ? 147  GLY D C   1 
ATOM   3955 O  O   . GLY D 1 148 ? 26.402  5.543   14.334  1.00 22.37 ? 147  GLY D O   1 
ATOM   3956 N  N   . VAL D 1 149 ? 27.222  6.785   16.091  1.00 21.07 ? 148  VAL D N   1 
ATOM   3957 C  CA  . VAL D 1 149 ? 26.002  6.679   16.866  1.00 19.47 ? 148  VAL D CA  1 
ATOM   3958 C  C   . VAL D 1 149 ? 25.124  7.817   16.317  1.00 19.58 ? 148  VAL D C   1 
ATOM   3959 O  O   . VAL D 1 149 ? 25.599  8.944   16.092  1.00 24.72 ? 148  VAL D O   1 
ATOM   3960 C  CB  . VAL D 1 149 ? 26.247  6.765   18.412  1.00 18.42 ? 148  VAL D CB  1 
ATOM   3961 C  CG1 . VAL D 1 149 ? 24.964  6.632   19.284  1.00 17.12 ? 148  VAL D CG1 1 
ATOM   3962 C  CG2 . VAL D 1 149 ? 27.408  5.821   18.973  1.00 20.66 ? 148  VAL D CG2 1 
ATOM   3963 N  N   . ILE D 1 150 ? 23.840  7.560   16.207  1.00 20.71 ? 149  ILE D N   1 
ATOM   3964 C  CA  . ILE D 1 150 ? 22.882  8.533   15.738  1.00 20.96 ? 149  ILE D CA  1 
ATOM   3965 C  C   . ILE D 1 150 ? 22.421  9.377   16.946  1.00 19.08 ? 149  ILE D C   1 
ATOM   3966 O  O   . ILE D 1 150 ? 21.734  8.898   17.863  1.00 22.24 ? 149  ILE D O   1 
ATOM   3967 C  CB  . ILE D 1 150 ? 21.728  7.769   15.019  1.00 17.70 ? 149  ILE D CB  1 
ATOM   3968 C  CG1 . ILE D 1 150 ? 22.211  6.989   13.781  1.00 22.37 ? 149  ILE D CG1 1 
ATOM   3969 C  CG2 . ILE D 1 150 ? 20.588  8.677   14.536  1.00 18.50 ? 149  ILE D CG2 1 
ATOM   3970 C  CD1 . ILE D 1 150 ? 21.247  5.915   13.415  1.00 23.67 ? 149  ILE D CD1 1 
ATOM   3971 N  N   . GLY D 1 151 ? 22.773  10.654  16.941  1.00 19.44 ? 150  GLY D N   1 
ATOM   3972 C  CA  . GLY D 1 151 ? 22.507  11.535  18.080  1.00 18.76 ? 150  GLY D CA  1 
ATOM   3973 C  C   . GLY D 1 151 ? 21.440  12.574  17.745  1.00 19.28 ? 150  GLY D C   1 
ATOM   3974 O  O   . GLY D 1 151 ? 21.160  12.783  16.591  1.00 21.40 ? 150  GLY D O   1 
ATOM   3975 N  N   . ILE D 1 152 ? 20.794  13.097  18.777  1.00 22.38 ? 151  ILE D N   1 
ATOM   3976 C  CA  . ILE D 1 152 ? 19.773  14.136  18.643  1.00 22.16 ? 151  ILE D CA  1 
ATOM   3977 C  C   . ILE D 1 152 ? 20.436  15.404  18.148  1.00 22.89 ? 151  ILE D C   1 
ATOM   3978 O  O   . ILE D 1 152 ? 21.513  15.755  18.614  1.00 23.93 ? 151  ILE D O   1 
ATOM   3979 C  CB  . ILE D 1 152 ? 19.073  14.357  19.955  1.00 21.69 ? 151  ILE D CB  1 
ATOM   3980 C  CG1 . ILE D 1 152 ? 18.376  13.069  20.354  1.00 20.92 ? 151  ILE D CG1 1 
ATOM   3981 C  CG2 . ILE D 1 152 ? 18.032  15.487  19.818  1.00 22.69 ? 151  ILE D CG2 1 
ATOM   3982 C  CD1 . ILE D 1 152 ? 18.050  13.033  21.802  1.00 20.68 ? 151  ILE D CD1 1 
ATOM   3983 N  N   . ALA D 1 153 ? 19.836  16.011  17.134  1.00 24.37 ? 152  ALA D N   1 
ATOM   3984 C  CA  . ALA D 1 153 ? 20.357  17.231  16.516  1.00 25.28 ? 152  ALA D CA  1 
ATOM   3985 C  C   . ALA D 1 153 ? 19.446  18.426  16.727  1.00 26.60 ? 152  ALA D C   1 
ATOM   3986 O  O   . ALA D 1 153 ? 18.245  18.270  17.002  1.00 27.42 ? 152  ALA D O   1 
ATOM   3987 C  CB  . ALA D 1 153 ? 20.631  16.993  15.034  1.00 25.51 ? 152  ALA D CB  1 
ATOM   3988 N  N   . GLN D 1 154 ? 20.035  19.622  16.649  1.00 27.93 ? 153  GLN D N   1 
ATOM   3989 C  CA  . GLN D 1 154 ? 19.308  20.866  16.805  1.00 28.94 ? 153  GLN D CA  1 
ATOM   3990 C  C   . GLN D 1 154 ? 18.584  21.169  15.505  1.00 29.29 ? 153  GLN D C   1 
ATOM   3991 O  O   . GLN D 1 154 ? 19.171  21.188  14.399  1.00 29.79 ? 153  GLN D O   1 
ATOM   3992 C  CB  . GLN D 1 154 ? 20.243  22.023  17.173  1.00 29.04 ? 153  GLN D CB  1 
ATOM   3993 C  CG  . GLN D 1 154 ? 19.513  23.389  17.285  1.00 31.27 ? 153  GLN D CG  1 
ATOM   3994 C  CD  . GLN D 1 154 ? 20.367  24.480  17.920  1.00 33.30 ? 153  GLN D CD  1 
ATOM   3995 O  OE1 . GLN D 1 154 ? 21.604  24.398  17.891  1.00 36.03 ? 153  GLN D OE1 1 
ATOM   3996 N  NE2 . GLN D 1 154 ? 19.716  25.496  18.512  1.00 35.24 ? 153  GLN D NE2 1 
ATOM   3997 O  OXT . GLN D 1 154 ? 17.383  21.359  15.617  1.00 30.09 ? 153  GLN D OXT 1 
HETATM 3998 ZN ZN  . ZN  E 2 .   ? -12.175 3.581   14.317  0.20 32.34 ? 155  ZN  A ZN  1 
HETATM 3999 ZN ZN  . ZN  F 2 .   ? 1.055   -3.578  50.978  0.20 37.71 ? 155  ZN  B ZN  1 
HETATM 4000 O  O   . HOH G 3 .   ? -24.621 -3.248  34.986  1.00 52.88 ? 2001 HOH A O   1 
HETATM 4001 O  O   . HOH G 3 .   ? -28.393 0.132   26.631  1.00 53.24 ? 2002 HOH A O   1 
HETATM 4002 O  O   . HOH G 3 .   ? -12.834 -3.442  33.157  1.00 43.00 ? 2003 HOH A O   1 
HETATM 4003 O  O   . HOH G 3 .   ? -16.909 -1.387  33.695  1.00 61.11 ? 2004 HOH A O   1 
HETATM 4004 O  O   . HOH G 3 .   ? -28.078 0.389   34.774  1.00 65.73 ? 2005 HOH A O   1 
HETATM 4005 O  O   . HOH G 3 .   ? -25.124 3.055   28.739  1.00 49.71 ? 2006 HOH A O   1 
HETATM 4006 O  O   . HOH G 3 .   ? -28.301 -6.770  32.204  1.00 53.68 ? 2007 HOH A O   1 
HETATM 4007 O  O   . HOH G 3 .   ? -24.829 -2.064  32.108  1.00 49.58 ? 2008 HOH A O   1 
HETATM 4008 O  O   . HOH G 3 .   ? -26.259 -0.752  28.735  1.00 42.79 ? 2009 HOH A O   1 
HETATM 4009 O  O   . HOH G 3 .   ? -8.632  -12.624 31.095  1.00 53.41 ? 2010 HOH A O   1 
HETATM 4010 O  O   . HOH G 3 .   ? -19.043 4.597   37.959  1.00 58.68 ? 2011 HOH A O   1 
HETATM 4011 O  O   . HOH G 3 .   ? -19.504 11.172  22.649  1.00 58.36 ? 2012 HOH A O   1 
HETATM 4012 O  O   . HOH G 3 .   ? 0.506   -7.406  17.627  1.00 53.16 ? 2013 HOH A O   1 
HETATM 4013 O  O   . HOH G 3 .   ? -3.056  8.177   6.487   1.00 60.60 ? 2014 HOH A O   1 
HETATM 4014 O  O   . HOH G 3 .   ? -23.233 -13.442 28.370  1.00 71.27 ? 2015 HOH A O   1 
HETATM 4015 O  O   . HOH G 3 .   ? -11.611 -10.006 13.264  1.00 53.85 ? 2016 HOH A O   1 
HETATM 4016 O  O   . HOH G 3 .   ? -28.768 -11.318 32.716  1.00 51.96 ? 2017 HOH A O   1 
HETATM 4017 O  O   . HOH G 3 .   ? -29.008 -2.659  24.860  1.00 46.74 ? 2018 HOH A O   1 
HETATM 4018 O  O   . HOH G 3 .   ? -28.944 -12.706 28.764  1.00 57.92 ? 2019 HOH A O   1 
HETATM 4019 O  O   . HOH G 3 .   ? -28.475 -2.840  21.854  1.00 43.02 ? 2020 HOH A O   1 
HETATM 4020 O  O   . HOH G 3 .   ? -34.170 -9.171  16.776  1.00 65.10 ? 2021 HOH A O   1 
HETATM 4021 O  O   . HOH G 3 .   ? -33.317 -8.125  20.591  1.00 51.42 ? 2022 HOH A O   1 
HETATM 4022 O  O   . HOH G 3 .   ? -27.302 -5.759  12.470  1.00 51.49 ? 2023 HOH A O   1 
HETATM 4023 O  O   . HOH G 3 .   ? -27.800 -3.570  15.161  1.00 53.83 ? 2024 HOH A O   1 
HETATM 4024 O  O   . HOH G 3 .   ? -14.840 1.952   33.231  1.00 53.87 ? 2025 HOH A O   1 
HETATM 4025 O  O   . HOH G 3 .   ? -8.095  12.416  21.549  1.00 61.71 ? 2026 HOH A O   1 
HETATM 4026 O  O   . HOH G 3 .   ? -2.843  9.023   24.437  1.00 53.43 ? 2027 HOH A O   1 
HETATM 4027 O  O   . HOH G 3 .   ? -12.608 13.985  31.271  1.00 60.64 ? 2028 HOH A O   1 
HETATM 4028 O  O   . HOH G 3 .   ? -9.162  11.912  30.105  1.00 45.69 ? 2029 HOH A O   1 
HETATM 4029 O  O   . HOH G 3 .   ? -14.986 5.624   29.828  1.00 44.89 ? 2030 HOH A O   1 
HETATM 4030 O  O   . HOH G 3 .   ? -16.518 3.020   36.406  1.00 53.65 ? 2031 HOH A O   1 
HETATM 4031 O  O   . HOH G 3 .   ? -19.847 2.548   34.285  1.00 51.70 ? 2032 HOH A O   1 
HETATM 4032 O  O   . HOH G 3 .   ? -11.518 6.050   34.719  1.00 43.24 ? 2033 HOH A O   1 
HETATM 4033 O  O   . HOH G 3 .   ? -22.007 5.713   30.151  1.00 42.18 ? 2034 HOH A O   1 
HETATM 4034 O  O   . HOH G 3 .   ? -16.551 11.496  23.731  1.00 57.58 ? 2035 HOH A O   1 
HETATM 4035 O  O   . HOH G 3 .   ? -20.809 9.139   24.364  1.00 55.10 ? 2036 HOH A O   1 
HETATM 4036 O  O   . HOH G 3 .   ? -17.657 4.685   17.178  1.00 55.43 ? 2037 HOH A O   1 
HETATM 4037 O  O   . HOH G 3 .   ? -16.992 6.763   18.614  1.00 51.92 ? 2038 HOH A O   1 
HETATM 4038 O  O   . HOH G 3 .   ? -9.379  9.440   14.927  1.00 51.78 ? 2039 HOH A O   1 
HETATM 4039 O  O   . HOH G 3 .   ? -4.143  4.492   14.278  1.00 47.96 ? 2040 HOH A O   1 
HETATM 4040 O  O   . HOH G 3 .   ? -5.826  7.943   19.400  1.00 51.60 ? 2041 HOH A O   1 
HETATM 4041 O  O   . HOH G 3 .   ? -2.174  0.635   11.607  1.00 52.93 ? 2042 HOH A O   1 
HETATM 4042 O  O   . HOH G 3 .   ? -13.553 -1.735  12.930  1.00 49.16 ? 2043 HOH A O   1 
HETATM 4043 O  O   . HOH G 3 .   ? -12.622 -6.048  8.307   1.00 45.69 ? 2044 HOH A O   1 
HETATM 4044 O  O   . HOH G 3 .   ? -4.884  -4.901  9.235   1.00 60.49 ? 2045 HOH A O   1 
HETATM 4045 O  O   . HOH G 3 .   ? -14.148 -2.139  5.031   1.00 57.48 ? 2046 HOH A O   1 
HETATM 4046 O  O   . HOH G 3 .   ? -3.245  -2.176  9.449   1.00 57.29 ? 2047 HOH A O   1 
HETATM 4047 O  O   . HOH G 3 .   ? -7.771  -3.765  2.839   1.00 55.56 ? 2048 HOH A O   1 
HETATM 4048 O  O   . HOH G 3 .   ? -5.494  8.646   5.750   1.00 62.52 ? 2049 HOH A O   1 
HETATM 4049 O  O   . HOH G 3 .   ? -7.320  -0.757  3.457   1.00 56.26 ? 2050 HOH A O   1 
HETATM 4050 O  O   . HOH G 3 .   ? -3.538  2.132   12.735  1.00 50.01 ? 2051 HOH A O   1 
HETATM 4051 O  O   . HOH G 3 .   ? -10.621 8.798   11.420  1.00 54.91 ? 2052 HOH A O   1 
HETATM 4052 O  O   . HOH G 3 .   ? -14.435 -8.458  14.800  1.00 51.21 ? 2053 HOH A O   1 
HETATM 4053 O  O   . HOH G 3 .   ? -19.260 -10.529 14.363  1.00 62.46 ? 2054 HOH A O   1 
HETATM 4054 O  O   . HOH G 3 .   ? -16.297 -10.097 16.111  1.00 55.70 ? 2055 HOH A O   1 
HETATM 4055 O  O   . HOH G 3 .   ? -18.698 -7.015  10.309  1.00 49.44 ? 2056 HOH A O   1 
HETATM 4056 O  O   . HOH G 3 .   ? -15.988 -7.378  12.464  1.00 48.78 ? 2057 HOH A O   1 
HETATM 4057 O  O   . HOH G 3 .   ? -22.771 -14.146 18.889  1.00 56.39 ? 2058 HOH A O   1 
HETATM 4058 O  O   . HOH G 3 .   ? -19.852 -11.456 17.591  1.00 56.76 ? 2059 HOH A O   1 
HETATM 4059 O  O   . HOH G 3 .   ? -20.919 -13.840 15.586  1.00 69.97 ? 2060 HOH A O   1 
HETATM 4060 O  O   . HOH G 3 .   ? -29.298 -10.632 26.859  1.00 50.77 ? 2061 HOH A O   1 
HETATM 4061 O  O   . HOH G 3 .   ? -24.420 -15.665 20.758  1.00 58.55 ? 2062 HOH A O   1 
HETATM 4062 O  O   . HOH G 3 .   ? -16.577 -12.481 17.264  1.00 50.55 ? 2063 HOH A O   1 
HETATM 4063 O  O   . HOH G 3 .   ? -9.066  -8.843  14.036  1.00 51.79 ? 2064 HOH A O   1 
HETATM 4064 O  O   . HOH G 3 .   ? -4.551  -12.163 13.537  1.00 63.36 ? 2065 HOH A O   1 
HETATM 4065 O  O   . HOH G 3 .   ? 6.097   -0.216  19.872  1.00 62.79 ? 2066 HOH A O   1 
HETATM 4066 O  O   . HOH G 3 .   ? 5.331   4.866   19.716  1.00 66.50 ? 2067 HOH A O   1 
HETATM 4067 O  O   . HOH G 3 .   ? 1.772   -3.348  16.534  1.00 64.89 ? 2068 HOH A O   1 
HETATM 4068 O  O   . HOH G 3 .   ? 2.541   -2.161  20.081  1.00 48.90 ? 2069 HOH A O   1 
HETATM 4069 O  O   . HOH G 3 .   ? 0.145   -2.277  12.662  1.00 58.82 ? 2070 HOH A O   1 
HETATM 4070 O  O   . HOH G 3 .   ? 0.366   0.038   29.739  1.00 71.07 ? 2071 HOH A O   1 
HETATM 4071 O  O   . HOH G 3 .   ? -0.980  7.682   25.024  1.00 53.83 ? 2072 HOH A O   1 
HETATM 4072 O  O   . HOH G 3 .   ? -0.145  2.641   23.892  1.00 46.84 ? 2073 HOH A O   1 
HETATM 4073 O  O   . HOH G 3 .   ? -14.345 3.640   30.585  1.00 47.12 ? 2074 HOH A O   1 
HETATM 4074 O  O   . HOH G 3 .   ? -27.157 -1.018  12.598  1.00 49.52 ? 2075 HOH A O   1 
HETATM 4075 O  O   . HOH G 3 .   ? -25.004 1.236   11.278  1.00 50.71 ? 2076 HOH A O   1 
HETATM 4076 O  O   . HOH G 3 .   ? -23.764 3.588   7.971   1.00 46.31 ? 2077 HOH A O   1 
HETATM 4077 O  O   . HOH G 3 .   ? -13.365 2.563   2.985   1.00 53.80 ? 2078 HOH A O   1 
HETATM 4078 O  O   . HOH G 3 .   ? -21.628 11.866  7.624   1.00 56.12 ? 2079 HOH A O   1 
HETATM 4079 O  O   . HOH G 3 .   ? -12.836 8.501   16.064  1.00 59.68 ? 2080 HOH A O   1 
HETATM 4080 O  O   . HOH G 3 .   ? -21.737 7.069   14.947  1.00 55.77 ? 2081 HOH A O   1 
HETATM 4081 O  O   . HOH G 3 .   ? -15.134 8.687   18.399  1.00 52.03 ? 2082 HOH A O   1 
HETATM 4082 O  O   . HOH G 3 .   ? -15.049 11.401  21.309  1.00 50.77 ? 2083 HOH A O   1 
HETATM 4083 O  O   . HOH G 3 .   ? -19.276 8.099   19.872  1.00 54.41 ? 2084 HOH A O   1 
HETATM 4084 O  O   . HOH G 3 .   ? -22.925 7.531   24.005  1.00 45.59 ? 2085 HOH A O   1 
HETATM 4085 O  O   . HOH G 3 .   ? -18.066 1.326   33.278  1.00 51.20 ? 2086 HOH A O   1 
HETATM 4086 O  O   . HOH G 3 .   ? -13.524 -0.214  33.976  1.00 41.37 ? 2087 HOH A O   1 
HETATM 4087 O  O   . HOH G 3 .   ? -0.497  -10.842 32.594  1.00 50.42 ? 2088 HOH A O   1 
HETATM 4088 O  O   . HOH G 3 .   ? -6.949  -11.726 36.660  1.00 53.70 ? 2089 HOH A O   1 
HETATM 4089 O  O   . HOH H 3 .   ? 3.357   15.207  32.498  1.00 72.12 ? 2001 HOH B O   1 
HETATM 4090 O  O   . HOH H 3 .   ? -1.306  10.578  29.624  1.00 47.34 ? 2002 HOH B O   1 
HETATM 4091 O  O   . HOH H 3 .   ? -19.671 0.401   53.294  1.00 57.12 ? 2003 HOH B O   1 
HETATM 4092 O  O   . HOH H 3 .   ? -15.317 1.747   38.732  1.00 57.98 ? 2004 HOH B O   1 
HETATM 4093 O  O   . HOH H 3 .   ? -10.034 17.026  42.127  1.00 61.38 ? 2005 HOH B O   1 
HETATM 4094 O  O   . HOH H 3 .   ? -17.605 -2.181  40.914  1.00 51.88 ? 2006 HOH B O   1 
HETATM 4095 O  O   . HOH H 3 .   ? -20.178 2.188   44.896  1.00 51.33 ? 2007 HOH B O   1 
HETATM 4096 O  O   . HOH H 3 .   ? -23.698 0.602   43.743  1.00 52.86 ? 2008 HOH B O   1 
HETATM 4097 O  O   . HOH H 3 .   ? -19.318 -1.339  51.446  1.00 64.98 ? 2009 HOH B O   1 
HETATM 4098 O  O   . HOH H 3 .   ? -18.162 -3.864  50.973  1.00 61.68 ? 2010 HOH B O   1 
HETATM 4099 O  O   . HOH H 3 .   ? -19.136 1.166   48.982  1.00 46.17 ? 2011 HOH B O   1 
HETATM 4100 O  O   . HOH H 3 .   ? -23.441 7.602   41.718  1.00 55.92 ? 2012 HOH B O   1 
HETATM 4101 O  O   . HOH H 3 .   ? -21.977 8.673   47.805  1.00 57.86 ? 2013 HOH B O   1 
HETATM 4102 O  O   . HOH H 3 .   ? -17.309 8.848   41.462  1.00 63.16 ? 2014 HOH B O   1 
HETATM 4103 O  O   . HOH H 3 .   ? -11.589 14.312  42.066  1.00 60.59 ? 2015 HOH B O   1 
HETATM 4104 O  O   . HOH H 3 .   ? -18.428 4.479   61.826  1.00 60.09 ? 2016 HOH B O   1 
HETATM 4105 O  O   . HOH H 3 .   ? -6.687  12.623  35.745  1.00 48.76 ? 2017 HOH B O   1 
HETATM 4106 O  O   . HOH H 3 .   ? -10.815 13.555  36.647  1.00 53.49 ? 2018 HOH B O   1 
HETATM 4107 O  O   . HOH H 3 .   ? 5.844   10.824  32.842  1.00 55.46 ? 2019 HOH B O   1 
HETATM 4108 O  O   . HOH H 3 .   ? 12.654  10.981  32.498  1.00 50.13 ? 2020 HOH B O   1 
HETATM 4109 O  O   . HOH H 3 .   ? 12.837  13.916  38.196  1.00 59.18 ? 2021 HOH B O   1 
HETATM 4110 O  O   . HOH H 3 .   ? 11.701  10.524  42.086  1.00 58.18 ? 2022 HOH B O   1 
HETATM 4111 O  O   . HOH H 3 .   ? 7.172   13.364  37.806  1.00 48.68 ? 2023 HOH B O   1 
HETATM 4112 O  O   . HOH H 3 .   ? 4.700   15.141  38.891  1.00 64.54 ? 2024 HOH B O   1 
HETATM 4113 O  O   . HOH H 3 .   ? -18.113 3.198   53.680  1.00 55.33 ? 2025 HOH B O   1 
HETATM 4114 O  O   . HOH H 3 .   ? -20.069 8.564   56.804  1.00 66.04 ? 2026 HOH B O   1 
HETATM 4115 O  O   . HOH H 3 .   ? -16.187 3.271   55.047  1.00 52.11 ? 2027 HOH B O   1 
HETATM 4116 O  O   . HOH H 3 .   ? -18.775 6.839   60.583  1.00 58.72 ? 2028 HOH B O   1 
HETATM 4117 O  O   . HOH H 3 .   ? -15.642 5.503   62.588  1.00 51.18 ? 2029 HOH B O   1 
HETATM 4118 O  O   . HOH H 3 .   ? 1.901   9.559   50.935  1.00 55.04 ? 2030 HOH B O   1 
HETATM 4119 O  O   . HOH H 3 .   ? -11.610 3.358   60.184  1.00 54.50 ? 2031 HOH B O   1 
HETATM 4120 O  O   . HOH H 3 .   ? -9.306  5.026   62.231  1.00 56.01 ? 2032 HOH B O   1 
HETATM 4121 O  O   . HOH H 3 .   ? -13.619 -1.668  38.046  1.00 60.71 ? 2033 HOH B O   1 
HETATM 4122 O  O   . HOH H 3 .   ? 1.601   -8.779  37.298  1.00 46.67 ? 2034 HOH B O   1 
HETATM 4123 O  O   . HOH H 3 .   ? -11.297 -5.079  40.677  1.00 44.00 ? 2035 HOH B O   1 
HETATM 4124 O  O   . HOH H 3 .   ? -18.863 -6.497  37.864  1.00 51.62 ? 2036 HOH B O   1 
HETATM 4125 O  O   . HOH H 3 .   ? -11.625 -5.665  34.746  1.00 45.26 ? 2037 HOH B O   1 
HETATM 4126 O  O   . HOH H 3 .   ? -5.585  -6.444  50.983  1.00 53.38 ? 2038 HOH B O   1 
HETATM 4127 O  O   . HOH H 3 .   ? -16.695 -5.264  45.120  1.00 48.32 ? 2039 HOH B O   1 
HETATM 4128 O  O   . HOH H 3 .   ? -5.904  -11.472 47.037  1.00 55.05 ? 2040 HOH B O   1 
HETATM 4129 O  O   . HOH H 3 .   ? -1.029  -8.581  49.507  1.00 49.46 ? 2041 HOH B O   1 
HETATM 4130 O  O   . HOH H 3 .   ? 7.303   -4.207  45.460  1.00 52.37 ? 2042 HOH B O   1 
HETATM 4131 O  O   . HOH H 3 .   ? 2.500   -9.587  48.320  1.00 51.76 ? 2043 HOH B O   1 
HETATM 4132 O  O   . HOH H 3 .   ? 2.478   -8.182  42.599  1.00 49.96 ? 2044 HOH B O   1 
HETATM 4133 O  O   . HOH H 3 .   ? 4.633   6.023   55.751  1.00 44.67 ? 2045 HOH B O   1 
HETATM 4134 O  O   . HOH H 3 .   ? 9.780   4.366   50.100  1.00 61.03 ? 2046 HOH B O   1 
HETATM 4135 O  O   . HOH H 3 .   ? 11.665  0.807   56.366  1.00 54.83 ? 2047 HOH B O   1 
HETATM 4136 O  O   . HOH H 3 .   ? 8.802   -2.396  46.611  1.00 48.94 ? 2048 HOH B O   1 
HETATM 4137 O  O   . HOH H 3 .   ? -1.257  7.269   57.870  1.00 62.31 ? 2049 HOH B O   1 
HETATM 4138 O  O   . HOH H 3 .   ? -0.510  7.306   54.901  1.00 50.98 ? 2050 HOH B O   1 
HETATM 4139 O  O   . HOH H 3 .   ? -2.723  10.348  53.042  1.00 62.45 ? 2051 HOH B O   1 
HETATM 4140 O  O   . HOH H 3 .   ? -6.707  11.907  53.212  1.00 61.32 ? 2052 HOH B O   1 
HETATM 4141 O  O   . HOH H 3 .   ? -5.278  11.455  59.624  1.00 66.01 ? 2053 HOH B O   1 
HETATM 4142 O  O   . HOH H 3 .   ? -21.495 17.547  60.223  1.00 56.68 ? 2054 HOH B O   1 
HETATM 4143 O  O   . HOH H 3 .   ? -19.710 10.654  52.992  1.00 51.94 ? 2055 HOH B O   1 
HETATM 4144 O  O   . HOH H 3 .   ? -22.460 12.251  55.142  1.00 50.68 ? 2056 HOH B O   1 
HETATM 4145 O  O   . HOH H 3 .   ? -21.482 9.347   53.665  0.50 45.23 ? 2057 HOH B O   1 
HETATM 4146 O  O   . HOH H 3 .   ? 0.647   13.949  51.163  1.00 57.91 ? 2058 HOH B O   1 
HETATM 4147 O  O   . HOH H 3 .   ? -0.652  16.136  44.838  1.00 56.37 ? 2059 HOH B O   1 
HETATM 4148 O  O   . HOH H 3 .   ? -4.231  12.550  51.473  1.00 59.02 ? 2060 HOH B O   1 
HETATM 4149 O  O   . HOH H 3 .   ? 2.290   11.967  50.469  1.00 57.03 ? 2061 HOH B O   1 
HETATM 4150 O  O   . HOH H 3 .   ? 1.414   17.266  46.021  1.00 57.28 ? 2062 HOH B O   1 
HETATM 4151 O  O   . HOH H 3 .   ? 3.949   8.642   49.160  1.00 48.86 ? 2063 HOH B O   1 
HETATM 4152 O  O   . HOH H 3 .   ? 11.179  7.800   41.727  1.00 52.87 ? 2064 HOH B O   1 
HETATM 4153 O  O   . HOH H 3 .   ? 7.616   12.137  46.444  1.00 62.32 ? 2065 HOH B O   1 
HETATM 4154 O  O   . HOH H 3 .   ? 7.601   8.109   48.024  1.00 50.18 ? 2066 HOH B O   1 
HETATM 4155 O  O   . HOH H 3 .   ? 2.637   4.601   30.148  1.00 52.21 ? 2067 HOH B O   1 
HETATM 4156 O  O   . HOH H 3 .   ? 5.502   8.088   33.273  1.00 51.63 ? 2068 HOH B O   1 
HETATM 4157 O  O   . HOH H 3 .   ? 8.977   6.000   29.786  1.00 54.24 ? 2069 HOH B O   1 
HETATM 4158 O  O   . HOH H 3 .   ? 11.332  -0.274  34.286  1.00 52.43 ? 2070 HOH B O   1 
HETATM 4159 O  O   . HOH H 3 .   ? 8.561   1.371   36.731  1.00 53.40 ? 2071 HOH B O   1 
HETATM 4160 O  O   . HOH H 3 .   ? 10.526  -0.428  37.921  1.00 62.25 ? 2072 HOH B O   1 
HETATM 4161 O  O   . HOH H 3 .   ? 2.539   -7.681  35.236  1.00 56.79 ? 2073 HOH B O   1 
HETATM 4162 O  O   . HOH H 3 .   ? -11.391 -3.128  39.508  1.00 52.98 ? 2074 HOH B O   1 
HETATM 4163 O  O   . HOH H 3 .   ? -14.827 -1.750  60.445  1.00 54.70 ? 2075 HOH B O   1 
HETATM 4164 O  O   . HOH H 3 .   ? -9.546  1.351   61.533  1.00 48.93 ? 2076 HOH B O   1 
HETATM 4165 O  O   . HOH H 3 .   ? -6.633  -1.710  61.242  1.00 54.74 ? 2077 HOH B O   1 
HETATM 4166 O  O   . HOH H 3 .   ? 0.104   1.428   53.063  1.00 56.27 ? 2078 HOH B O   1 
HETATM 4167 O  O   . HOH H 3 .   ? 0.287   1.358   63.058  1.00 55.71 ? 2079 HOH B O   1 
HETATM 4168 O  O   . HOH H 3 .   ? 5.019   -4.644  64.200  1.00 57.52 ? 2080 HOH B O   1 
HETATM 4169 O  O   . HOH H 3 .   ? 8.751   -2.562  65.186  1.00 58.99 ? 2081 HOH B O   1 
HETATM 4170 O  O   . HOH H 3 .   ? 3.429   -6.351  62.696  1.00 46.79 ? 2082 HOH B O   1 
HETATM 4171 O  O   . HOH H 3 .   ? -0.142  -13.949 63.735  1.00 53.28 ? 2083 HOH B O   1 
HETATM 4172 O  O   . HOH H 3 .   ? 4.572   -12.138 61.716  1.00 57.08 ? 2084 HOH B O   1 
HETATM 4173 O  O   . HOH H 3 .   ? -2.368  -11.989 61.763  1.00 50.57 ? 2085 HOH B O   1 
HETATM 4174 O  O   . HOH H 3 .   ? 3.594   -8.952  52.437  1.00 57.85 ? 2086 HOH B O   1 
HETATM 4175 O  O   . HOH H 3 .   ? -4.784  -4.329  52.464  1.00 54.29 ? 2087 HOH B O   1 
HETATM 4176 O  O   . HOH H 3 .   ? -6.907  -7.327  56.443  1.00 68.26 ? 2088 HOH B O   1 
HETATM 4177 O  O   . HOH H 3 .   ? -13.521 -7.102  50.324  1.00 49.08 ? 2089 HOH B O   1 
HETATM 4178 O  O   . HOH H 3 .   ? -9.165  -7.739  51.131  1.00 50.40 ? 2090 HOH B O   1 
HETATM 4179 O  O   . HOH H 3 .   ? -4.360  -7.900  49.404  1.00 56.88 ? 2091 HOH B O   1 
HETATM 4180 O  O   . HOH H 3 .   ? -5.397  -10.466 49.257  1.00 59.36 ? 2092 HOH B O   1 
HETATM 4181 O  O   . HOH H 3 .   ? -15.160 -0.769  40.184  1.00 57.97 ? 2093 HOH B O   1 
HETATM 4182 O  O   . HOH H 3 .   ? -11.526 3.651   36.715  1.00 40.41 ? 2094 HOH B O   1 
HETATM 4183 O  O   . HOH H 3 .   ? -12.651 0.309   36.530  1.00 42.22 ? 2095 HOH B O   1 
HETATM 4184 O  O   . HOH H 3 .   ? -3.039  13.361  26.041  1.00 54.27 ? 2096 HOH B O   1 
HETATM 4185 O  O   . HOH H 3 .   ? -8.328  14.331  31.424  1.00 60.35 ? 2097 HOH B O   1 
HETATM 4186 O  O   . HOH I 3 .   ? 19.420  -1.461  26.987  1.00 45.66 ? 2001 HOH C O   1 
HETATM 4187 O  O   . HOH I 3 .   ? 41.492  8.990   20.651  1.00 60.35 ? 2002 HOH C O   1 
HETATM 4188 O  O   . HOH I 3 .   ? 33.662  9.114   20.390  1.00 48.10 ? 2003 HOH C O   1 
HETATM 4189 O  O   . HOH I 3 .   ? 41.257  11.302  22.111  1.00 46.67 ? 2004 HOH C O   1 
HETATM 4190 O  O   . HOH I 3 .   ? 47.111  7.968   27.614  1.00 56.35 ? 2005 HOH C O   1 
HETATM 4191 O  O   . HOH I 3 .   ? 43.666  17.411  25.361  1.00 56.99 ? 2006 HOH C O   1 
HETATM 4192 O  O   . HOH I 3 .   ? 34.943  0.159   30.769  1.00 59.57 ? 2007 HOH C O   1 
HETATM 4193 O  O   . HOH I 3 .   ? 27.471  -0.699  28.704  1.00 49.99 ? 2008 HOH C O   1 
HETATM 4194 O  O   . HOH I 3 .   ? 31.694  -1.507  27.551  1.00 51.37 ? 2009 HOH C O   1 
HETATM 4195 O  O   . HOH I 3 .   ? 14.917  4.008   31.404  1.00 59.08 ? 2010 HOH C O   1 
HETATM 4196 O  O   . HOH I 3 .   ? 14.925  0.800   33.262  1.00 49.86 ? 2011 HOH C O   1 
HETATM 4197 O  O   . HOH I 3 .   ? 12.449  6.986   32.836  1.00 42.63 ? 2012 HOH C O   1 
HETATM 4198 O  O   . HOH I 3 .   ? 8.942   5.156   34.736  1.00 45.61 ? 2013 HOH C O   1 
HETATM 4199 O  O   . HOH I 3 .   ? 8.025   7.367   40.544  1.00 49.45 ? 2014 HOH C O   1 
HETATM 4200 O  O   . HOH I 3 .   ? 16.999  8.212   37.605  1.00 40.41 ? 2015 HOH C O   1 
HETATM 4201 O  O   . HOH I 3 .   ? 17.068  2.185   38.516  1.00 47.02 ? 2016 HOH C O   1 
HETATM 4202 O  O   . HOH I 3 .   ? 20.523  1.182   38.169  1.00 52.75 ? 2017 HOH C O   1 
HETATM 4203 O  O   . HOH I 3 .   ? 44.734  16.027  28.348  1.00 47.49 ? 2018 HOH C O   1 
HETATM 4204 O  O   . HOH I 3 .   ? 46.530  8.879   30.861  1.00 52.33 ? 2019 HOH C O   1 
HETATM 4205 O  O   . HOH I 3 .   ? 48.642  13.014  33.950  1.00 58.99 ? 2020 HOH C O   1 
HETATM 4206 O  O   . HOH I 3 .   ? 43.475  17.099  30.859  1.00 56.47 ? 2021 HOH C O   1 
HETATM 4207 O  O   . HOH I 3 .   ? 14.720  18.251  26.125  1.00 57.86 ? 2022 HOH C O   1 
HETATM 4208 O  O   . HOH I 3 .   ? 26.952  13.249  15.793  1.00 46.92 ? 2023 HOH C O   1 
HETATM 4209 O  O   . HOH I 3 .   ? 24.514  19.230  12.615  1.00 55.92 ? 2024 HOH C O   1 
HETATM 4210 O  O   . HOH I 3 .   ? 31.355  11.669  18.929  1.00 49.81 ? 2025 HOH C O   1 
HETATM 4211 O  O   . HOH I 3 .   ? 32.672  14.044  17.446  1.00 51.66 ? 2026 HOH C O   1 
HETATM 4212 O  O   . HOH I 3 .   ? 36.521  18.120  19.564  1.00 48.49 ? 2027 HOH C O   1 
HETATM 4213 O  O   . HOH I 3 .   ? 34.767  27.036  18.622  1.00 56.16 ? 2028 HOH C O   1 
HETATM 4214 O  O   . HOH I 3 .   ? 25.009  21.058  34.127  1.00 62.53 ? 2029 HOH C O   1 
HETATM 4215 O  O   . HOH I 3 .   ? 30.965  22.975  31.323  1.00 60.44 ? 2030 HOH C O   1 
HETATM 4216 O  O   . HOH I 3 .   ? 27.084  24.857  28.639  1.00 56.37 ? 2031 HOH C O   1 
HETATM 4217 O  O   . HOH I 3 .   ? 28.672  25.110  34.986  1.00 63.48 ? 2032 HOH C O   1 
HETATM 4218 O  O   . HOH I 3 .   ? 19.120  21.164  27.050  1.00 58.23 ? 2033 HOH C O   1 
HETATM 4219 O  O   . HOH I 3 .   ? 30.812  13.549  40.110  1.00 39.24 ? 2034 HOH C O   1 
HETATM 4220 O  O   . HOH I 3 .   ? 39.427  8.270   39.756  1.00 50.31 ? 2035 HOH C O   1 
HETATM 4221 O  O   . HOH I 3 .   ? 47.414  8.696   42.245  1.00 61.06 ? 2036 HOH C O   1 
HETATM 4222 O  O   . HOH I 3 .   ? 49.952  8.408   31.818  1.00 56.43 ? 2037 HOH C O   1 
HETATM 4223 O  O   . HOH I 3 .   ? 36.530  9.786   38.771  1.00 48.79 ? 2038 HOH C O   1 
HETATM 4224 O  O   . HOH I 3 .   ? 34.951  2.231   38.031  1.00 55.71 ? 2039 HOH C O   1 
HETATM 4225 O  O   . HOH I 3 .   ? 30.469  8.903   43.137  1.00 45.78 ? 2040 HOH C O   1 
HETATM 4226 O  O   . HOH I 3 .   ? 26.725  11.957  42.625  1.00 53.68 ? 2041 HOH C O   1 
HETATM 4227 O  O   . HOH I 3 .   ? 27.271  9.555   42.915  1.00 50.46 ? 2042 HOH C O   1 
HETATM 4228 O  O   . HOH I 3 .   ? 25.265  12.827  40.656  1.00 53.29 ? 2043 HOH C O   1 
HETATM 4229 O  O   . HOH I 3 .   ? 15.129  9.348   40.085  1.00 52.44 ? 2044 HOH C O   1 
HETATM 4230 O  O   . HOH I 3 .   ? 21.398  9.142   43.252  1.00 60.26 ? 2045 HOH C O   1 
HETATM 4231 O  O   . HOH I 3 .   ? 15.586  7.466   41.586  1.00 57.09 ? 2046 HOH C O   1 
HETATM 4232 O  O   . HOH I 3 .   ? 21.148  12.346  42.065  1.00 50.28 ? 2047 HOH C O   1 
HETATM 4233 O  O   . HOH I 3 .   ? 15.183  4.689   25.853  1.00 52.64 ? 2048 HOH C O   1 
HETATM 4234 O  O   . HOH I 3 .   ? 9.758   4.304   30.455  1.00 49.10 ? 2049 HOH C O   1 
HETATM 4235 O  O   . HOH I 3 .   ? 9.063   11.581  30.964  1.00 47.45 ? 2050 HOH C O   1 
HETATM 4236 O  O   . HOH I 3 .   ? 12.569  18.356  34.277  1.00 59.35 ? 2051 HOH C O   1 
HETATM 4237 O  O   . HOH I 3 .   ? 16.645  10.810  24.016  1.00 50.15 ? 2052 HOH C O   1 
HETATM 4238 O  O   . HOH I 3 .   ? 15.268  13.379  26.187  1.00 47.64 ? 2053 HOH C O   1 
HETATM 4239 O  O   . HOH I 3 .   ? 15.022  17.134  22.909  1.00 54.10 ? 2054 HOH C O   1 
HETATM 4240 O  O   . HOH I 3 .   ? 16.936  18.774  22.794  1.00 57.15 ? 2055 HOH C O   1 
HETATM 4241 O  O   . HOH I 3 .   ? 33.251  23.790  42.037  1.00 62.07 ? 2056 HOH C O   1 
HETATM 4242 O  O   . HOH I 3 .   ? 28.518  24.915  22.898  1.00 58.93 ? 2057 HOH C O   1 
HETATM 4243 O  O   . HOH I 3 .   ? 36.262  20.049  21.116  1.00 54.79 ? 2058 HOH C O   1 
HETATM 4244 O  O   . HOH I 3 .   ? 36.678  22.718  23.511  1.00 54.99 ? 2059 HOH C O   1 
HETATM 4245 O  O   . HOH I 3 .   ? 30.250  24.077  28.303  1.00 52.56 ? 2060 HOH C O   1 
HETATM 4246 O  O   . HOH I 3 .   ? 32.451  24.417  27.124  1.00 57.35 ? 2061 HOH C O   1 
HETATM 4247 O  O   . HOH I 3 .   ? 41.850  14.989  24.230  1.00 44.02 ? 2062 HOH C O   1 
HETATM 4248 O  O   . HOH I 3 .   ? 33.993  11.611  19.844  1.00 50.33 ? 2063 HOH C O   1 
HETATM 4249 O  O   . HOH I 3 .   ? 30.052  9.055   19.757  1.00 40.98 ? 2064 HOH C O   1 
HETATM 4250 O  O   . HOH I 3 .   ? 29.964  6.774   21.879  1.00 38.51 ? 2065 HOH C O   1 
HETATM 4251 O  O   . HOH I 3 .   ? 26.346  -3.345  23.639  1.00 45.20 ? 2066 HOH C O   1 
HETATM 4252 O  O   . HOH J 3 .   ? 12.986  14.062  21.970  1.00 62.54 ? 2001 HOH D O   1 
HETATM 4253 O  O   . HOH J 3 .   ? 32.027  15.134  4.399   1.00 59.60 ? 2002 HOH D O   1 
HETATM 4254 O  O   . HOH J 3 .   ? 32.319  10.477  15.563  1.00 54.56 ? 2003 HOH D O   1 
HETATM 4255 O  O   . HOH J 3 .   ? 35.847  0.187   13.138  1.00 50.56 ? 2004 HOH D O   1 
HETATM 4256 O  O   . HOH J 3 .   ? 39.014  11.293  3.176   1.00 68.62 ? 2005 HOH D O   1 
HETATM 4257 O  O   . HOH J 3 .   ? 34.044  13.763  6.987   1.00 54.56 ? 2006 HOH D O   1 
HETATM 4258 O  O   . HOH J 3 .   ? 37.795  -1.950  2.225   1.00 56.74 ? 2007 HOH D O   1 
HETATM 4259 O  O   . HOH J 3 .   ? 20.847  17.238  11.281  1.00 54.11 ? 2008 HOH D O   1 
HETATM 4260 O  O   . HOH J 3 .   ? 25.893  17.829  5.951   1.00 58.25 ? 2009 HOH D O   1 
HETATM 4261 O  O   . HOH J 3 .   ? 25.066  18.323  10.010  1.00 51.39 ? 2010 HOH D O   1 
HETATM 4262 O  O   . HOH J 3 .   ? 4.519   6.507   5.730   1.00 50.60 ? 2011 HOH D O   1 
HETATM 4263 O  O   . HOH J 3 .   ? 8.736   6.867   8.988   1.00 58.29 ? 2012 HOH D O   1 
HETATM 4264 O  O   . HOH J 3 .   ? 7.890   13.030  8.467   1.00 55.02 ? 2013 HOH D O   1 
HETATM 4265 O  O   . HOH J 3 .   ? 27.762  16.393  4.690   1.00 60.20 ? 2014 HOH D O   1 
HETATM 4266 O  O   . HOH J 3 .   ? 37.353  3.179   1.151   1.00 57.27 ? 2015 HOH D O   1 
HETATM 4267 O  O   . HOH J 3 .   ? 34.922  -1.312  -0.017  1.00 56.52 ? 2016 HOH D O   1 
HETATM 4268 O  O   . HOH J 3 .   ? 35.321  2.177   0.060   1.00 63.20 ? 2017 HOH D O   1 
HETATM 4269 O  O   . HOH J 3 .   ? 37.722  4.590   -6.206  1.00 61.39 ? 2018 HOH D O   1 
HETATM 4270 O  O   . HOH J 3 .   ? 28.186  1.449   -8.544  1.00 54.47 ? 2019 HOH D O   1 
HETATM 4271 O  O   . HOH J 3 .   ? 28.232  -1.402  -7.397  1.00 58.53 ? 2020 HOH D O   1 
HETATM 4272 O  O   . HOH J 3 .   ? 17.550  -3.216  21.336  1.00 58.19 ? 2021 HOH D O   1 
HETATM 4273 O  O   . HOH J 3 .   ? 28.923  -2.480  26.160  1.00 59.13 ? 2022 HOH D O   1 
HETATM 4274 O  O   . HOH J 3 .   ? 30.086  -4.660  23.422  1.00 52.55 ? 2023 HOH D O   1 
HETATM 4275 O  O   . HOH J 3 .   ? 29.576  1.694   16.780  1.00 40.04 ? 2024 HOH D O   1 
HETATM 4276 O  O   . HOH J 3 .   ? 31.451  5.806   16.654  1.00 54.93 ? 2025 HOH D O   1 
HETATM 4277 O  O   . HOH J 3 .   ? 34.636  3.699   15.041  1.00 61.15 ? 2026 HOH D O   1 
HETATM 4278 O  O   . HOH J 3 .   ? 29.295  3.925   16.499  1.00 45.82 ? 2027 HOH D O   1 
HETATM 4279 O  O   . HOH J 3 .   ? 29.535  3.910   21.924  1.00 45.22 ? 2028 HOH D O   1 
HETATM 4280 O  O   . HOH J 3 .   ? 34.023  6.156   18.563  1.00 51.73 ? 2029 HOH D O   1 
HETATM 4281 O  O   . HOH J 3 .   ? 37.972  -1.841  23.344  1.00 60.03 ? 2030 HOH D O   1 
HETATM 4282 O  O   . HOH J 3 .   ? 26.996  -5.383  21.116  1.00 63.06 ? 2031 HOH D O   1 
HETATM 4283 O  O   . HOH J 3 .   ? 24.046  -7.991  10.081  1.00 59.40 ? 2032 HOH D O   1 
HETATM 4284 O  O   . HOH J 3 .   ? 17.101  -5.397  16.379  1.00 56.54 ? 2033 HOH D O   1 
HETATM 4285 O  O   . HOH J 3 .   ? 10.216  3.555   2.558   1.00 53.96 ? 2034 HOH D O   1 
HETATM 4286 O  O   . HOH J 3 .   ? 8.820   -8.063  4.706   1.00 58.50 ? 2035 HOH D O   1 
HETATM 4287 O  O   . HOH J 3 .   ? 15.389  2.870   1.621   1.00 55.48 ? 2036 HOH D O   1 
HETATM 4288 O  O   . HOH J 3 .   ? 19.442  3.615   -0.639  1.00 48.08 ? 2037 HOH D O   1 
HETATM 4289 O  O   . HOH J 3 .   ? 24.600  8.050   -2.490  1.00 55.71 ? 2038 HOH D O   1 
HETATM 4290 O  O   . HOH J 3 .   ? 36.892  10.438  -1.429  1.00 51.46 ? 2039 HOH D O   1 
HETATM 4291 O  O   . HOH J 3 .   ? 22.394  12.782  -4.567  1.00 57.50 ? 2040 HOH D O   1 
HETATM 4292 O  O   . HOH J 3 .   ? 15.687  11.556  -2.869  1.00 56.10 ? 2041 HOH D O   1 
HETATM 4293 O  O   . HOH J 3 .   ? 11.475  5.041   0.206   1.00 60.14 ? 2042 HOH D O   1 
HETATM 4294 O  O   . HOH J 3 .   ? 14.669  7.174   -1.191  1.00 55.04 ? 2043 HOH D O   1 
HETATM 4295 O  O   . HOH J 3 .   ? 7.010   4.480   11.698  1.00 58.75 ? 2044 HOH D O   1 
HETATM 4296 O  O   . HOH J 3 .   ? 4.209   -0.213  16.290  1.00 56.65 ? 2045 HOH D O   1 
HETATM 4297 O  O   . HOH J 3 .   ? 8.297   4.012   15.664  1.00 50.26 ? 2046 HOH D O   1 
HETATM 4298 O  O   . HOH J 3 .   ? 13.650  1.949   19.076  1.00 45.48 ? 2047 HOH D O   1 
HETATM 4299 O  O   . HOH J 3 .   ? 15.616  -1.730  22.129  1.00 52.63 ? 2048 HOH D O   1 
HETATM 4300 O  O   . HOH J 3 .   ? 29.395  -5.723  2.954   1.00 52.74 ? 2049 HOH D O   1 
HETATM 4301 O  O   . HOH J 3 .   ? 31.348  -9.910  3.036   1.00 58.89 ? 2050 HOH D O   1 
HETATM 4302 O  O   . HOH J 3 .   ? 19.333  -2.119  3.164   1.00 62.06 ? 2051 HOH D O   1 
HETATM 4303 O  O   . HOH J 3 .   ? 29.269  -6.979  8.858   1.00 56.53 ? 2052 HOH D O   1 
HETATM 4304 O  O   . HOH J 3 .   ? 34.512  -4.339  9.806   1.00 58.32 ? 2053 HOH D O   1 
HETATM 4305 O  O   . HOH J 3 .   ? 26.145  -6.797  9.316   1.00 54.94 ? 2054 HOH D O   1 
HETATM 4306 O  O   . HOH J 3 .   ? 33.001  6.210   14.896  1.00 58.37 ? 2055 HOH D O   1 
HETATM 4307 O  O   . HOH J 3 .   ? 29.483  8.212   17.037  1.00 39.40 ? 2056 HOH D O   1 
HETATM 4308 O  O   . HOH J 3 .   ? 27.905  10.457  15.500  1.00 38.78 ? 2057 HOH D O   1 
HETATM 4309 O  O   . HOH J 3 .   ? 15.395  17.257  17.187  1.00 50.14 ? 2058 HOH D O   1 
HETATM 4310 O  O   . HOH J 3 .   ? 22.633  20.074  15.987  1.00 47.95 ? 2059 HOH D 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   1   ALA ALA 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  67  LEU LEU A . n 
A 1 69  SER 69  68  68  SER SER A . n 
A 1 70  ARG 70  69  69  ARG ARG A . n 
A 1 71  LYS 71  70  70  LYS LYS A . n 
A 1 72  HIS 72  71  71  HIS HIS A . n 
A 1 73  GLY 73  72  72  GLY GLY A . n 
A 1 74  GLY 74  73  73  GLY GLY A . n 
A 1 75  PRO 75  74  74  PRO PRO A . n 
A 1 76  LYS 76  75  75  LYS LYS A . n 
A 1 77  ASP 77  76  76  ASP ASP A . n 
A 1 78  GLU 78  77  77  GLU GLU A . n 
A 1 79  GLU 79  78  78  GLU GLU A . n 
A 1 80  ARG 80  79  79  ARG ARG A . n 
A 1 81  HIS 81  80  80  HIS HIS 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 CYS 112 111 111 CYS CYS 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 126 125 125 ASP ASP A . n 
A 1 127 LEU 127 126 126 LEU LEU A . n 
A 1 128 GLY 128 127 127 GLY GLY A . n 
A 1 129 LYS 129 128 128 LYS LYS A . n 
A 1 130 GLY 130 129 129 GLY GLY A . n 
A 1 131 GLY 131 130 130 GLY GLY A . n 
A 1 132 ASN 132 131 131 ASN ASN A . n 
A 1 133 GLU 133 132 132 GLU GLU A . n 
A 1 134 GLU 134 133 133 GLU GLU A . n 
A 1 135 SER 135 134 134 SER SER A . n 
A 1 136 THR 136 135 135 THR THR A . n 
A 1 137 LYS 137 136 136 LYS LYS A . n 
A 1 138 THR 138 137 137 THR THR A . n 
A 1 139 GLY 139 138 138 GLY GLY A . n 
A 1 140 ASN 140 139 139 ASN ASN A . n 
A 1 141 ALA 141 140 140 ALA ALA 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 1 1   ACE 1   0   0   ACE ACE B . n 
B 1 2   ALA 2   1   1   ALA ALA B . n 
B 1 3   THR 3   2   2   THR THR B . n 
B 1 4   LYS 4   3   3   LYS LYS B . n 
B 1 5   ALA 5   4   4   ALA ALA B . n 
B 1 6   VAL 6   5   5   VAL VAL B . n 
B 1 7   CYS 7   6   6   CYS CYS B . n 
B 1 8   VAL 8   7   7   VAL VAL B . n 
B 1 9   LEU 9   8   8   LEU LEU B . n 
B 1 10  LYS 10  9   9   LYS LYS B . n 
B 1 11  GLY 11  10  10  GLY GLY B . n 
B 1 12  ASP 12  11  11  ASP ASP B . n 
B 1 13  GLY 13  12  12  GLY GLY B . n 
B 1 14  PRO 14  13  13  PRO PRO B . n 
B 1 15  VAL 15  14  14  VAL VAL B . n 
B 1 16  GLN 16  15  15  GLN GLN B . n 
B 1 17  GLY 17  16  16  GLY GLY B . n 
B 1 18  ILE 18  17  17  ILE ILE B . n 
B 1 19  ILE 19  18  18  ILE ILE B . n 
B 1 20  ASN 20  19  19  ASN ASN B . n 
B 1 21  PHE 21  20  20  PHE PHE B . n 
B 1 22  GLU 22  21  21  GLU GLU B . n 
B 1 23  GLN 23  22  22  GLN GLN B . n 
B 1 24  LYS 24  23  23  LYS LYS B . n 
B 1 25  GLU 25  24  24  GLU GLU B . n 
B 1 26  SER 26  25  25  SER SER B . n 
B 1 27  ASN 27  26  26  ASN ASN B . n 
B 1 28  GLY 28  27  27  GLY GLY B . n 
B 1 29  PRO 29  28  28  PRO PRO B . n 
B 1 30  VAL 30  29  29  VAL VAL B . n 
B 1 31  LYS 31  30  30  LYS LYS B . n 
B 1 32  VAL 32  31  31  VAL VAL B . n 
B 1 33  TRP 33  32  32  TRP TRP B . n 
B 1 34  GLY 34  33  33  GLY GLY B . n 
B 1 35  SER 35  34  34  SER SER B . n 
B 1 36  ILE 36  35  35  ILE ILE B . n 
B 1 37  LYS 37  36  36  LYS LYS B . n 
B 1 38  GLY 38  37  37  GLY GLY B . n 
B 1 39  LEU 39  38  38  LEU LEU B . n 
B 1 40  THR 40  39  39  THR THR B . n 
B 1 41  GLU 41  40  40  GLU GLU B . n 
B 1 42  GLY 42  41  41  GLY GLY B . n 
B 1 43  LEU 43  42  42  LEU LEU B . n 
B 1 44  HIS 44  43  43  HIS HIS B . n 
B 1 45  GLY 45  44  44  GLY GLY B . n 
B 1 46  PHE 46  45  45  PHE PHE B . n 
B 1 47  HIS 47  46  46  HIS HIS B . n 
B 1 48  VAL 48  47  47  VAL VAL B . n 
B 1 49  HIS 49  48  48  HIS HIS B . n 
B 1 50  GLU 50  49  49  GLU GLU B . n 
B 1 51  PHE 51  50  50  PHE PHE B . n 
B 1 52  GLY 52  51  51  GLY GLY B . n 
B 1 53  ASP 53  52  52  ASP ASP B . n 
B 1 54  ASN 54  53  53  ASN ASN B . n 
B 1 55  THR 55  54  54  THR THR B . n 
B 1 56  ALA 56  55  55  ALA ALA B . n 
B 1 57  GLY 57  56  56  GLY GLY B . n 
B 1 58  CYS 58  57  57  CYS CYS B . n 
B 1 59  THR 59  58  58  THR THR B . n 
B 1 60  SER 60  59  59  SER SER B . n 
B 1 61  ALA 61  60  60  ALA ALA B . n 
B 1 62  GLY 62  61  61  GLY GLY B . n 
B 1 63  PRO 63  62  62  PRO PRO B . n 
B 1 64  HIS 64  63  63  HIS HIS B . n 
B 1 65  PHE 65  64  64  PHE PHE B . n 
B 1 66  ASN 66  65  65  ASN ASN B . n 
B 1 67  PRO 67  66  66  PRO PRO B . n 
B 1 68  LEU 68  67  67  LEU LEU B . n 
B 1 69  SER 69  68  68  SER SER B . n 
B 1 70  ARG 70  69  69  ARG ARG B . n 
B 1 71  LYS 71  70  70  LYS LYS B . n 
B 1 72  HIS 72  71  71  HIS HIS B . n 
B 1 73  GLY 73  72  72  GLY GLY B . n 
B 1 74  GLY 74  73  73  GLY GLY B . n 
B 1 75  PRO 75  74  74  PRO PRO B . n 
B 1 76  LYS 76  75  75  LYS LYS B . n 
B 1 77  ASP 77  76  76  ASP ASP B . n 
B 1 78  GLU 78  77  77  GLU GLU B . n 
B 1 79  GLU 79  78  78  GLU GLU B . n 
B 1 80  ARG 80  79  79  ARG ARG B . n 
B 1 81  HIS 81  80  80  HIS HIS B . n 
B 1 82  VAL 82  81  81  VAL VAL B . n 
B 1 83  GLY 83  82  82  GLY GLY B . n 
B 1 84  ASP 84  83  83  ASP ASP B . n 
B 1 85  LEU 85  84  84  LEU LEU B . n 
B 1 86  GLY 86  85  85  GLY GLY B . n 
B 1 87  ASN 87  86  86  ASN ASN B . n 
B 1 88  VAL 88  87  87  VAL VAL B . n 
B 1 89  THR 89  88  88  THR THR B . n 
B 1 90  ALA 90  89  89  ALA ALA B . n 
B 1 91  ASP 91  90  90  ASP ASP B . n 
B 1 92  LYS 92  91  91  LYS LYS B . n 
B 1 93  ASP 93  92  92  ASP ASP B . n 
B 1 94  GLY 94  93  93  GLY GLY B . n 
B 1 95  VAL 95  94  94  VAL VAL B . n 
B 1 96  ALA 96  95  95  ALA ALA B . n 
B 1 97  ASP 97  96  96  ASP ASP B . n 
B 1 98  VAL 98  97  97  VAL VAL B . n 
B 1 99  SER 99  98  98  SER SER B . n 
B 1 100 ILE 100 99  99  ILE ILE B . n 
B 1 101 GLU 101 100 100 GLU GLU B . n 
B 1 102 ASP 102 101 101 ASP ASP B . n 
B 1 103 SER 103 102 102 SER SER B . n 
B 1 104 VAL 104 103 103 VAL VAL B . n 
B 1 105 ILE 105 104 104 ILE ILE B . n 
B 1 106 SER 106 105 105 SER SER B . n 
B 1 107 LEU 107 106 106 LEU LEU B . n 
B 1 108 SER 108 107 107 SER SER B . n 
B 1 109 GLY 109 108 108 GLY GLY B . n 
B 1 110 ASP 110 109 109 ASP ASP B . n 
B 1 111 HIS 111 110 110 HIS HIS B . n 
B 1 112 CYS 112 111 111 CYS CYS B . n 
B 1 113 ILE 113 112 112 ILE ILE B . n 
B 1 114 ILE 114 113 113 ILE ILE B . n 
B 1 115 GLY 115 114 114 GLY GLY B . n 
B 1 116 ARG 116 115 115 ARG ARG B . n 
B 1 117 THR 117 116 116 THR THR B . n 
B 1 118 LEU 118 117 117 LEU LEU B . n 
B 1 119 VAL 119 118 118 VAL VAL B . n 
B 1 120 VAL 120 119 119 VAL VAL B . n 
B 1 121 HIS 121 120 120 HIS HIS B . n 
B 1 122 GLU 122 121 121 GLU GLU B . n 
B 1 123 LYS 123 122 122 LYS LYS B . n 
B 1 124 ALA 124 123 123 ALA ALA B . n 
B 1 125 ASP 125 124 124 ASP ASP B . n 
B 1 126 ASP 126 125 125 ASP ASP B . n 
B 1 127 LEU 127 126 126 LEU LEU B . n 
B 1 128 GLY 128 127 127 GLY GLY B . n 
B 1 129 LYS 129 128 128 LYS LYS B . n 
B 1 130 GLY 130 129 129 GLY GLY B . n 
B 1 131 GLY 131 130 130 GLY GLY B . n 
B 1 132 ASN 132 131 131 ASN ASN B . n 
B 1 133 GLU 133 132 132 GLU GLU B . n 
B 1 134 GLU 134 133 133 GLU GLU B . n 
B 1 135 SER 135 134 134 SER SER B . n 
B 1 136 THR 136 135 135 THR THR B . n 
B 1 137 LYS 137 136 136 LYS LYS B . n 
B 1 138 THR 138 137 137 THR THR B . n 
B 1 139 GLY 139 138 138 GLY GLY B . n 
B 1 140 ASN 140 139 139 ASN ASN B . n 
B 1 141 ALA 141 140 140 ALA ALA B . n 
B 1 142 GLY 142 141 141 GLY GLY B . n 
B 1 143 SER 143 142 142 SER SER B . n 
B 1 144 ARG 144 143 143 ARG ARG B . n 
B 1 145 LEU 145 144 144 LEU LEU B . n 
B 1 146 ALA 146 145 145 ALA ALA B . n 
B 1 147 CYS 147 146 146 CYS CYS B . n 
B 1 148 GLY 148 147 147 GLY GLY B . n 
B 1 149 VAL 149 148 148 VAL VAL B . n 
B 1 150 ILE 150 149 149 ILE ILE B . n 
B 1 151 GLY 151 150 150 GLY GLY B . n 
B 1 152 ILE 152 151 151 ILE ILE B . n 
B 1 153 ALA 153 152 152 ALA ALA B . n 
B 1 154 GLN 154 153 153 GLN GLN B . n 
C 1 1   ACE 1   0   ?   ?   ?   C . n 
C 1 2   ALA 2   1   1   ALA ALA C . n 
C 1 3   THR 3   2   2   THR THR C . n 
C 1 4   LYS 4   3   3   LYS LYS C . n 
C 1 5   ALA 5   4   4   ALA ALA C . n 
C 1 6   VAL 6   5   5   VAL VAL C . n 
C 1 7   CYS 7   6   6   CYS CYS C . n 
C 1 8   VAL 8   7   7   VAL VAL C . n 
C 1 9   LEU 9   8   8   LEU LEU C . n 
C 1 10  LYS 10  9   9   LYS LYS C . n 
C 1 11  GLY 11  10  10  GLY GLY C . n 
C 1 12  ASP 12  11  11  ASP ASP C . n 
C 1 13  GLY 13  12  12  GLY GLY C . n 
C 1 14  PRO 14  13  13  PRO PRO C . n 
C 1 15  VAL 15  14  14  VAL VAL C . n 
C 1 16  GLN 16  15  15  GLN GLN C . n 
C 1 17  GLY 17  16  16  GLY GLY C . n 
C 1 18  ILE 18  17  17  ILE ILE C . n 
C 1 19  ILE 19  18  18  ILE ILE C . n 
C 1 20  ASN 20  19  19  ASN ASN C . n 
C 1 21  PHE 21  20  20  PHE PHE C . n 
C 1 22  GLU 22  21  21  GLU GLU C . n 
C 1 23  GLN 23  22  22  GLN GLN C . n 
C 1 24  LYS 24  23  23  LYS LYS C . n 
C 1 25  GLU 25  24  24  GLU GLU C . n 
C 1 26  SER 26  25  25  SER SER C . n 
C 1 27  ASN 27  26  26  ASN ASN C . n 
C 1 28  GLY 28  27  27  GLY GLY C . n 
C 1 29  PRO 29  28  28  PRO PRO C . n 
C 1 30  VAL 30  29  29  VAL VAL C . n 
C 1 31  LYS 31  30  30  LYS LYS C . n 
C 1 32  VAL 32  31  31  VAL VAL C . n 
C 1 33  TRP 33  32  32  TRP TRP C . n 
C 1 34  GLY 34  33  33  GLY GLY C . n 
C 1 35  SER 35  34  34  SER SER C . n 
C 1 36  ILE 36  35  35  ILE ILE C . n 
C 1 37  LYS 37  36  36  LYS LYS C . n 
C 1 38  GLY 38  37  37  GLY GLY C . n 
C 1 39  LEU 39  38  38  LEU LEU C . n 
C 1 40  THR 40  39  39  THR THR C . n 
C 1 41  GLU 41  40  40  GLU GLU C . n 
C 1 42  GLY 42  41  41  GLY GLY C . n 
C 1 43  LEU 43  42  42  LEU LEU C . n 
C 1 44  HIS 44  43  43  HIS HIS C . n 
C 1 45  GLY 45  44  44  GLY GLY C . n 
C 1 46  PHE 46  45  45  PHE PHE C . n 
C 1 47  HIS 47  46  46  HIS HIS C . n 
C 1 48  VAL 48  47  47  VAL VAL C . n 
C 1 49  HIS 49  48  48  HIS HIS C . n 
C 1 50  GLU 50  49  49  GLU GLU C . n 
C 1 51  PHE 51  50  50  PHE PHE C . n 
C 1 52  GLY 52  51  51  GLY GLY C . n 
C 1 53  ASP 53  52  52  ASP ASP C . n 
C 1 54  ASN 54  53  53  ASN ASN C . n 
C 1 55  THR 55  54  54  THR THR C . n 
C 1 56  ALA 56  55  55  ALA ALA C . n 
C 1 57  GLY 57  56  56  GLY GLY C . n 
C 1 58  CYS 58  57  57  CYS CYS C . n 
C 1 59  THR 59  58  58  THR THR C . n 
C 1 60  SER 60  59  59  SER SER C . n 
C 1 61  ALA 61  60  60  ALA ALA C . n 
C 1 62  GLY 62  61  61  GLY GLY C . n 
C 1 63  PRO 63  62  62  PRO PRO C . n 
C 1 64  HIS 64  63  63  HIS HIS C . n 
C 1 65  PHE 65  64  64  PHE PHE C . n 
C 1 66  ASN 66  65  65  ASN ASN C . n 
C 1 67  PRO 67  66  66  PRO PRO C . n 
C 1 68  LEU 68  67  67  LEU LEU C . n 
C 1 69  SER 69  68  68  SER SER C . n 
C 1 70  ARG 70  69  ?   ?   ?   C . n 
C 1 71  LYS 71  70  ?   ?   ?   C . n 
C 1 72  HIS 72  71  ?   ?   ?   C . n 
C 1 73  GLY 73  72  ?   ?   ?   C . n 
C 1 74  GLY 74  73  ?   ?   ?   C . n 
C 1 75  PRO 75  74  ?   ?   ?   C . n 
C 1 76  LYS 76  75  ?   ?   ?   C . n 
C 1 77  ASP 77  76  ?   ?   ?   C . n 
C 1 78  GLU 78  77  ?   ?   ?   C . n 
C 1 79  GLU 79  78  ?   ?   ?   C . n 
C 1 80  ARG 80  79  79  ARG ARG C . n 
C 1 81  HIS 81  80  80  HIS HIS C . n 
C 1 82  VAL 82  81  81  VAL VAL C . n 
C 1 83  GLY 83  82  82  GLY GLY C . n 
C 1 84  ASP 84  83  83  ASP ASP C . n 
C 1 85  LEU 85  84  84  LEU LEU C . n 
C 1 86  GLY 86  85  85  GLY GLY C . n 
C 1 87  ASN 87  86  86  ASN ASN C . n 
C 1 88  VAL 88  87  87  VAL VAL C . n 
C 1 89  THR 89  88  88  THR THR C . n 
C 1 90  ALA 90  89  89  ALA ALA C . n 
C 1 91  ASP 91  90  90  ASP ASP C . n 
C 1 92  LYS 92  91  91  LYS LYS C . n 
C 1 93  ASP 93  92  92  ASP ASP C . n 
C 1 94  GLY 94  93  93  GLY GLY C . n 
C 1 95  VAL 95  94  94  VAL VAL C . n 
C 1 96  ALA 96  95  95  ALA ALA C . n 
C 1 97  ASP 97  96  96  ASP ASP C . n 
C 1 98  VAL 98  97  97  VAL VAL C . n 
C 1 99  SER 99  98  98  SER SER C . n 
C 1 100 ILE 100 99  99  ILE ILE C . n 
C 1 101 GLU 101 100 100 GLU GLU C . n 
C 1 102 ASP 102 101 101 ASP ASP C . n 
C 1 103 SER 103 102 102 SER SER C . n 
C 1 104 VAL 104 103 103 VAL VAL C . n 
C 1 105 ILE 105 104 104 ILE ILE C . n 
C 1 106 SER 106 105 105 SER SER C . n 
C 1 107 LEU 107 106 106 LEU LEU C . n 
C 1 108 SER 108 107 107 SER SER C . n 
C 1 109 GLY 109 108 108 GLY GLY C . n 
C 1 110 ASP 110 109 109 ASP ASP C . n 
C 1 111 HIS 111 110 110 HIS HIS C . n 
C 1 112 CYS 112 111 111 CYS CYS C . n 
C 1 113 ILE 113 112 112 ILE ILE C . n 
C 1 114 ILE 114 113 113 ILE ILE C . n 
C 1 115 GLY 115 114 114 GLY GLY C . n 
C 1 116 ARG 116 115 115 ARG ARG C . n 
C 1 117 THR 117 116 116 THR THR C . n 
C 1 118 LEU 118 117 117 LEU LEU C . n 
C 1 119 VAL 119 118 118 VAL VAL C . n 
C 1 120 VAL 120 119 119 VAL VAL C . n 
C 1 121 HIS 121 120 120 HIS HIS C . n 
C 1 122 GLU 122 121 121 GLU GLU C . n 
C 1 123 LYS 123 122 122 LYS LYS C . n 
C 1 124 ALA 124 123 123 ALA ALA C . n 
C 1 125 ASP 125 124 124 ASP ASP C . n 
C 1 126 ASP 126 125 ?   ?   ?   C . n 
C 1 127 LEU 127 126 ?   ?   ?   C . n 
C 1 128 GLY 128 127 ?   ?   ?   C . n 
C 1 129 LYS 129 128 ?   ?   ?   C . n 
C 1 130 GLY 130 129 ?   ?   ?   C . n 
C 1 131 GLY 131 130 ?   ?   ?   C . n 
C 1 132 ASN 132 131 ?   ?   ?   C . n 
C 1 133 GLU 133 132 ?   ?   ?   C . n 
C 1 134 GLU 134 133 ?   ?   ?   C . n 
C 1 135 SER 135 134 ?   ?   ?   C . n 
C 1 136 THR 136 135 ?   ?   ?   C . n 
C 1 137 LYS 137 136 ?   ?   ?   C . n 
C 1 138 THR 138 137 ?   ?   ?   C . n 
C 1 139 GLY 139 138 ?   ?   ?   C . n 
C 1 140 ASN 140 139 ?   ?   ?   C . n 
C 1 141 ALA 141 140 ?   ?   ?   C . n 
C 1 142 GLY 142 141 141 GLY GLY C . n 
C 1 143 SER 143 142 142 SER SER C . n 
C 1 144 ARG 144 143 143 ARG ARG C . n 
C 1 145 LEU 145 144 144 LEU LEU C . n 
C 1 146 ALA 146 145 145 ALA ALA C . n 
C 1 147 CYS 147 146 146 CYS CYS C . n 
C 1 148 GLY 148 147 147 GLY GLY C . n 
C 1 149 VAL 149 148 148 VAL VAL C . n 
C 1 150 ILE 150 149 149 ILE ILE C . n 
C 1 151 GLY 151 150 150 GLY GLY C . n 
C 1 152 ILE 152 151 151 ILE ILE C . n 
C 1 153 ALA 153 152 152 ALA ALA C . n 
C 1 154 GLN 154 153 153 GLN GLN C . n 
D 1 1   ACE 1   0   ?   ?   ?   D . n 
D 1 2   ALA 2   1   1   ALA ALA D . n 
D 1 3   THR 3   2   2   THR THR D . n 
D 1 4   LYS 4   3   3   LYS LYS D . n 
D 1 5   ALA 5   4   4   ALA ALA D . n 
D 1 6   VAL 6   5   5   VAL VAL D . n 
D 1 7   CYS 7   6   6   CYS CYS D . n 
D 1 8   VAL 8   7   7   VAL VAL D . n 
D 1 9   LEU 9   8   8   LEU LEU D . n 
D 1 10  LYS 10  9   9   LYS LYS D . n 
D 1 11  GLY 11  10  10  GLY GLY D . n 
D 1 12  ASP 12  11  11  ASP ASP D . n 
D 1 13  GLY 13  12  12  GLY GLY D . n 
D 1 14  PRO 14  13  13  PRO PRO D . n 
D 1 15  VAL 15  14  14  VAL VAL D . n 
D 1 16  GLN 16  15  15  GLN GLN D . n 
D 1 17  GLY 17  16  16  GLY GLY D . n 
D 1 18  ILE 18  17  17  ILE ILE D . n 
D 1 19  ILE 19  18  18  ILE ILE D . n 
D 1 20  ASN 20  19  19  ASN ASN D . n 
D 1 21  PHE 21  20  20  PHE PHE D . n 
D 1 22  GLU 22  21  21  GLU GLU D . n 
D 1 23  GLN 23  22  22  GLN GLN D . n 
D 1 24  LYS 24  23  23  LYS LYS D . n 
D 1 25  GLU 25  24  24  GLU GLU D . n 
D 1 26  SER 26  25  25  SER SER D . n 
D 1 27  ASN 27  26  26  ASN ASN D . n 
D 1 28  GLY 28  27  27  GLY GLY D . n 
D 1 29  PRO 29  28  28  PRO PRO D . n 
D 1 30  VAL 30  29  29  VAL VAL D . n 
D 1 31  LYS 31  30  30  LYS LYS D . n 
D 1 32  VAL 32  31  31  VAL VAL D . n 
D 1 33  TRP 33  32  32  TRP TRP D . n 
D 1 34  GLY 34  33  33  GLY GLY D . n 
D 1 35  SER 35  34  34  SER SER D . n 
D 1 36  ILE 36  35  35  ILE ILE D . n 
D 1 37  LYS 37  36  36  LYS LYS D . n 
D 1 38  GLY 38  37  37  GLY GLY D . n 
D 1 39  LEU 39  38  38  LEU LEU D . n 
D 1 40  THR 40  39  39  THR THR D . n 
D 1 41  GLU 41  40  40  GLU GLU D . n 
D 1 42  GLY 42  41  41  GLY GLY D . n 
D 1 43  LEU 43  42  42  LEU LEU D . n 
D 1 44  HIS 44  43  43  HIS HIS D . n 
D 1 45  GLY 45  44  44  GLY GLY D . n 
D 1 46  PHE 46  45  45  PHE PHE D . n 
D 1 47  HIS 47  46  46  HIS HIS D . n 
D 1 48  VAL 48  47  47  VAL VAL D . n 
D 1 49  HIS 49  48  48  HIS HIS D . n 
D 1 50  GLU 50  49  49  GLU GLU D . n 
D 1 51  PHE 51  50  50  PHE PHE D . n 
D 1 52  GLY 52  51  51  GLY GLY D . n 
D 1 53  ASP 53  52  52  ASP ASP D . n 
D 1 54  ASN 54  53  53  ASN ASN D . n 
D 1 55  THR 55  54  54  THR THR D . n 
D 1 56  ALA 56  55  55  ALA ALA D . n 
D 1 57  GLY 57  56  56  GLY GLY D . n 
D 1 58  CYS 58  57  57  CYS CYS D . n 
D 1 59  THR 59  58  58  THR THR D . n 
D 1 60  SER 60  59  59  SER SER D . n 
D 1 61  ALA 61  60  60  ALA ALA D . n 
D 1 62  GLY 62  61  61  GLY GLY D . n 
D 1 63  PRO 63  62  62  PRO PRO D . n 
D 1 64  HIS 64  63  63  HIS HIS D . n 
D 1 65  PHE 65  64  64  PHE PHE D . n 
D 1 66  ASN 66  65  65  ASN ASN D . n 
D 1 67  PRO 67  66  66  PRO PRO D . n 
D 1 68  LEU 68  67  67  LEU LEU D . n 
D 1 69  SER 69  68  ?   ?   ?   D . n 
D 1 70  ARG 70  69  ?   ?   ?   D . n 
D 1 71  LYS 71  70  ?   ?   ?   D . n 
D 1 72  HIS 72  71  ?   ?   ?   D . n 
D 1 73  GLY 73  72  ?   ?   ?   D . n 
D 1 74  GLY 74  73  ?   ?   ?   D . n 
D 1 75  PRO 75  74  ?   ?   ?   D . n 
D 1 76  LYS 76  75  ?   ?   ?   D . n 
D 1 77  ASP 77  76  ?   ?   ?   D . n 
D 1 78  GLU 78  77  ?   ?   ?   D . n 
D 1 79  GLU 79  78  ?   ?   ?   D . n 
D 1 80  ARG 80  79  79  ARG ARG D . n 
D 1 81  HIS 81  80  80  HIS HIS D . n 
D 1 82  VAL 82  81  81  VAL VAL D . n 
D 1 83  GLY 83  82  82  GLY GLY D . n 
D 1 84  ASP 84  83  83  ASP ASP D . n 
D 1 85  LEU 85  84  84  LEU LEU D . n 
D 1 86  GLY 86  85  85  GLY GLY D . n 
D 1 87  ASN 87  86  86  ASN ASN D . n 
D 1 88  VAL 88  87  87  VAL VAL D . n 
D 1 89  THR 89  88  88  THR THR D . n 
D 1 90  ALA 90  89  89  ALA ALA D . n 
D 1 91  ASP 91  90  90  ASP ASP D . n 
D 1 92  LYS 92  91  91  LYS LYS D . n 
D 1 93  ASP 93  92  92  ASP ASP D . n 
D 1 94  GLY 94  93  93  GLY GLY D . n 
D 1 95  VAL 95  94  94  VAL VAL D . n 
D 1 96  ALA 96  95  95  ALA ALA D . n 
D 1 97  ASP 97  96  96  ASP ASP D . n 
D 1 98  VAL 98  97  97  VAL VAL D . n 
D 1 99  SER 99  98  98  SER SER D . n 
D 1 100 ILE 100 99  99  ILE ILE D . n 
D 1 101 GLU 101 100 100 GLU GLU D . n 
D 1 102 ASP 102 101 101 ASP ASP D . n 
D 1 103 SER 103 102 102 SER SER D . n 
D 1 104 VAL 104 103 103 VAL VAL D . n 
D 1 105 ILE 105 104 104 ILE ILE D . n 
D 1 106 SER 106 105 105 SER SER D . n 
D 1 107 LEU 107 106 106 LEU LEU D . n 
D 1 108 SER 108 107 107 SER SER D . n 
D 1 109 GLY 109 108 108 GLY GLY D . n 
D 1 110 ASP 110 109 109 ASP ASP D . n 
D 1 111 HIS 111 110 110 HIS HIS D . n 
D 1 112 CYS 112 111 111 CYS CYS D . n 
D 1 113 ILE 113 112 112 ILE ILE D . n 
D 1 114 ILE 114 113 113 ILE ILE D . n 
D 1 115 GLY 115 114 114 GLY GLY D . n 
D 1 116 ARG 116 115 115 ARG ARG D . n 
D 1 117 THR 117 116 116 THR THR D . n 
D 1 118 LEU 118 117 117 LEU LEU D . n 
D 1 119 VAL 119 118 118 VAL VAL D . n 
D 1 120 VAL 120 119 119 VAL VAL D . n 
D 1 121 HIS 121 120 120 HIS HIS D . n 
D 1 122 GLU 122 121 121 GLU GLU D . n 
D 1 123 LYS 123 122 122 LYS LYS D . n 
D 1 124 ALA 124 123 123 ALA ALA D . n 
D 1 125 ASP 125 124 124 ASP ASP D . n 
D 1 126 ASP 126 125 ?   ?   ?   D . n 
D 1 127 LEU 127 126 ?   ?   ?   D . n 
D 1 128 GLY 128 127 ?   ?   ?   D . n 
D 1 129 LYS 129 128 ?   ?   ?   D . n 
D 1 130 GLY 130 129 ?   ?   ?   D . n 
D 1 131 GLY 131 130 ?   ?   ?   D . n 
D 1 132 ASN 132 131 ?   ?   ?   D . n 
D 1 133 GLU 133 132 ?   ?   ?   D . n 
D 1 134 GLU 134 133 ?   ?   ?   D . n 
D 1 135 SER 135 134 ?   ?   ?   D . n 
D 1 136 THR 136 135 ?   ?   ?   D . n 
D 1 137 LYS 137 136 ?   ?   ?   D . n 
D 1 138 THR 138 137 ?   ?   ?   D . n 
D 1 139 GLY 139 138 ?   ?   ?   D . n 
D 1 140 ASN 140 139 ?   ?   ?   D . n 
D 1 141 ALA 141 140 ?   ?   ?   D . n 
D 1 142 GLY 142 141 ?   ?   ?   D . n 
D 1 143 SER 143 142 142 SER SER D . n 
D 1 144 ARG 144 143 143 ARG ARG D . n 
D 1 145 LEU 145 144 144 LEU LEU D . n 
D 1 146 ALA 146 145 145 ALA ALA D . n 
D 1 147 CYS 147 146 146 CYS CYS D . n 
D 1 148 GLY 148 147 147 GLY GLY D . n 
D 1 149 VAL 149 148 148 VAL VAL D . n 
D 1 150 ILE 150 149 149 ILE ILE D . n 
D 1 151 GLY 151 150 150 GLY GLY D . n 
D 1 152 ILE 152 151 151 ILE ILE D . n 
D 1 153 ALA 153 152 152 ALA ALA D . n 
D 1 154 GLN 154 153 153 GLN GLN D . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
E 2 ZN  1  155  155  ZN  ZN  A . 
F 2 ZN  1  155  155  ZN  ZN  B . 
G 3 HOH 1  2001 2001 HOH HOH A . 
G 3 HOH 2  2002 2002 HOH HOH A . 
G 3 HOH 3  2003 2003 HOH HOH A . 
G 3 HOH 4  2004 2004 HOH HOH A . 
G 3 HOH 5  2005 2005 HOH HOH A . 
G 3 HOH 6  2006 2006 HOH HOH A . 
G 3 HOH 7  2007 2007 HOH HOH A . 
G 3 HOH 8  2008 2008 HOH HOH A . 
G 3 HOH 9  2009 2009 HOH HOH A . 
G 3 HOH 10 2010 2010 HOH HOH A . 
G 3 HOH 11 2011 2011 HOH HOH A . 
G 3 HOH 12 2012 2012 HOH HOH A . 
G 3 HOH 13 2013 2013 HOH HOH A . 
G 3 HOH 14 2014 2014 HOH HOH A . 
G 3 HOH 15 2015 2015 HOH HOH A . 
G 3 HOH 16 2016 2016 HOH HOH A . 
G 3 HOH 17 2017 2017 HOH HOH A . 
G 3 HOH 18 2018 2018 HOH HOH A . 
G 3 HOH 19 2019 2019 HOH HOH A . 
G 3 HOH 20 2020 2020 HOH HOH A . 
G 3 HOH 21 2021 2021 HOH HOH A . 
G 3 HOH 22 2022 2022 HOH HOH A . 
G 3 HOH 23 2023 2023 HOH HOH A . 
G 3 HOH 24 2024 2024 HOH HOH A . 
G 3 HOH 25 2025 2025 HOH HOH A . 
G 3 HOH 26 2026 2026 HOH HOH A . 
G 3 HOH 27 2027 2027 HOH HOH A . 
G 3 HOH 28 2028 2028 HOH HOH A . 
G 3 HOH 29 2029 2029 HOH HOH A . 
G 3 HOH 30 2030 2030 HOH HOH A . 
G 3 HOH 31 2031 2031 HOH HOH A . 
G 3 HOH 32 2032 2032 HOH HOH A . 
G 3 HOH 33 2033 2033 HOH HOH A . 
G 3 HOH 34 2034 2034 HOH HOH A . 
G 3 HOH 35 2035 2035 HOH HOH A . 
G 3 HOH 36 2036 2036 HOH HOH A . 
G 3 HOH 37 2037 2037 HOH HOH A . 
G 3 HOH 38 2038 2038 HOH HOH A . 
G 3 HOH 39 2039 2039 HOH HOH A . 
G 3 HOH 40 2040 2040 HOH HOH A . 
G 3 HOH 41 2041 2041 HOH HOH A . 
G 3 HOH 42 2042 2042 HOH HOH A . 
G 3 HOH 43 2043 2043 HOH HOH A . 
G 3 HOH 44 2044 2044 HOH HOH A . 
G 3 HOH 45 2045 2045 HOH HOH A . 
G 3 HOH 46 2046 2046 HOH HOH A . 
G 3 HOH 47 2047 2047 HOH HOH A . 
G 3 HOH 48 2048 2048 HOH HOH A . 
G 3 HOH 49 2049 2049 HOH HOH A . 
G 3 HOH 50 2050 2050 HOH HOH A . 
G 3 HOH 51 2051 2051 HOH HOH A . 
G 3 HOH 52 2052 2052 HOH HOH A . 
G 3 HOH 53 2053 2053 HOH HOH A . 
G 3 HOH 54 2054 2054 HOH HOH A . 
G 3 HOH 55 2055 2055 HOH HOH A . 
G 3 HOH 56 2056 2056 HOH HOH A . 
G 3 HOH 57 2057 2057 HOH HOH A . 
G 3 HOH 58 2058 2058 HOH HOH A . 
G 3 HOH 59 2059 2059 HOH HOH A . 
G 3 HOH 60 2060 2060 HOH HOH A . 
G 3 HOH 61 2061 2061 HOH HOH A . 
G 3 HOH 62 2062 2062 HOH HOH A . 
G 3 HOH 63 2063 2063 HOH HOH A . 
G 3 HOH 64 2064 2064 HOH HOH A . 
G 3 HOH 65 2065 2065 HOH HOH A . 
G 3 HOH 66 2066 2066 HOH HOH A . 
G 3 HOH 67 2067 2067 HOH HOH A . 
G 3 HOH 68 2068 2068 HOH HOH A . 
G 3 HOH 69 2069 2069 HOH HOH A . 
G 3 HOH 70 2070 2070 HOH HOH A . 
G 3 HOH 71 2071 2071 HOH HOH A . 
G 3 HOH 72 2072 2072 HOH HOH A . 
G 3 HOH 73 2073 2073 HOH HOH A . 
G 3 HOH 74 2074 2074 HOH HOH A . 
G 3 HOH 75 2075 2075 HOH HOH A . 
G 3 HOH 76 2076 2076 HOH HOH A . 
G 3 HOH 77 2077 2077 HOH HOH A . 
G 3 HOH 78 2078 2078 HOH HOH A . 
G 3 HOH 79 2079 2079 HOH HOH A . 
G 3 HOH 80 2080 2080 HOH HOH A . 
G 3 HOH 81 2081 2081 HOH HOH A . 
G 3 HOH 82 2082 2082 HOH HOH A . 
G 3 HOH 83 2083 2083 HOH HOH A . 
G 3 HOH 84 2084 2084 HOH HOH A . 
G 3 HOH 85 2085 2085 HOH HOH A . 
G 3 HOH 86 2086 2086 HOH HOH A . 
G 3 HOH 87 2087 2087 HOH HOH A . 
G 3 HOH 88 2088 2088 HOH HOH A . 
G 3 HOH 89 2089 2089 HOH HOH A . 
H 3 HOH 1  2001 2001 HOH HOH B . 
H 3 HOH 2  2002 2002 HOH HOH B . 
H 3 HOH 3  2003 2003 HOH HOH B . 
H 3 HOH 4  2004 2004 HOH HOH B . 
H 3 HOH 5  2005 2005 HOH HOH B . 
H 3 HOH 6  2006 2006 HOH HOH B . 
H 3 HOH 7  2007 2007 HOH HOH B . 
H 3 HOH 8  2008 2008 HOH HOH B . 
H 3 HOH 9  2009 2009 HOH HOH B . 
H 3 HOH 10 2010 2010 HOH HOH B . 
H 3 HOH 11 2011 2011 HOH HOH B . 
H 3 HOH 12 2012 2012 HOH HOH B . 
H 3 HOH 13 2013 2013 HOH HOH B . 
H 3 HOH 14 2014 2014 HOH HOH B . 
H 3 HOH 15 2015 2015 HOH HOH B . 
H 3 HOH 16 2016 2016 HOH HOH B . 
H 3 HOH 17 2017 2017 HOH HOH B . 
H 3 HOH 18 2018 2018 HOH HOH B . 
H 3 HOH 19 2019 2019 HOH HOH B . 
H 3 HOH 20 2020 2020 HOH HOH B . 
H 3 HOH 21 2021 2021 HOH HOH B . 
H 3 HOH 22 2022 2022 HOH HOH B . 
H 3 HOH 23 2023 2023 HOH HOH B . 
H 3 HOH 24 2024 2024 HOH HOH B . 
H 3 HOH 25 2025 2025 HOH HOH B . 
H 3 HOH 26 2026 2026 HOH HOH B . 
H 3 HOH 27 2027 2027 HOH HOH B . 
H 3 HOH 28 2028 2028 HOH HOH B . 
H 3 HOH 29 2029 2029 HOH HOH B . 
H 3 HOH 30 2030 2030 HOH HOH B . 
H 3 HOH 31 2031 2031 HOH HOH B . 
H 3 HOH 32 2032 2032 HOH HOH B . 
H 3 HOH 33 2033 2033 HOH HOH B . 
H 3 HOH 34 2034 2034 HOH HOH B . 
H 3 HOH 35 2035 2035 HOH HOH B . 
H 3 HOH 36 2036 2036 HOH HOH B . 
H 3 HOH 37 2037 2037 HOH HOH B . 
H 3 HOH 38 2038 2038 HOH HOH B . 
H 3 HOH 39 2039 2039 HOH HOH B . 
H 3 HOH 40 2040 2040 HOH HOH B . 
H 3 HOH 41 2041 2041 HOH HOH B . 
H 3 HOH 42 2042 2042 HOH HOH B . 
H 3 HOH 43 2043 2043 HOH HOH B . 
H 3 HOH 44 2044 2044 HOH HOH B . 
H 3 HOH 45 2045 2045 HOH HOH B . 
H 3 HOH 46 2046 2046 HOH HOH B . 
H 3 HOH 47 2047 2047 HOH HOH B . 
H 3 HOH 48 2048 2048 HOH HOH B . 
H 3 HOH 49 2049 2049 HOH HOH B . 
H 3 HOH 50 2050 2050 HOH HOH B . 
H 3 HOH 51 2051 2051 HOH HOH B . 
H 3 HOH 52 2052 2052 HOH HOH B . 
H 3 HOH 53 2053 2053 HOH HOH B . 
H 3 HOH 54 2054 2054 HOH HOH B . 
H 3 HOH 55 2055 2055 HOH HOH B . 
H 3 HOH 56 2056 2056 HOH HOH B . 
H 3 HOH 57 2057 2057 HOH HOH B . 
H 3 HOH 58 2058 2058 HOH HOH B . 
H 3 HOH 59 2059 2059 HOH HOH B . 
H 3 HOH 60 2060 2060 HOH HOH B . 
H 3 HOH 61 2061 2061 HOH HOH B . 
H 3 HOH 62 2062 2062 HOH HOH B . 
H 3 HOH 63 2063 2063 HOH HOH B . 
H 3 HOH 64 2064 2064 HOH HOH B . 
H 3 HOH 65 2065 2065 HOH HOH B . 
H 3 HOH 66 2066 2066 HOH HOH B . 
H 3 HOH 67 2067 2067 HOH HOH B . 
H 3 HOH 68 2068 2068 HOH HOH B . 
H 3 HOH 69 2069 2069 HOH HOH B . 
H 3 HOH 70 2070 2070 HOH HOH B . 
H 3 HOH 71 2071 2071 HOH HOH B . 
H 3 HOH 72 2072 2072 HOH HOH B . 
H 3 HOH 73 2073 2073 HOH HOH B . 
H 3 HOH 74 2074 2074 HOH HOH B . 
H 3 HOH 75 2075 2075 HOH HOH B . 
H 3 HOH 76 2076 2076 HOH HOH B . 
H 3 HOH 77 2077 2077 HOH HOH B . 
H 3 HOH 78 2078 2078 HOH HOH B . 
H 3 HOH 79 2079 2079 HOH HOH B . 
H 3 HOH 80 2080 2080 HOH HOH B . 
H 3 HOH 81 2081 2081 HOH HOH B . 
H 3 HOH 82 2082 2082 HOH HOH B . 
H 3 HOH 83 2083 2083 HOH HOH B . 
H 3 HOH 84 2084 2084 HOH HOH B . 
H 3 HOH 85 2085 2085 HOH HOH B . 
H 3 HOH 86 2086 2086 HOH HOH B . 
H 3 HOH 87 2087 2087 HOH HOH B . 
H 3 HOH 88 2088 2088 HOH HOH B . 
H 3 HOH 89 2089 2089 HOH HOH B . 
H 3 HOH 90 2090 2090 HOH HOH B . 
H 3 HOH 91 2091 2091 HOH HOH B . 
H 3 HOH 92 2092 2092 HOH HOH B . 
H 3 HOH 93 2093 2093 HOH HOH B . 
H 3 HOH 94 2094 2094 HOH HOH B . 
H 3 HOH 95 2095 2095 HOH HOH B . 
H 3 HOH 96 2096 2096 HOH HOH B . 
H 3 HOH 97 2097 2097 HOH HOH B . 
I 3 HOH 1  2001 2001 HOH HOH C . 
I 3 HOH 2  2002 2002 HOH HOH C . 
I 3 HOH 3  2003 2003 HOH HOH C . 
I 3 HOH 4  2004 2004 HOH HOH C . 
I 3 HOH 5  2005 2005 HOH HOH C . 
I 3 HOH 6  2006 2006 HOH HOH C . 
I 3 HOH 7  2007 2007 HOH HOH C . 
I 3 HOH 8  2008 2008 HOH HOH C . 
I 3 HOH 9  2009 2009 HOH HOH C . 
I 3 HOH 10 2010 2010 HOH HOH C . 
I 3 HOH 11 2011 2011 HOH HOH C . 
I 3 HOH 12 2012 2012 HOH HOH C . 
I 3 HOH 13 2013 2013 HOH HOH C . 
I 3 HOH 14 2014 2014 HOH HOH C . 
I 3 HOH 15 2015 2015 HOH HOH C . 
I 3 HOH 16 2016 2016 HOH HOH C . 
I 3 HOH 17 2017 2017 HOH HOH C . 
I 3 HOH 18 2018 2018 HOH HOH C . 
I 3 HOH 19 2019 2019 HOH HOH C . 
I 3 HOH 20 2020 2020 HOH HOH C . 
I 3 HOH 21 2021 2021 HOH HOH C . 
I 3 HOH 22 2022 2022 HOH HOH C . 
I 3 HOH 23 2023 2023 HOH HOH C . 
I 3 HOH 24 2024 2024 HOH HOH C . 
I 3 HOH 25 2025 2025 HOH HOH C . 
I 3 HOH 26 2026 2026 HOH HOH C . 
I 3 HOH 27 2027 2027 HOH HOH C . 
I 3 HOH 28 2028 2028 HOH HOH C . 
I 3 HOH 29 2029 2029 HOH HOH C . 
I 3 HOH 30 2030 2030 HOH HOH C . 
I 3 HOH 31 2031 2031 HOH HOH C . 
I 3 HOH 32 2032 2032 HOH HOH C . 
I 3 HOH 33 2033 2033 HOH HOH C . 
I 3 HOH 34 2034 2034 HOH HOH C . 
I 3 HOH 35 2035 2035 HOH HOH C . 
I 3 HOH 36 2036 2036 HOH HOH C . 
I 3 HOH 37 2037 2037 HOH HOH C . 
I 3 HOH 38 2038 2038 HOH HOH C . 
I 3 HOH 39 2039 2039 HOH HOH C . 
I 3 HOH 40 2040 2040 HOH HOH C . 
I 3 HOH 41 2041 2041 HOH HOH C . 
I 3 HOH 42 2042 2042 HOH HOH C . 
I 3 HOH 43 2043 2043 HOH HOH C . 
I 3 HOH 44 2044 2044 HOH HOH C . 
I 3 HOH 45 2045 2045 HOH HOH C . 
I 3 HOH 46 2046 2046 HOH HOH C . 
I 3 HOH 47 2047 2047 HOH HOH C . 
I 3 HOH 48 2048 2048 HOH HOH C . 
I 3 HOH 49 2049 2049 HOH HOH C . 
I 3 HOH 50 2050 2050 HOH HOH C . 
I 3 HOH 51 2051 2051 HOH HOH C . 
I 3 HOH 52 2052 2052 HOH HOH C . 
I 3 HOH 53 2053 2053 HOH HOH C . 
I 3 HOH 54 2054 2054 HOH HOH C . 
I 3 HOH 55 2055 2055 HOH HOH C . 
I 3 HOH 56 2056 2056 HOH HOH C . 
I 3 HOH 57 2057 2057 HOH HOH C . 
I 3 HOH 58 2058 2058 HOH HOH C . 
I 3 HOH 59 2059 2059 HOH HOH C . 
I 3 HOH 60 2060 2060 HOH HOH C . 
I 3 HOH 61 2061 2061 HOH HOH C . 
I 3 HOH 62 2062 2062 HOH HOH C . 
I 3 HOH 63 2063 2063 HOH HOH C . 
I 3 HOH 64 2064 2064 HOH HOH C . 
I 3 HOH 65 2065 2065 HOH HOH C . 
I 3 HOH 66 2066 2066 HOH HOH C . 
J 3 HOH 1  2001 2001 HOH HOH D . 
J 3 HOH 2  2002 2002 HOH HOH D . 
J 3 HOH 3  2003 2003 HOH HOH D . 
J 3 HOH 4  2004 2004 HOH HOH D . 
J 3 HOH 5  2005 2005 HOH HOH D . 
J 3 HOH 6  2006 2006 HOH HOH D . 
J 3 HOH 7  2007 2007 HOH HOH D . 
J 3 HOH 8  2008 2008 HOH HOH D . 
J 3 HOH 9  2009 2009 HOH HOH D . 
J 3 HOH 10 2010 2010 HOH HOH D . 
J 3 HOH 11 2011 2011 HOH HOH D . 
J 3 HOH 12 2012 2012 HOH HOH D . 
J 3 HOH 13 2013 2013 HOH HOH D . 
J 3 HOH 14 2014 2014 HOH HOH D . 
J 3 HOH 15 2015 2015 HOH HOH D . 
J 3 HOH 16 2016 2016 HOH HOH D . 
J 3 HOH 17 2017 2017 HOH HOH D . 
J 3 HOH 18 2018 2018 HOH HOH D . 
J 3 HOH 19 2019 2019 HOH HOH D . 
J 3 HOH 20 2020 2020 HOH HOH D . 
J 3 HOH 21 2021 2021 HOH HOH D . 
J 3 HOH 22 2022 2022 HOH HOH D . 
J 3 HOH 23 2023 2023 HOH HOH D . 
J 3 HOH 24 2024 2024 HOH HOH D . 
J 3 HOH 25 2025 2025 HOH HOH D . 
J 3 HOH 26 2026 2026 HOH HOH D . 
J 3 HOH 27 2027 2027 HOH HOH D . 
J 3 HOH 28 2028 2028 HOH HOH D . 
J 3 HOH 29 2029 2029 HOH HOH D . 
J 3 HOH 30 2030 2030 HOH HOH D . 
J 3 HOH 31 2031 2031 HOH HOH D . 
J 3 HOH 32 2032 2032 HOH HOH D . 
J 3 HOH 33 2033 2033 HOH HOH D . 
J 3 HOH 34 2034 2034 HOH HOH D . 
J 3 HOH 35 2035 2035 HOH HOH D . 
J 3 HOH 36 2036 2036 HOH HOH D . 
J 3 HOH 37 2037 2037 HOH HOH D . 
J 3 HOH 38 2038 2038 HOH HOH D . 
J 3 HOH 39 2039 2039 HOH HOH D . 
J 3 HOH 40 2040 2040 HOH HOH D . 
J 3 HOH 41 2041 2041 HOH HOH D . 
J 3 HOH 42 2042 2042 HOH HOH D . 
J 3 HOH 43 2043 2043 HOH HOH D . 
J 3 HOH 44 2044 2044 HOH HOH D . 
J 3 HOH 45 2045 2045 HOH HOH D . 
J 3 HOH 46 2046 2046 HOH HOH D . 
J 3 HOH 47 2047 2047 HOH HOH D . 
J 3 HOH 48 2048 2048 HOH HOH D . 
J 3 HOH 49 2049 2049 HOH HOH D . 
J 3 HOH 50 2050 2050 HOH HOH D . 
J 3 HOH 51 2051 2051 HOH HOH D . 
J 3 HOH 52 2052 2052 HOH HOH D . 
J 3 HOH 53 2053 2053 HOH HOH D . 
J 3 HOH 54 2054 2054 HOH HOH D . 
J 3 HOH 55 2055 2055 HOH HOH D . 
J 3 HOH 56 2056 2056 HOH HOH D . 
J 3 HOH 57 2057 2057 HOH HOH D . 
J 3 HOH 58 2058 2058 HOH HOH D . 
J 3 HOH 59 2059 2059 HOH HOH D . 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA dimeric 2 
2 author_and_software_defined_assembly PISA dimeric 2 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,E,F,G,H 
2 1 C,D,I,J     
# 
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)' 1550  ? 
1 MORE         -13.0 ? 
1 'SSA (A^2)'  13740 ? 
2 'ABSA (A^2)' 1410  ? 
2 MORE         -12.0 ? 
2 'SSA (A^2)'  11470 ? 
# 
_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 72 ? A HIS 71 ? 1_555 ZN ? E ZN . ? A ZN 155 ? 1_555 OD1 ? A ASP 84 ? A ASP 83 ? 1_555 75.2  ? 
2  ND1 ? A HIS 72 ? A HIS 71 ? 1_555 ZN ? E ZN . ? A ZN 155 ? 1_555 ND1 ? A HIS 64 ? A HIS 63 ? 1_555 119.9 ? 
3  OD1 ? A ASP 84 ? A ASP 83 ? 1_555 ZN ? E ZN . ? A ZN 155 ? 1_555 ND1 ? A HIS 64 ? A HIS 63 ? 1_555 131.8 ? 
4  ND1 ? A HIS 72 ? A HIS 71 ? 1_555 ZN ? E ZN . ? A ZN 155 ? 1_555 ND1 ? A HIS 81 ? A HIS 80 ? 1_555 122.1 ? 
5  OD1 ? A ASP 84 ? A ASP 83 ? 1_555 ZN ? E ZN . ? A ZN 155 ? 1_555 ND1 ? A HIS 81 ? A HIS 80 ? 1_555 113.8 ? 
6  ND1 ? A HIS 64 ? A HIS 63 ? 1_555 ZN ? E ZN . ? A ZN 155 ? 1_555 ND1 ? A HIS 81 ? A HIS 80 ? 1_555 96.5  ? 
7  OD1 ? B ASP 84 ? B ASP 83 ? 1_555 ZN ? F ZN . ? B ZN 155 ? 1_555 ND1 ? B HIS 72 ? B HIS 71 ? 1_555 91.2  ? 
8  OD1 ? B ASP 84 ? B ASP 83 ? 1_555 ZN ? F ZN . ? B ZN 155 ? 1_555 ND1 ? B HIS 81 ? B HIS 80 ? 1_555 109.1 ? 
9  ND1 ? B HIS 72 ? B HIS 71 ? 1_555 ZN ? F ZN . ? B ZN 155 ? 1_555 ND1 ? B HIS 81 ? B HIS 80 ? 1_555 121.4 ? 
10 OD1 ? B ASP 84 ? B ASP 83 ? 1_555 ZN ? F ZN . ? B ZN 155 ? 1_555 ND1 ? B HIS 64 ? B HIS 63 ? 1_555 110.9 ? 
11 ND1 ? B HIS 72 ? B HIS 71 ? 1_555 ZN ? F ZN . ? B ZN 155 ? 1_555 ND1 ? B HIS 64 ? B HIS 63 ? 1_555 125.8 ? 
12 ND1 ? B HIS 81 ? B HIS 80 ? 1_555 ZN ? F ZN . ? B ZN 155 ? 1_555 ND1 ? B HIS 64 ? B HIS 63 ? 1_555 97.7  ? 
# 
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 2003-05-08 
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         ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' Advisory                    
2 2 'Structure model' 'Refinement description'    
3 2 'Structure model' 'Version format compliance' 
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][3] 
'X-RAY DIFFRACTION' 1 ? refined -13.3230 -2.5300 20.7480 0.1922 0.1108 0.1997 -0.0052 0.0202  0.0057 1.2765 0.7852 1.9569 0.1158  
0.5674  0.1294  0.0469  0.1603  -0.0890 -0.0800 -0.0491 -0.0227 0.0730  0.0248  0.0021  
'X-RAY DIFFRACTION' 2 ? refined -3.8120  2.5550  46.5030 0.1585 0.1559 0.2102 -0.0249 0.0079  0.0205 1.1759 0.6777 1.9011 -0.0593 
0.2634  -0.0656 -0.0044 -0.2088 0.0367  0.0104  0.0213  -0.0295 0.0043  0.0004  -0.0169 
'X-RAY DIFFRACTION' 3 ? refined 28.9140  11.7480 30.4600 0.1839 0.0101 0.2097 -0.0400 0.0079  0.0152 2.0460 0.9230 2.9785 0.3265  
-0.1157 0.0417  0.0364  -0.2785 0.0774  -0.0237 -0.0181 -0.0128 -0.0973 0.2112  -0.0183 
'X-RAY DIFFRACTION' 4 ? refined 22.7840  5.2450  8.5970  0.2253 0.0122 0.2179 -0.0273 -0.0071 0.0070 1.6552 1.4424 3.2502 0.0299  
0.2515  0.0485  0.0116  0.2408  -0.0718 -0.0622 -0.0191 0.0385  0.0728  -0.0322 0.0075  
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
'X-RAY DIFFRACTION' 1 1 A 1 ? ? A 153 ? ? ? ? 
'X-RAY DIFFRACTION' 2 2 B 0 ? ? B 153 ? ? ? ? 
'X-RAY DIFFRACTION' 3 3 C 1 ? ? C 153 ? ? ? ? 
'X-RAY DIFFRACTION' 4 4 D 1 ? ? D 153 ? ? ? ? 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
REFMAC   refinement       5.0 ? 1 
HKL-2000 'data reduction' .   ? 2 
HKL-2000 'data scaling'   .   ? 3 
MOLREP   phasing          .   ? 4 
# 
_pdbx_database_remark.id     700 
_pdbx_database_remark.text   
;
SHEET
DETERMINATION METHOD: DSSP
THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS
BELOW IS ACTUALLY AN 10-STRANDED BARREL THIS IS REPRESENTED BY
A 11-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
ARE IDENTICAL.
;
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O   B HOH 2069 ? ? O   C HOH 2049 ? ? 1.98 
2 1 NH2 C ARG 79   ? ? OD1 C ASP 101  ? ? 2.01 
3 1 OD2 B ASP 124  ? ? O   B HOH 2078 ? ? 2.17 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    B 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     2013 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    B 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     2026 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   2_556 
_pdbx_validate_symm_contact.dist              2.19 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1  1 CB A ASP 76  ? ? CG A ASP 76  ? ? OD2 A ASP 76  ? ? 123.73 118.30 5.43  0.90 N 
2  1 CB A ASP 101 ? ? CG A ASP 101 ? ? OD2 A ASP 101 ? ? 123.99 118.30 5.69  0.90 N 
3  1 CB A ASP 109 ? ? CG A ASP 109 ? ? OD2 A ASP 109 ? ? 125.18 118.30 6.88  0.90 N 
4  1 NE A ARG 115 ? ? CZ A ARG 115 ? ? NH1 A ARG 115 ? ? 117.06 120.30 -3.24 0.50 N 
5  1 NE B ARG 143 ? ? CZ B ARG 143 ? ? NH2 B ARG 143 ? ? 116.87 120.30 -3.43 0.50 N 
6  1 CB C ASP 11  ? ? CG C ASP 11  ? ? OD2 C ASP 11  ? ? 124.46 118.30 6.16  0.90 N 
7  1 CA C LEU 38  ? ? CB C LEU 38  ? ? CG  C LEU 38  ? ? 131.19 115.30 15.89 2.30 N 
8  1 CB C ASP 52  ? ? CG C ASP 52  ? ? OD1 C ASP 52  ? ? 123.86 118.30 5.56  0.90 N 
9  1 CB C ASP 124 ? ? CG C ASP 124 ? ? OD2 C ASP 124 ? ? 123.81 118.30 5.51  0.90 N 
10 1 CB D ASP 124 ? ? CG D ASP 124 ? ? OD2 D ASP 124 ? ? 123.96 118.30 5.66  0.90 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 LYS B 136 ? ? -125.50 -53.66  
2 1 ASN C 65  ? ? -159.78 87.13   
3 1 ASP C 90  ? ? -76.29  -168.92 
4 1 ASN D 65  ? ? -152.05 72.96   
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 23  ? CG  ? A LYS 24  CG  
2  1 Y 1 A LYS 23  ? CD  ? A LYS 24  CD  
3  1 Y 1 A LYS 23  ? CE  ? A LYS 24  CE  
4  1 Y 1 A LYS 23  ? NZ  ? A LYS 24  NZ  
5  1 Y 1 A GLU 24  ? CD  ? A GLU 25  CD  
6  1 Y 1 A GLU 24  ? OE1 ? A GLU 25  OE1 
7  1 Y 1 A GLU 24  ? OE2 ? A GLU 25  OE2 
8  1 Y 1 A LYS 30  ? CG  ? A LYS 31  CG  
9  1 Y 1 A LYS 30  ? CD  ? A LYS 31  CD  
10 1 Y 1 A LYS 30  ? CE  ? A LYS 31  CE  
11 1 Y 1 A LYS 30  ? NZ  ? A LYS 31  NZ  
12 1 Y 1 A LYS 70  ? CE  ? A LYS 71  CE  
13 1 Y 1 A LYS 70  ? NZ  ? A LYS 71  NZ  
14 1 Y 1 A GLU 132 ? CG  ? A GLU 133 CG  
15 1 Y 1 A GLU 132 ? CD  ? A GLU 133 CD  
16 1 Y 1 A GLU 132 ? OE1 ? A GLU 133 OE1 
17 1 Y 1 A GLU 132 ? OE2 ? A GLU 133 OE2 
18 1 Y 1 A LYS 136 ? NZ  ? A LYS 137 NZ  
19 1 Y 1 B LYS 9   ? CD  ? B LYS 10  CD  
20 1 Y 1 B LYS 9   ? CE  ? B LYS 10  CE  
21 1 Y 1 B LYS 9   ? NZ  ? B LYS 10  NZ  
22 1 Y 1 B LYS 75  ? CE  ? B LYS 76  CE  
23 1 Y 1 B LYS 75  ? NZ  ? B LYS 76  NZ  
24 1 Y 1 B GLU 77  ? CG  ? B GLU 78  CG  
25 1 Y 1 B GLU 77  ? CD  ? B GLU 78  CD  
26 1 Y 1 B GLU 77  ? OE1 ? B GLU 78  OE1 
27 1 Y 1 B GLU 77  ? OE2 ? B GLU 78  OE2 
28 1 Y 1 B LYS 91  ? NZ  ? B LYS 92  NZ  
29 1 Y 1 B LYS 122 ? CE  ? B LYS 123 CE  
30 1 Y 1 B LYS 122 ? NZ  ? B LYS 123 NZ  
31 1 Y 1 C SER 68  ? C   ? C SER 69  C   
32 1 Y 1 C SER 68  ? O   ? C SER 69  O   
33 1 Y 1 C SER 68  ? OG  ? C SER 69  OG  
34 1 Y 1 C HIS 80  ? CG  ? C HIS 81  CG  
35 1 Y 1 C HIS 80  ? ND1 ? C HIS 81  ND1 
36 1 Y 1 C HIS 80  ? CD2 ? C HIS 81  CD2 
37 1 Y 1 C HIS 80  ? CE1 ? C HIS 81  CE1 
38 1 Y 1 C HIS 80  ? NE2 ? C HIS 81  NE2 
39 1 Y 1 C LYS 91  ? CE  ? C LYS 92  CE  
40 1 Y 1 C LYS 91  ? NZ  ? C LYS 92  NZ  
41 1 Y 1 C LYS 122 ? CD  ? C LYS 123 CD  
42 1 Y 1 C LYS 122 ? CE  ? C LYS 123 CE  
43 1 Y 1 C LYS 122 ? NZ  ? C LYS 123 NZ  
44 1 Y 1 D HIS 80  ? C   ? D HIS 81  C   
45 1 Y 1 D HIS 80  ? O   ? D HIS 81  O   
46 1 Y 1 D HIS 80  ? CB  ? D HIS 81  CB  
47 1 Y 1 D HIS 80  ? CG  ? D HIS 81  CG  
48 1 Y 1 D HIS 80  ? ND1 ? D HIS 81  ND1 
49 1 Y 1 D HIS 80  ? CD2 ? D HIS 81  CD2 
50 1 Y 1 D HIS 80  ? CE1 ? D HIS 81  CE1 
51 1 Y 1 D HIS 80  ? NE2 ? D HIS 81  NE2 
52 1 Y 1 D ASP 83  ? CG  ? D ASP 84  CG  
53 1 Y 1 D ASP 83  ? OD1 ? D ASP 84  OD1 
54 1 Y 1 D ASP 83  ? OD2 ? D ASP 84  OD2 
55 1 Y 1 D LYS 91  ? CG  ? D LYS 92  CG  
56 1 Y 1 D LYS 91  ? CD  ? D LYS 92  CD  
57 1 Y 1 D LYS 91  ? CE  ? D LYS 92  CE  
58 1 Y 1 D LYS 91  ? NZ  ? D LYS 92  NZ  
# 
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 C ACE 0   ? C ACE 1   
3  1 Y 1 C ARG 69  ? C ARG 70  
4  1 Y 1 C LYS 70  ? C LYS 71  
5  1 Y 1 C HIS 71  ? C HIS 72  
6  1 Y 1 C GLY 72  ? C GLY 73  
7  1 Y 1 C GLY 73  ? C GLY 74  
8  1 Y 1 C PRO 74  ? C PRO 75  
9  1 Y 1 C LYS 75  ? C LYS 76  
10 1 Y 1 C ASP 76  ? C ASP 77  
11 1 Y 1 C GLU 77  ? C GLU 78  
12 1 Y 1 C GLU 78  ? C GLU 79  
13 1 Y 1 C ASP 125 ? C ASP 126 
14 1 Y 1 C LEU 126 ? C LEU 127 
15 1 Y 1 C GLY 127 ? C GLY 128 
16 1 Y 1 C LYS 128 ? C LYS 129 
17 1 Y 1 C GLY 129 ? C GLY 130 
18 1 Y 1 C GLY 130 ? C GLY 131 
19 1 Y 1 C ASN 131 ? C ASN 132 
20 1 Y 1 C GLU 132 ? C GLU 133 
21 1 Y 1 C GLU 133 ? C GLU 134 
22 1 Y 1 C SER 134 ? C SER 135 
23 1 Y 1 C THR 135 ? C THR 136 
24 1 Y 1 C LYS 136 ? C LYS 137 
25 1 Y 1 C THR 137 ? C THR 138 
26 1 Y 1 C GLY 138 ? C GLY 139 
27 1 Y 1 C ASN 139 ? C ASN 140 
28 1 Y 1 C ALA 140 ? C ALA 141 
29 1 Y 1 D ACE 0   ? D ACE 1   
30 1 Y 1 D SER 68  ? D SER 69  
31 1 Y 1 D ARG 69  ? D ARG 70  
32 1 Y 1 D LYS 70  ? D LYS 71  
33 1 Y 1 D HIS 71  ? D HIS 72  
34 1 Y 1 D GLY 72  ? D GLY 73  
35 1 Y 1 D GLY 73  ? D GLY 74  
36 1 Y 1 D PRO 74  ? D PRO 75  
37 1 Y 1 D LYS 75  ? D LYS 76  
38 1 Y 1 D ASP 76  ? D ASP 77  
39 1 Y 1 D GLU 77  ? D GLU 78  
40 1 Y 1 D GLU 78  ? D GLU 79  
41 1 Y 1 D ASP 125 ? D ASP 126 
42 1 Y 1 D LEU 126 ? D LEU 127 
43 1 Y 1 D GLY 127 ? D GLY 128 
44 1 Y 1 D LYS 128 ? D LYS 129 
45 1 Y 1 D GLY 129 ? D GLY 130 
46 1 Y 1 D GLY 130 ? D GLY 131 
47 1 Y 1 D ASN 131 ? D ASN 132 
48 1 Y 1 D GLU 132 ? D GLU 133 
49 1 Y 1 D GLU 133 ? D GLU 134 
50 1 Y 1 D SER 134 ? D SER 135 
51 1 Y 1 D THR 135 ? D THR 136 
52 1 Y 1 D LYS 136 ? D LYS 137 
53 1 Y 1 D THR 137 ? D THR 138 
54 1 Y 1 D GLY 138 ? D GLY 139 
55 1 Y 1 D ASN 139 ? D ASN 140 
56 1 Y 1 D ALA 140 ? D ALA 141 
57 1 Y 1 D GLY 141 ? D GLY 142 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION' ZN  
3 water      HOH 
# 
