HEADER HYDROLASE/HYDROLASE INHIBITOR 18-MAY-11 3S3Q
TITLE STRUCTURE OF CATHEPSIN B1 FROM SCHISTOSOMA MANSONI IN COMPLEX WITH
TITLE 2 K11017 INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CATHEPSIN B-LIKE PEPTIDASE (C01 FAMILY);
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 87-340;
COMPND 5 SYNONYM: CATHEPSIN B1 ISOTYPE 1;
COMPND 6 EC: 3.4.22.1;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SCHISTOSOMA MANSONI;
SOURCE 3 ORGANISM_COMMON: BLOOD FLUKE;
SOURCE 4 ORGANISM_TAXID: 6183;
SOURCE 5 GENE: CB1.1, SMP_103610;
SOURCE 6 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: X33;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PPICZALPHAA
KEYWDS PEPTIDASE, DIGESTIVE TRACT, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR P.REZACOVA,A.JILKOVA,J.BRYNDA,M.HORN,M.MARES
REVDAT 4 13-SEP-23 3S3Q 1 REMARK SEQADV LINK
REVDAT 3 26-OCT-11 3S3Q 1 JRNL
REVDAT 2 07-SEP-11 3S3Q 1 LINK
REVDAT 1 10-AUG-11 3S3Q 0
JRNL AUTH A.JILKOVA,P.REZACOVA,M.LEPSIK,M.HORN,J.VACHOVA,J.FANFRLIK,
JRNL AUTH 2 J.BRYNDA,J.H.MCKERROW,C.R.CAFFREY,M.MARES
JRNL TITL STRUCTURAL BASIS FOR INHIBITION OF CATHEPSIN B DRUG TARGET
JRNL TITL 2 FROM THE HUMAN BLOOD FLUKE, SCHISTOSOMA MANSONI.
JRNL REF J.BIOL.CHEM. V. 286 35770 2011
JRNL REFN ISSN 0021-9258
JRNL PMID 21832058
JRNL DOI 10.1074/JBC.M111.271304
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.3.0037
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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.84
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 21548
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) : 0.170
REMARK 3 R VALUE (WORKING SET) : 0.166
REMARK 3 FREE R VALUE : 0.236
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1162
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) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.85
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1560
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.74
REMARK 3 BIN R VALUE (WORKING SET) : 0.2330
REMARK 3 BIN FREE R VALUE SET COUNT : 83
REMARK 3 BIN FREE R VALUE : 0.3500
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1998
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 45
REMARK 3 SOLVENT ATOMS : 536
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 13.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.09
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.18000
REMARK 3 B22 (A**2) : -0.07000
REMARK 3 B33 (A**2) : 0.25000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.152
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.103
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.333
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.955
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.902
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2172 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2950 ; 1.268 ; 1.963
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 276 ; 5.816 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 98 ;31.337 ;24.184
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 376 ;12.420 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ;15.311 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 294 ; 0.094 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1680 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1256 ; 0.215 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1477 ; 0.311 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 460 ; 0.153 ; 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): 67 ; 0.172 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 80 ; 0.184 ; 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): 1340 ; 0.642 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2092 ; 0.976 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 980 ; 1.740 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 846 ; 2.604 ; 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 : BABINET MODEL WITH 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 3S3Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-JUN-11.
REMARK 100 THE DEPOSITION ID IS D_1000065722.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-OCT-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9791
REMARK 200 MONOCHROMATOR : SI111 DOUBLE-CRYSTAL
REMARK 200 MONOCHROMATOR
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22894
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 6.800
REMARK 200 R MERGE (I) : 0.10500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.83
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.47900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: REFMAC 5.3.0037
REMARK 200 STARTING MODEL: PDB ENTRY 3QSD
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.96
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: RESERVOIR: 0.2 M AMMONIUM ACETATE PH
REMARK 280 6.2, 0.1 M NA CITRATE, 30%(V/W) PEG 1500, PROTEIN BUFFER AND
REMARK 280 CONCENTRATION: 10 MM NA ACETATE, PH 5.5, CPR = 2.5 MG/ML,
REMARK 280 PROTEIN: RESERVOIR: 1:1, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-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 SMTRY1 2 -1.000000 0.000000 0.000000 16.54600
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 45.13450
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.76400
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 45.13450
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 16.54600
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.76400
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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 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 SER A 95 -151.49 65.48
REMARK 500 LYS A 208 47.14 -92.66
REMARK 500 ASN A 293 172.83 64.11
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 C1P A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 324
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 2
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3QSD RELATED DB: PDB
REMARK 900 RELATED ID: 3S3R RELATED DB: PDB
DBREF 3S3Q A 70 323 UNP Q8MNY2 Q8MNY2_SCHMA 87 340
SEQADV 3S3Q ALA A 168 UNP Q8MNY2 THR 185 ENGINEERED MUTATION
SEQADV 3S3Q ALA A 283 UNP Q8MNY2 THR 300 ENGINEERED MUTATION
SEQRES 1 A 254 VAL GLU ILE PRO SER SER PHE ASP SER ARG LYS LYS TRP
SEQRES 2 A 254 PRO ARG CYS LYS SER ILE ALA THR ILE ARG ASP GLN SER
SEQRES 3 A 254 ARG CYS GLY SER CYS TRP ALA PHE GLY ALA VAL GLU ALA
SEQRES 4 A 254 MET SER ASP ARG SER CYS ILE GLN SER GLY GLY LYS GLN
SEQRES 5 A 254 ASN VAL GLU LEU SER ALA VAL ASP LEU LEU SER CYS CYS
SEQRES 6 A 254 GLU SER CYS GLY LEU GLY CYS GLU GLY GLY ILE LEU GLY
SEQRES 7 A 254 PRO ALA TRP ASP TYR TRP VAL LYS GLU GLY ILE VAL THR
SEQRES 8 A 254 GLY SER SER LYS GLU ASN HIS ALA GLY CYS GLU PRO TYR
SEQRES 9 A 254 PRO PHE PRO LYS CYS GLU HIS HIS THR LYS GLY LYS TYR
SEQRES 10 A 254 PRO PRO CYS GLY SER LYS ILE TYR LYS THR PRO ARG CYS
SEQRES 11 A 254 LYS GLN THR CYS GLN LYS LYS TYR LYS THR PRO TYR THR
SEQRES 12 A 254 GLN ASP LYS HIS ARG GLY LYS SER SER TYR ASN VAL LYS
SEQRES 13 A 254 ASN ASP GLU LYS ALA ILE GLN LYS GLU ILE MET LYS TYR
SEQRES 14 A 254 GLY PRO VAL GLU ALA GLY PHE THR VAL TYR GLU ASP PHE
SEQRES 15 A 254 LEU ASN TYR LYS SER GLY ILE TYR LYS HIS ILE THR GLY
SEQRES 16 A 254 GLU THR LEU GLY GLY HIS ALA ILE ARG ILE ILE GLY TRP
SEQRES 17 A 254 GLY VAL GLU ASN LYS ALA PRO TYR TRP LEU ILE ALA ASN
SEQRES 18 A 254 SER TRP ASN GLU ASP TRP GLY GLU ASN GLY TYR PHE ARG
SEQRES 19 A 254 ILE VAL ARG GLY ARG ASP GLU CYS SER ILE GLU SER GLU
SEQRES 20 A 254 VAL THR ALA GLY ARG ILE ASN
HET C1P A 1 37
HET ACT A 324 4
HET ACT A 2 4
HETNAM C1P N~2~-(MORPHOLIN-4-YLCARBONYL)-N-[(3S)-1-PHENYL-5-
HETNAM 2 C1P (PHENYLSULFONYL)PENTAN-3-YL]-L-LEUCINAMIDE
HETNAM ACT ACETATE ION
HETSYN C1P K11017, BOUND FORM
FORMUL 2 C1P C28 H39 N3 O5 S
FORMUL 3 ACT 2(C2 H3 O2 1-)
FORMUL 5 HOH *536(H2 O)
HELIX 1 1 SER A 78 TRP A 82 1 5
HELIX 2 2 SER A 99 SER A 117 1 19
HELIX 3 3 SER A 126 CYS A 134 1 9
HELIX 4 4 LEU A 139 GLY A 143 5 5
HELIX 5 5 ILE A 145 GLU A 156 1 12
HELIX 6 6 PRO A 210 LYS A 215 5 6
HELIX 7 7 ASP A 227 GLY A 239 1 13
HELIX 8 8 ASP A 250 TYR A 254 5 5
HELIX 9 9 ASP A 309 ILE A 313 5 5
SHEET 1 A 5 PHE A 76 ASP A 77 0
SHEET 2 A 5 THR A 266 GLU A 280 -1 O TRP A 277 N PHE A 76
SHEET 3 A 5 VAL A 241 TYR A 248 -1 N VAL A 247 O LEU A 267
SHEET 4 A 5 VAL A 317 ARG A 321 -1 O THR A 318 N GLU A 242
SHEET 5 A 5 SER A 220 ASN A 223 -1 N TYR A 222 O ALA A 319
SHEET 1 B 5 PHE A 76 ASP A 77 0
SHEET 2 B 5 THR A 266 GLU A 280 -1 O TRP A 277 N PHE A 76
SHEET 3 B 5 ALA A 283 ALA A 289 -1 O TYR A 285 N GLY A 278
SHEET 4 B 5 TYR A 301 VAL A 305 -1 O PHE A 302 N ILE A 288
SHEET 5 B 5 ILE A 258 TYR A 259 1 N TYR A 259 O ARG A 303
SSBOND 1 CYS A 85 CYS A 114 1555 1555 2.05
SSBOND 2 CYS A 97 CYS A 141 1555 1555 2.02
SSBOND 3 CYS A 133 CYS A 199 1555 1555 2.03
SSBOND 4 CYS A 134 CYS A 137 1555 1555 2.02
SSBOND 5 CYS A 170 CYS A 203 1555 1555 2.05
SSBOND 6 CYS A 178 CYS A 189 1555 1555 2.03
LINK C18 C1P A 1 SG CYS A 100 1555 1555 1.99
SITE 1 AC1 17 GLN A 94 GLY A 98 CYS A 100 TRP A 101
SITE 2 AC1 17 CYS A 141 GLU A 142 GLY A 143 GLY A 144
SITE 3 AC1 17 LEU A 146 ILE A 193 VAL A 247 GLY A 269
SITE 4 AC1 17 HIS A 270 TRP A 292 GLU A 316 HOH A 469
SITE 5 AC1 17 HOH A 600
SITE 1 AC2 8 GLN A 121 LYS A 215 HIS A 216 ARG A 217
SITE 2 AC2 8 HOH A 349 HOH A 544 HOH A 578 HOH A 684
SITE 1 AC3 8 HOH A 24 GLU A 179 HIS A 180 HIS A 181
SITE 2 AC3 8 PRO A 188 GLY A 190 HOH A 354 HOH A 793
CRYST1 33.092 79.528 90.269 90.00 90.00 90.00 P 21 21 21 4
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 0.030219 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012574 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011078 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
