HEADER CHAPERONE 08-AUG-16 5LO6
TITLE HSP90 WITH INDAZOLE DERIVATIVE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEAT SHOCK PROTEIN HSP 90-ALPHA;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: ATPASE DOMAIN (8-236);
COMPND 5 SYNONYM: HEAT SHOCK 86 KDA,HSP86,LIPOPOLYSACCHARIDE-ASSOCIATED
COMPND 6 PROTEIN 2,LPS-ASSOCIATED PROTEIN 2,RENAL CARCINOMA ANTIGEN NY-REN-38;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: HSP90AA1, HSP90A, HSPC1, HSPCA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CHAPERONE
EXPDTA X-RAY DIFFRACTION
AUTHOR U.GRAEDLER,M.AMARAL
REVDAT 3 10-JAN-24 5LO6 1 REMARK
REVDAT 2 23-JAN-19 5LO6 1 JRNL
REVDAT 1 29-NOV-17 5LO6 0
JRNL AUTH D.B.KOKH,M.AMARAL,J.BOMKE,U.GRADLER,D.MUSIL,H.P.BUCHSTALLER,
JRNL AUTH 2 M.K.DREYER,M.FRECH,M.LOWINSKI,F.VALLEE,M.BIANCIOTTO,A.RAK,
JRNL AUTH 3 R.C.WADE
JRNL TITL ESTIMATION OF DRUG-TARGET RESIDENCE TIMES BY TAU-RANDOM
JRNL TITL 2 ACCELERATION MOLECULAR DYNAMICS SIMULATIONS.
JRNL REF J CHEM THEORY COMPUT V. 14 3859 2018
JRNL REFN ISSN 1549-9626
JRNL PMID 29768913
JRNL DOI 10.1021/ACS.JCTC.8B00230
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.6
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.63
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 12350
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.193
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.217
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.820
REMARK 3 FREE R VALUE TEST SET COUNT : 595
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.010
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.63
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.76
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2893
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.1950
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2755
REMARK 3 BIN R VALUE (WORKING SET) : 0.1940
REMARK 3 BIN FREE R VALUE : 0.2260
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.77
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 138
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.000
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1626
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 33
REMARK 3 SOLVENT ATOMS : 13
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 81.38
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 86.06
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 6.19390
REMARK 3 B22 (A**2) : -4.95010
REMARK 3 B33 (A**2) : -1.24390
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.290
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.246
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.188
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.251
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.192
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.953
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 1689 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 2283 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 599 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 46 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 239 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 1689 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 229 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 1859 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.15
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.93
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 18.47
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 0.2688 14.8925 20.5022
REMARK 3 T TENSOR
REMARK 3 T11: -0.1988 T22: -0.2219
REMARK 3 T33: -0.1948 T12: 0.0162
REMARK 3 T13: 0.0621 T23: -0.0493
REMARK 3 L TENSOR
REMARK 3 L11: 5.8698 L22: 2.9590
REMARK 3 L33: 3.8575 L12: 1.0727
REMARK 3 L13: 0.2392 L23: 0.5382
REMARK 3 S TENSOR
REMARK 3 S11: 0.0173 S12: -0.1164 S13: -0.2396
REMARK 3 S21: -0.0082 S22: -0.0260 S23: -0.0162
REMARK 3 S31: 0.0122 S32: -0.0720 S33: 0.0087
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5LO6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-AUG-16.
REMARK 100 THE DEPOSITION ID IS D_1200001090.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-DEC-08
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X1A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12350
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 49.630
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.8
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.04100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.42200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 4EEH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: BIS-TRIS PROPAN, PH 6.5, 22% PEG 3350,
REMARK 280 0.2M NAF, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 33.88000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 45.60500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 49.63500
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 33.88000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 45.60500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 49.63500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 33.88000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 45.60500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 49.63500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 33.88000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 45.60500
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 49.63500
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10330 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 8
REMARK 465 ASP A 9
REMARK 465 GLN A 10
REMARK 465 PRO A 11
REMARK 465 MET A 12
REMARK 465 GLU A 13
REMARK 465 GLU A 14
REMARK 465 GLU A 15
REMARK 465 GLU A 16
REMARK 465 LYS A 224
REMARK 465 GLU A 225
REMARK 465 ARG A 226
REMARK 465 ASP A 227
REMARK 465 LYS A 228
REMARK 465 GLU A 229
REMARK 465 VAL A 230
REMARK 465 SER A 231
REMARK 465 ASP A 232
REMARK 465 ASP A 233
REMARK 465 GLU A 234
REMARK 465 ALA A 235
REMARK 465 GLU A 236
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 LEU A 64 CA CB CG CD1 CD2
REMARK 480 LEU A 70 CA CB CG CD1 CD2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 THR A 94 40.16 -109.11
REMARK 500 ALA A 166 -145.05 64.92
REMARK 500 PHE A 213 54.93 -119.47
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 70O A 301
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 I222 A= 67.7370 B= 91.1370 C= 99.1630 ALPHA= 90.0000 BETA= 90.0000
REMARK 999 MMA= 90.0000
DBREF 5LO6 A 9 236 UNP P07900 HS90A_HUMAN 9 236
SEQADV 5LO6 GLY A 8 UNP P07900 EXPRESSION TAG
SEQRES 1 A 229 GLY ASP GLN PRO MET GLU GLU GLU GLU VAL GLU THR PHE
SEQRES 2 A 229 ALA PHE GLN ALA GLU ILE ALA GLN LEU MET SER LEU ILE
SEQRES 3 A 229 ILE ASN THR PHE TYR SER ASN LYS GLU ILE PHE LEU ARG
SEQRES 4 A 229 GLU LEU ILE SER ASN SER SER ASP ALA LEU ASP LYS ILE
SEQRES 5 A 229 ARG TYR GLU SER LEU THR ASP PRO SER LYS LEU ASP SER
SEQRES 6 A 229 GLY LYS GLU LEU HIS ILE ASN LEU ILE PRO ASN LYS GLN
SEQRES 7 A 229 ASP ARG THR LEU THR ILE VAL ASP THR GLY ILE GLY MET
SEQRES 8 A 229 THR LYS ALA ASP LEU ILE ASN ASN LEU GLY THR ILE ALA
SEQRES 9 A 229 LYS SER GLY THR LYS ALA PHE MET GLU ALA LEU GLN ALA
SEQRES 10 A 229 GLY ALA ASP ILE SER MET ILE GLY GLN PHE GLY VAL GLY
SEQRES 11 A 229 PHE TYR SER ALA TYR LEU VAL ALA GLU LYS VAL THR VAL
SEQRES 12 A 229 ILE THR LYS HIS ASN ASP ASP GLU GLN TYR ALA TRP GLU
SEQRES 13 A 229 SER SER ALA GLY GLY SER PHE THR VAL ARG THR ASP THR
SEQRES 14 A 229 GLY GLU PRO MET GLY ARG GLY THR LYS VAL ILE LEU HIS
SEQRES 15 A 229 LEU LYS GLU ASP GLN THR GLU TYR LEU GLU GLU ARG ARG
SEQRES 16 A 229 ILE LYS GLU ILE VAL LYS LYS HIS SER GLN PHE ILE GLY
SEQRES 17 A 229 TYR PRO ILE THR LEU PHE VAL GLU LYS GLU ARG ASP LYS
SEQRES 18 A 229 GLU VAL SER ASP ASP GLU ALA GLU
HET 70O A 301 33
HETNAM 70O 3-(3,3-DIMETHYLBUTYL)-~{N}-METHYL-~{N}-[4-(1-
HETNAM 2 70O METHYLPIPERIDIN-4-YL)PHENYL]-6-OXIDANYL-2~{H}-
HETNAM 3 70O INDAZOLE-5-CARBOXAMIDE
FORMUL 2 70O C27 H36 N4 O2
FORMUL 3 HOH *13(H2 O)
HELIX 1 AA1 GLN A 23 THR A 36 1 14
HELIX 2 AA2 ASN A 40 GLU A 42 5 3
HELIX 3 AA3 ILE A 43 ASP A 66 1 24
HELIX 4 AA4 PRO A 67 GLY A 73 5 7
HELIX 5 AA5 THR A 99 LEU A 107 1 9
HELIX 6 AA6 GLY A 108 ALA A 124 1 17
HELIX 7 AA7 ASP A 127 GLY A 135 5 9
HELIX 8 AA8 VAL A 136 LEU A 143 5 8
HELIX 9 AA9 GLU A 192 LEU A 198 5 7
HELIX 10 AB1 GLU A 199 SER A 211 1 13
SHEET 1 AA1 8 GLU A 18 ALA A 21 0
SHEET 2 AA1 8 SER A 169 THR A 174 -1 O PHE A 170 N PHE A 20
SHEET 3 AA1 8 TYR A 160 SER A 164 -1 N ALA A 161 O ARG A 173
SHEET 4 AA1 8 ALA A 145 LYS A 153 -1 N VAL A 150 O TRP A 162
SHEET 5 AA1 8 GLY A 183 LEU A 190 -1 O ILE A 187 N THR A 149
SHEET 6 AA1 8 THR A 88 ASP A 93 -1 N LEU A 89 O LEU A 188
SHEET 7 AA1 8 ILE A 78 ASN A 83 -1 N ASN A 79 O VAL A 92
SHEET 8 AA1 8 ILE A 218 LEU A 220 1 O THR A 219 N LEU A 80
SITE 1 AC1 13 ASN A 51 ASP A 54 ALA A 55 ASP A 93
SITE 2 AC1 13 GLY A 97 MET A 98 ASN A 106 GLY A 135
SITE 3 AC1 13 PHE A 138 THR A 184 VAL A 186 HOH A 408
SITE 4 AC1 13 HOH A 409
CRYST1 67.760 91.210 99.270 90.00 90.00 90.00 I 2 2 2 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.014758 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010964 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010074 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
