HEADER HYDROLASE 21-AUG-17 5QC0
TITLE CRYSTAL STRUCTURE OF HUMAN CATHEPSIN-S WITH BOUND LIGAND
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CATHEPSIN S;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.4.22.27;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: CTSS;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS D3R, CATHEPSIN S, LIGAND DOCKING, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.D.BEMBENEK,M.K.AMERIKS,T.MIRZADEGAN,H.YANG,C.SHAO,S.K.BURLEY
REVDAT 5 17-NOV-21 5QC0 1 REMARK
REVDAT 4 10-FEB-21 5QC0 1 AUTHOR JRNL
REVDAT 3 06-JUN-18 5QC0 1 REMARK SCALE ATOM
REVDAT 2 21-FEB-18 5QC0 1 REMARK
REVDAT 1 20-DEC-17 5QC0 0
JRNL AUTH S.D.BEMBENEK,M.K.AMERIKS,T.MIRZADEGAN,H.YANG,C.SHAO,
JRNL AUTH 2 S.K.BURLEY
JRNL TITL CRYSTAL STRUCTURE OF HUMAN CATHEPSIN-S WITH BOUND LIGAND
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0158
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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 53.67
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 79.2
REMARK 3 NUMBER OF REFLECTIONS : 23098
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) : 0.215
REMARK 3 R VALUE (WORKING SET) : 0.213
REMARK 3 FREE R VALUE : 0.257
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1246
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 577
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 26.16
REMARK 3 BIN R VALUE (WORKING SET) : 0.3820
REMARK 3 BIN FREE R VALUE SET COUNT : 26
REMARK 3 BIN FREE R VALUE : 0.3820
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3400
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 92
REMARK 3 SOLVENT ATOMS : 311
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.89
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.49000
REMARK 3 B22 (A**2) : 0.40000
REMARK 3 B33 (A**2) : -0.01000
REMARK 3 B12 (A**2) : 0.12000
REMARK 3 B13 (A**2) : -0.20000
REMARK 3 B23 (A**2) : 0.01000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.309
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.218
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.167
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.097
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.940
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.912
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3590 ; 0.009 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 3148 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4869 ; 1.317 ; 1.928
REMARK 3 BOND ANGLES OTHERS (DEGREES): 7337 ; 0.922 ; 2.990
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 438 ; 5.587 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 162 ;38.803 ;24.444
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 553 ;13.562 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 14 ;24.242 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 485 ; 0.073 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4038 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 746 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 1758 ; 1.323 ; 2.802
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1757 ; 1.309 ; 2.801
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2194 ; 2.027 ; 4.197
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2195 ; 2.030 ; 4.197
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1832 ; 1.624 ; 3.010
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1830 ; 1.622 ; 3.010
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2676 ; 2.577 ; 4.434
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 4196 ; 3.932 ;32.959
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 4126 ; 3.783 ;32.607
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 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 1
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 1 218 B 1 218 14508 0.06 0.05
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 : 1.20
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 5QC0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-AUG-17.
REMARK 100 THE DEPOSITION ID IS D_1001401757.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-MAY-06
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 4.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54178
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 944
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23098
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 53.670
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 79.2
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
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) : NULL
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: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.65
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM SODIUM ACETATE PH 4.5, 200MM
REMARK 280 AMMONIUM ACETATE, 25% PEG 8000. PROTEIN CONCENTRATION 7 MG/ML,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K, PH 4.50
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 220
REMARK 465 GLY A 221
REMARK 465 GLY A 222
REMARK 465 ILE B 0
REMARK 465 GLY B 221
REMARK 465 GLY B 222
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ILE A 0 CG1 CG2 CD1
REMARK 470 LYS A 60 CD CE NZ
REMARK 470 LYS A 82 CE NZ
REMARK 470 LYS A 98 CG CD CE NZ
REMARK 470 LYS B 98 CG CD CE NZ
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 58 -120.51 -116.18
REMARK 500 THR B 58 -118.67 -116.52
REMARK 500
REMARK 500 REMARK: NULL
REMARK 615
REMARK 615 ZERO OCCUPANCY ATOM
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 615 M RES C SSEQI
REMARK 615 BQJ B 901
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BQJ A 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BQJ B 901
DBREF 5QC0 A 0 217 UNP P25774 CATS_HUMAN 114 331
DBREF 5QC0 B 0 217 UNP P25774 CATS_HUMAN 114 331
SEQADV 5QC0 SER A 25 UNP P25774 CYS 139 ENGINEERED MUTATION
SEQADV 5QC0 LEU A 218 UNP P25774 EXPRESSION TAG
SEQADV 5QC0 GLN A 219 UNP P25774 EXPRESSION TAG
SEQADV 5QC0 GLY A 220 UNP P25774 EXPRESSION TAG
SEQADV 5QC0 GLY A 221 UNP P25774 EXPRESSION TAG
SEQADV 5QC0 GLY A 222 UNP P25774 EXPRESSION TAG
SEQADV 5QC0 SER B 25 UNP P25774 CYS 139 ENGINEERED MUTATION
SEQADV 5QC0 LEU B 218 UNP P25774 EXPRESSION TAG
SEQADV 5QC0 GLN B 219 UNP P25774 EXPRESSION TAG
SEQADV 5QC0 GLY B 220 UNP P25774 EXPRESSION TAG
SEQADV 5QC0 GLY B 221 UNP P25774 EXPRESSION TAG
SEQADV 5QC0 GLY B 222 UNP P25774 EXPRESSION TAG
SEQRES 1 A 223 ILE LEU PRO ASP SER VAL ASP TRP ARG GLU LYS GLY CYS
SEQRES 2 A 223 VAL THR GLU VAL LYS TYR GLN GLY SER CYS GLY ALA SER
SEQRES 3 A 223 TRP ALA PHE SER ALA VAL GLY ALA LEU GLU ALA GLN LEU
SEQRES 4 A 223 LYS LEU LYS THR GLY LYS LEU VAL SER LEU SER ALA GLN
SEQRES 5 A 223 ASN LEU VAL ASP CYS SER THR GLU LYS TYR GLY ASN LYS
SEQRES 6 A 223 GLY CYS ASN GLY GLY PHE MET THR THR ALA PHE GLN TYR
SEQRES 7 A 223 ILE ILE ASP ASN LYS GLY ILE ASP SER ASP ALA SER TYR
SEQRES 8 A 223 PRO TYR LYS ALA MET ASP GLN LYS CYS GLN TYR ASP SER
SEQRES 9 A 223 LYS TYR ARG ALA ALA THR CYS SER LYS TYR THR GLU LEU
SEQRES 10 A 223 PRO TYR GLY ARG GLU ASP VAL LEU LYS GLU ALA VAL ALA
SEQRES 11 A 223 ASN LYS GLY PRO VAL SER VAL GLY VAL ASP ALA ARG HIS
SEQRES 12 A 223 PRO SER PHE PHE LEU TYR ARG SER GLY VAL TYR TYR GLU
SEQRES 13 A 223 PRO SER CYS THR GLN ASN VAL ASN HIS GLY VAL LEU VAL
SEQRES 14 A 223 VAL GLY TYR GLY ASP LEU ASN GLY LYS GLU TYR TRP LEU
SEQRES 15 A 223 VAL LYS ASN SER TRP GLY HIS ASN PHE GLY GLU GLU GLY
SEQRES 16 A 223 TYR ILE ARG MET ALA ARG ASN LYS GLY ASN HIS CYS GLY
SEQRES 17 A 223 ILE ALA SER PHE PRO SER TYR PRO GLU ILE LEU GLN GLY
SEQRES 18 A 223 GLY GLY
SEQRES 1 B 223 ILE LEU PRO ASP SER VAL ASP TRP ARG GLU LYS GLY CYS
SEQRES 2 B 223 VAL THR GLU VAL LYS TYR GLN GLY SER CYS GLY ALA SER
SEQRES 3 B 223 TRP ALA PHE SER ALA VAL GLY ALA LEU GLU ALA GLN LEU
SEQRES 4 B 223 LYS LEU LYS THR GLY LYS LEU VAL SER LEU SER ALA GLN
SEQRES 5 B 223 ASN LEU VAL ASP CYS SER THR GLU LYS TYR GLY ASN LYS
SEQRES 6 B 223 GLY CYS ASN GLY GLY PHE MET THR THR ALA PHE GLN TYR
SEQRES 7 B 223 ILE ILE ASP ASN LYS GLY ILE ASP SER ASP ALA SER TYR
SEQRES 8 B 223 PRO TYR LYS ALA MET ASP GLN LYS CYS GLN TYR ASP SER
SEQRES 9 B 223 LYS TYR ARG ALA ALA THR CYS SER LYS TYR THR GLU LEU
SEQRES 10 B 223 PRO TYR GLY ARG GLU ASP VAL LEU LYS GLU ALA VAL ALA
SEQRES 11 B 223 ASN LYS GLY PRO VAL SER VAL GLY VAL ASP ALA ARG HIS
SEQRES 12 B 223 PRO SER PHE PHE LEU TYR ARG SER GLY VAL TYR TYR GLU
SEQRES 13 B 223 PRO SER CYS THR GLN ASN VAL ASN HIS GLY VAL LEU VAL
SEQRES 14 B 223 VAL GLY TYR GLY ASP LEU ASN GLY LYS GLU TYR TRP LEU
SEQRES 15 B 223 VAL LYS ASN SER TRP GLY HIS ASN PHE GLY GLU GLU GLY
SEQRES 16 B 223 TYR ILE ARG MET ALA ARG ASN LYS GLY ASN HIS CYS GLY
SEQRES 17 B 223 ILE ALA SER PHE PRO SER TYR PRO GLU ILE LEU GLN GLY
SEQRES 18 B 223 GLY GLY
HET BQJ A 901 46
HET BQJ B 901 46
HETNAM BQJ 2-(DIMETHYLAMINO)-1-[4-(2-OXO-2-{3-[3-{[2-(PIPERIDIN-1-
HETNAM 2 BQJ YL)ETHYL]SULFANYL}-4-(TRIFLUOROMETHYL)PHENYL]-1-
HETNAM 3 BQJ PROPYL-1,4,6,7-TETRAHYDRO-5H-PYRAZOLO[4,3-C]PYRIDIN-5-
HETNAM 4 BQJ YL}ETHYL)PIPERIDIN-1-YL]ETHAN-1-ONE
FORMUL 3 BQJ 2(C34 H49 F3 N6 O2 S)
FORMUL 5 HOH *311(H2 O)
HELIX 1 AA1 ARG A 8 GLY A 11 5 4
HELIX 2 AA2 ALA A 24 GLY A 43 1 20
HELIX 3 AA3 SER A 49 SER A 57 1 9
HELIX 4 AA4 THR A 58 GLY A 62 5 5
HELIX 5 AA5 LYS A 64 GLY A 68 5 5
HELIX 6 AA6 PHE A 70 LYS A 82 1 13
HELIX 7 AA7 ASP A 102 LYS A 104 5 3
HELIX 8 AA8 ARG A 120 LYS A 131 1 12
HELIX 9 AA9 HIS A 142 LEU A 147 1 6
HELIX 10 AB1 ASN A 204 ILE A 208 5 5
HELIX 11 AB2 ARG B 8 GLY B 11 5 4
HELIX 12 AB3 ALA B 24 GLY B 43 1 20
HELIX 13 AB4 SER B 49 SER B 57 1 9
HELIX 14 AB5 THR B 58 GLY B 62 5 5
HELIX 15 AB6 LYS B 64 GLY B 68 5 5
HELIX 16 AB7 PHE B 70 LYS B 82 1 13
HELIX 17 AB8 ASP B 102 LYS B 104 5 3
HELIX 18 AB9 ARG B 120 LYS B 131 1 12
HELIX 19 AC1 HIS B 142 LEU B 147 1 6
HELIX 20 AC2 ASN B 204 ILE B 208 5 5
SHEET 1 AA1 3 VAL A 5 ASP A 6 0
SHEET 2 AA1 3 HIS A 164 LEU A 174 -1 O TYR A 171 N VAL A 5
SHEET 3 AA1 3 VAL A 134 VAL A 138 -1 N VAL A 136 O VAL A 166
SHEET 1 AA2 5 VAL A 5 ASP A 6 0
SHEET 2 AA2 5 HIS A 164 LEU A 174 -1 O TYR A 171 N VAL A 5
SHEET 3 AA2 5 LYS A 177 LYS A 183 -1 O LYS A 183 N LEU A 167
SHEET 4 AA2 5 TYR A 195 ALA A 199 -1 O ILE A 196 N VAL A 182
SHEET 5 AA2 5 VAL A 152 TYR A 153 1 N TYR A 153 O ARG A 197
SHEET 1 AA3 2 ILE A 84 ASP A 85 0
SHEET 2 AA3 2 ARG A 106 ALA A 108 -1 O ALA A 107 N ILE A 84
SHEET 1 AA4 2 LYS A 112 GLU A 115 0
SHEET 2 AA4 2 SER A 213 GLU A 216 -1 O GLU A 216 N LYS A 112
SHEET 1 AA5 3 VAL B 5 ASP B 6 0
SHEET 2 AA5 3 HIS B 164 LEU B 174 -1 O TYR B 171 N VAL B 5
SHEET 3 AA5 3 VAL B 134 VAL B 138 -1 N VAL B 136 O VAL B 166
SHEET 1 AA6 5 VAL B 5 ASP B 6 0
SHEET 2 AA6 5 HIS B 164 LEU B 174 -1 O TYR B 171 N VAL B 5
SHEET 3 AA6 5 LYS B 177 LYS B 183 -1 O LYS B 183 N LEU B 167
SHEET 4 AA6 5 TYR B 195 ALA B 199 -1 O ILE B 196 N VAL B 182
SHEET 5 AA6 5 VAL B 152 TYR B 153 1 N TYR B 153 O ARG B 197
SHEET 1 AA7 2 ILE B 84 ASP B 85 0
SHEET 2 AA7 2 ARG B 106 ALA B 108 -1 O ALA B 107 N ILE B 84
SHEET 1 AA8 2 LYS B 112 GLU B 115 0
SHEET 2 AA8 2 SER B 213 GLU B 216 -1 O GLU B 216 N LYS B 112
SSBOND 1 CYS A 22 CYS A 66 1555 1555 2.02
SSBOND 2 CYS A 56 CYS A 99 1555 1555 2.06
SSBOND 3 CYS A 158 CYS A 206 1555 1555 2.04
SSBOND 4 CYS B 22 CYS B 66 1555 1555 2.06
SSBOND 5 CYS B 56 CYS B 99 1555 1555 2.06
SSBOND 6 CYS B 158 CYS B 206 1555 1555 2.04
SITE 1 AC1 21 TRP A 26 GLY A 62 GLY A 69 PHE A 70
SITE 2 AC1 21 MET A 71 THR A 72 GLU A 115 GLY A 137
SITE 3 AC1 21 ASN A 163 HIS A 164 GLY A 165 PHE A 211
SITE 4 AC1 21 HOH A1022 HOH A1032 HOH A1088 HOH A1099
SITE 5 AC1 21 HOH A1114 HOH A1123 TYR B 118 GLY B 119
SITE 6 AC1 21 ARG B 120
SITE 1 AC2 16 LYS B 60 GLY B 62 GLY B 69 PHE B 70
SITE 2 AC2 16 MET B 71 THR B 72 GLU B 115 GLY B 137
SITE 3 AC2 16 VAL B 162 ASN B 163 HIS B 164 GLY B 165
SITE 4 AC2 16 PHE B 211 HOH B1018 HOH B1076 HOH B1101
CRYST1 36.980 52.930 58.460 70.92 72.06 73.46 P 1 2
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 0.027042 -0.008031 -0.006890 0.00000
SCALE2 0.000000 0.019708 -0.005357 0.00000
SCALE3 0.000000 0.000000 0.018632 0.00000
(ATOM LINES ARE NOT SHOWN.)
END