HEADER HYDROLASE 02-DEC-09 3KX1
TITLE CATHEPSIN K IN COMPLEX WITH A SELECTIVE 2-CYANO-PYRIMIDINE INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CATHEPSIN K;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 115-329;
COMPND 5 SYNONYM: CATHEPSIN O, CATHEPSIN X, CATHEPSIN O2;
COMPND 6 EC: 3.4.22.38;
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 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: OVARY CELLS
KEYWDS CATHEPSIN K, ENZYME INHIBITOR, COVALENT REVERSIBLE INHIBITOR, DISEASE
KEYWDS 2 MUTATION, DISULFIDE BOND, GLYCOPROTEIN, HYDROLASE, LYSOSOME,
KEYWDS 3 PROTEASE, THIOL PROTEASE, ZYMOGEN
EXPDTA X-RAY DIFFRACTION
AUTHOR X.FRADERA,J.C.M.UITDEHAAG,M.VAN ZEELAND
REVDAT 3 03-APR-24 3KX1 1 REMARK
REVDAT 2 12-FEB-14 3KX1 1 JRNL VERSN
REVDAT 1 02-MAR-10 3KX1 0
JRNL AUTH Z.RANKOVIC,J.CAI,J.KERR,X.FRADERA,J.ROBINSON,A.MISTRY,
JRNL AUTH 2 E.HAMILTON,G.MCGARRY,F.ANDREWS,W.CAULFIELD,I.CUMMING,
JRNL AUTH 3 M.DEMPSTER,J.WALLER,P.SCULLION,I.MARTIN,A.MITCHELL,C.LONG,
JRNL AUTH 4 M.BAUGH,P.WESTWOOD,E.KINGHORN,J.BRUIN,W.HAMILTON,
JRNL AUTH 5 J.UITDEHAAG,M.VAN ZEELAND,D.POTIN,L.SANIERE,A.FOUQUET,
JRNL AUTH 6 F.CHEVALLIER,H.DERONZIER,C.DORLEANS,E.NICOLAI
JRNL TITL DESIGN AND OPTIMIZATION OF A SERIES OF NOVEL
JRNL TITL 2 2-CYANO-PYRIMIDINES AS CATHEPSIN K INHIBITORS
JRNL REF BIOORG.MED.CHEM.LETT. V. 20 1524 2010
JRNL REFN ISSN 0960-894X
JRNL PMID 20149657
JRNL DOI 10.1016/J.BMCL.2010.01.100
REMARK 2
REMARK 2 RESOLUTION. 1.51 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.51
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.03
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 70.1
REMARK 3 NUMBER OF REFLECTIONS : 22075
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) : 0.243
REMARK 3 R VALUE (WORKING SET) : 0.239
REMARK 3 FREE R VALUE : 0.306
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1167
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.51
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.55
REMARK 3 REFLECTION IN BIN (WORKING SET) : 157
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 6.78
REMARK 3 BIN R VALUE (WORKING SET) : 0.3900
REMARK 3 BIN FREE R VALUE SET COUNT : 5
REMARK 3 BIN FREE R VALUE : 0.4250
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1637
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 34
REMARK 3 SOLVENT ATOMS : 203
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 14.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.27
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.48000
REMARK 3 B22 (A**2) : 0.48000
REMARK 3 B33 (A**2) : -0.97000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.149
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.155
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.115
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.312
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.932
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.894
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1729 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 1194 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2337 ; 1.508 ; 1.962
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2907 ; 1.003 ; 3.004
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 218 ; 6.122 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 79 ;36.128 ;25.190
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 289 ;14.360 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 7 ; 9.928 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 235 ; 0.087 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1953 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 342 ; 0.003 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 352 ; 0.211 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 1233 ; 0.196 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 811 ; 0.174 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 865 ; 0.085 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 146 ; 0.180 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 14 ; 0.205 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 43 ; 0.247 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 14 ; 0.210 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1374 ; 0.869 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 447 ; 0.190 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1687 ; 1.030 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 812 ; 1.837 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 648 ; 2.519 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3KX1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-DEC-09.
REMARK 100 THE DEPOSITION ID IS D_1000056553.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-MAR-05
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 2.9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.933
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSTALCLEAR
REMARK 200 DATA SCALING SOFTWARE : CRYSTALCLEAR
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23303
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.510
REMARK 200 RESOLUTION RANGE LOW (A) : 37.890
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 70.3
REMARK 200 DATA REDUNDANCY : 2.790
REMARK 200 R MERGE (I) : 0.10100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.51
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.56
REMARK 200 COMPLETENESS FOR SHELL (%) : 9.2
REMARK 200 DATA REDUNDANCY IN SHELL : 1.13
REMARK 200 R MERGE FOR SHELL (I) : 0.10100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: IN-HOUSE CATHEPSIN K STRUCTURE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.85
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 34% PEG 4000, 0.2M AMMONIUM SULPHATE
REMARK 280 PH 2.9, 4% METHANOL , VAPOR DIFFUSION, HANGING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 64.41450
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 28.03450
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 28.03450
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 96.62175
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 28.03450
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 28.03450
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 32.20725
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 28.03450
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 28.03450
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 96.62175
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 28.03450
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 28.03450
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 32.20725
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 64.41450
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 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 ALA A 1
REMARK 465 PRO A 2
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 GLN A 21 50.20 -95.18
REMARK 500 SER A 146 -43.84 -130.89
REMARK 500 ASN A 159 70.21 -116.07
REMARK 500 LYS A 200 57.74 -112.46
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 KX1 A 216
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 217
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 218
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3KWZ RELATED DB: PDB
REMARK 900 SIMLAR 2-CYANO-PYRIMIDINE INHIBITOR DESCRIBED IN SAME REFERENCE
DBREF 3KX1 A 1 215 UNP P43235 CATK_HUMAN 115 329
SEQRES 1 A 215 ALA PRO ASP SER VAL ASP TYR ARG LYS LYS GLY TYR VAL
SEQRES 2 A 215 THR PRO VAL LYS ASN GLN GLY GLN CYS GLY SER CYS TRP
SEQRES 3 A 215 ALA PHE SER SER VAL GLY ALA LEU GLU GLY GLN LEU LYS
SEQRES 4 A 215 LYS LYS THR GLY LYS LEU LEU ASN LEU SER PRO GLN ASN
SEQRES 5 A 215 LEU VAL ASP CYS VAL SER GLU ASN ASP GLY CYS GLY GLY
SEQRES 6 A 215 GLY TYR MET THR ASN ALA PHE GLN TYR VAL GLN LYS ASN
SEQRES 7 A 215 ARG GLY ILE ASP SER GLU ASP ALA TYR PRO TYR VAL GLY
SEQRES 8 A 215 GLN GLU GLU SER CYS MET TYR ASN PRO THR GLY LYS ALA
SEQRES 9 A 215 ALA LYS CYS ARG GLY TYR ARG GLU ILE PRO GLU GLY ASN
SEQRES 10 A 215 GLU LYS ALA LEU LYS ARG ALA VAL ALA ARG VAL GLY PRO
SEQRES 11 A 215 VAL SER VAL ALA ILE ASP ALA SER LEU THR SER PHE GLN
SEQRES 12 A 215 PHE TYR SER LYS GLY VAL TYR TYR ASP GLU SER CYS ASN
SEQRES 13 A 215 SER ASP ASN LEU ASN HIS ALA VAL LEU ALA VAL GLY TYR
SEQRES 14 A 215 GLY ILE GLN LYS GLY ASN LYS HIS TRP ILE ILE LYS ASN
SEQRES 15 A 215 SER TRP GLY GLU ASN TRP GLY ASN LYS GLY TYR ILE LEU
SEQRES 16 A 215 MET ALA ARG ASN LYS ASN ASN ALA CYS GLY ILE ALA ASN
SEQRES 17 A 215 LEU ALA SER PHE PRO LYS MET
HET KX1 A 216 24
HET SO4 A 217 5
HET SO4 A 218 5
HETNAM KX1 4-CYCLOHEPTYL-6-(3-PIPERIDIN-1-YLPROPYL)PYRIMIDINE-2-
HETNAM 2 KX1 CARBONITRILE
HETNAM SO4 SULFATE ION
FORMUL 2 KX1 C20 H30 N4
FORMUL 3 SO4 2(O4 S 2-)
FORMUL 5 HOH *203(H2 O)
HELIX 1 1 ARG A 8 GLY A 11 5 4
HELIX 2 2 SER A 24 GLY A 43 1 20
HELIX 3 3 SER A 49 VAL A 57 1 9
HELIX 4 4 ASP A 61 GLY A 65 5 5
HELIX 5 5 TYR A 67 ARG A 79 1 13
HELIX 6 6 ASN A 99 THR A 101 5 3
HELIX 7 7 ASN A 117 VAL A 128 1 12
HELIX 8 8 LEU A 139 PHE A 144 1 6
HELIX 9 9 ASN A 202 ILE A 206 5 5
SHEET 1 A 3 VAL A 5 ASP A 6 0
SHEET 2 A 3 HIS A 162 GLN A 172 -1 O TYR A 169 N VAL A 5
SHEET 3 A 3 VAL A 131 ILE A 135 -1 N ILE A 135 O HIS A 162
SHEET 1 B 5 VAL A 5 ASP A 6 0
SHEET 2 B 5 HIS A 162 GLN A 172 -1 O TYR A 169 N VAL A 5
SHEET 3 B 5 ASN A 175 LYS A 181 -1 O LYS A 181 N LEU A 165
SHEET 4 B 5 TYR A 193 ALA A 197 -1 O ILE A 194 N ILE A 180
SHEET 5 B 5 VAL A 149 TYR A 150 1 N TYR A 150 O LEU A 195
SHEET 1 C 2 ILE A 81 ASP A 82 0
SHEET 2 C 2 LYS A 103 ALA A 105 -1 O ALA A 104 N ILE A 81
SHEET 1 D 2 TYR A 110 GLU A 112 0
SHEET 2 D 2 SER A 211 PRO A 213 -1 O PHE A 212 N ARG A 111
SSBOND 1 CYS A 22 CYS A 63 1555 1555 2.05
SSBOND 2 CYS A 56 CYS A 96 1555 1555 2.03
SSBOND 3 CYS A 155 CYS A 204 1555 1555 2.05
SITE 1 AC1 9 GLN A 19 GLY A 23 CYS A 25 LYS A 44
SITE 2 AC1 9 GLY A 64 GLY A 65 GLY A 66 ASN A 161
SITE 3 AC1 9 HIS A 162
SITE 1 AC2 8 ASN A 18 ARG A 111 GLY A 185 GLU A 186
SITE 2 AC2 8 ASN A 187 LYS A 214 HOH A 375 HOH A 408
SITE 1 AC3 5 ASP A 3 LEU A 139 THR A 140 SER A 141
SITE 2 AC3 5 HOH A 369
CRYST1 56.069 56.069 128.829 90.00 90.00 90.00 P 43 21 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 0.017835 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017835 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007762 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
