HEADER HYDROLASE/HYDROLASE INHIBITOR 22-FEB-08 3CBK
TITLE CHAGASIN-CATHEPSIN B
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CATHEPSIN B;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CATHEPSIN B1, APP SECRETASE, APPS;
COMPND 5 EC: 3.4.22.1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: CHAGASIN;
COMPND 10 CHAIN: B;
COMPND 11 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: CTSB, CPSB;
SOURCE 6 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: GS115;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PPIC9;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: TRYPANOSOMA CRUZI;
SOURCE 13 ORGANISM_TAXID: 5693;
SOURCE 14 GENE: CHA;
SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: P-GEX-6P-1
KEYWDS CHAGASIN, CATHEPSIN B, OCCLUDING LOOP, CHAGAS DISEASE, GLYCOPROTEIN,
KEYWDS 2 HYDROLASE, LYSOSOME, PROTEASE, THIOL PROTEASE, ZYMOGEN, CYTOPLASMIC
KEYWDS 3 VESICLE, PROTEASE INHIBITOR, THIOL PROTEASE INHIBITOR, HYDROLASE-
KEYWDS 4 HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR I.REDZYNIA,G.D.BUJACZ,M.ABRAHAMSON,A.LJUNGGREN,M.JASKOLSKI,J.S.MORT
REVDAT 7 01-NOV-23 3CBK 1 REMARK
REVDAT 6 10-NOV-21 3CBK 1 SEQADV
REVDAT 5 23-MAY-18 3CBK 1 REMARK
REVDAT 4 19-MAR-14 3CBK 1 JRNL
REVDAT 3 13-JUL-11 3CBK 1 VERSN
REVDAT 2 24-FEB-09 3CBK 1 VERSN
REVDAT 1 27-MAY-08 3CBK 0
JRNL AUTH I.REDZYNIA,A.LJUNGGREN,M.ABRAHAMSON,J.S.MORT,J.C.KRUPA,
JRNL AUTH 2 M.JASKOLSKI,G.BUJACZ
JRNL TITL DISPLACEMENT OF THE OCCLUDING LOOP BY THE PARASITE PROTEIN,
JRNL TITL 2 CHAGASIN, RESULTS IN EFFICIENT INHIBITION OF HUMAN CATHEPSIN
JRNL TITL 3 B.
JRNL REF J.BIOL.CHEM. V. 283 22815 2008
JRNL REFN ISSN 0021-9258
JRNL PMID 18515357
JRNL DOI 10.1074/JBC.M802064200
REMARK 2
REMARK 2 RESOLUTION. 2.67 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) : 2.67
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.1
REMARK 3 NUMBER OF REFLECTIONS : 11311
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) : 0.195
REMARK 3 R VALUE (WORKING SET) : 0.193
REMARK 3 FREE R VALUE : 0.242
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 573
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) : 2.67
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.74
REMARK 3 REFLECTION IN BIN (WORKING SET) : 828
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.92
REMARK 3 BIN R VALUE (WORKING SET) : 0.2640
REMARK 3 BIN FREE R VALUE SET COUNT : 42
REMARK 3 BIN FREE R VALUE : 0.2890
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2820
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 63
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 69.27
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 52.48
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.39000
REMARK 3 B22 (A**2) : 1.39000
REMARK 3 B33 (A**2) : -2.79000
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): 0.339
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.249
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 19.175
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.943
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): 2917 ; 0.024 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3972 ; 2.357 ; 1.927
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 365 ; 9.084 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 132 ;34.414 ;24.242
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 436 ;22.790 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 11 ;20.704 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 409 ; 0.156 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2282 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1421 ; 0.264 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1902 ; 0.334 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 133 ; 0.253 ; 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): 45 ; 0.358 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 4 ; 0.418 ; 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): 1859 ; 0.956 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2915 ; 1.608 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1246 ; 2.494 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1057 ; 3.743 ; 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 : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 61 A 255
REMARK 3 ORIGIN FOR THE GROUP (A): 32.6751 18.2207 22.4048
REMARK 3 T TENSOR
REMARK 3 T11: -0.3277 T22: 0.0586
REMARK 3 T33: -0.0626 T12: -0.0053
REMARK 3 T13: 0.0865 T23: -0.0786
REMARK 3 L TENSOR
REMARK 3 L11: 2.5255 L22: 2.0875
REMARK 3 L33: 3.9530 L12: 0.2215
REMARK 3 L13: 0.7673 L23: 0.6087
REMARK 3 S TENSOR
REMARK 3 S11: -0.0687 S12: -0.0373 S13: 0.2761
REMARK 3 S21: -0.1221 S22: -0.0199 S23: 0.0324
REMARK 3 S31: -0.0556 S32: 0.3993 S33: 0.0886
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1 B 110
REMARK 3 ORIGIN FOR THE GROUP (A): 24.4211 43.4757 10.1906
REMARK 3 T TENSOR
REMARK 3 T11: -0.0097 T22: 0.0733
REMARK 3 T33: -0.0894 T12: -0.1607
REMARK 3 T13: 0.1233 T23: -0.1136
REMARK 3 L TENSOR
REMARK 3 L11: 1.6037 L22: 3.0368
REMARK 3 L33: 2.3883 L12: -0.5978
REMARK 3 L13: 0.0866 L23: -1.4900
REMARK 3 S TENSOR
REMARK 3 S11: -0.0869 S12: 0.2534 S13: 0.0151
REMARK 3 S21: -0.1599 S22: 0.0409 S23: 0.2583
REMARK 3 S31: -0.3234 S32: -0.2420 S33: 0.0460
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: NULL
REMARK 4
REMARK 4 3CBK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-FEB-08.
REMARK 100 THE DEPOSITION ID IS D_1000046577.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-APR-07
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 : MAX II
REMARK 200 BEAMLINE : I911-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.041
REMARK 200 MONOCHROMATOR : BENT SILICON CRYSTAL
REMARK 200 OPTICS : MONOCHROMATOR, MULTILAYER MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 11903
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.670
REMARK 200 RESOLUTION RANGE LOW (A) : 68.520
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.4
REMARK 200 DATA REDUNDANCY : 5.700
REMARK 200 R MERGE (I) : 0.10900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.67
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.77
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.5
REMARK 200 DATA REDUNDANCY IN SHELL : 5.00
REMARK 200 R MERGE FOR SHELL (I) : 0.57600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
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: PDB ENTRY 3CBJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.38
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.14M AMMONIUM FLUORIDE, 14% PEG 3350,
REMARK 280 PH 6.2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42 21 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 -Y+1/2,X+1/2,Z+1/2
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/2
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 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 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 0.000000 -1.000000 0.000000 42.53300
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 42.53300
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 57.84550
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 42.53300
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 42.53300
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 57.84550
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 42.53300
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 42.53300
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 57.84550
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 42.53300
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 42.53300
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 57.84550
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 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2710 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16140 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.4 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 PHE A 57P
REMARK 465 THR A 58P
REMARK 465 GLU A 59P
REMARK 465 ASP A 60P
REMARK 465 TYR A 256
REMARK 465 TRP A 257
REMARK 465 GLU A 258
REMARK 465 LYS A 259
REMARK 465 ILE A 260
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 CYS A 26 CB CYS A 26 SG -0.139
REMARK 500 GLU B 23 CD GLU B 23 OE2 0.071
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 GLU A 109 N - CA - C ANGL. DEV. = 18.3 DEGREES
REMARK 500 VAL A 112 CB - CA - C ANGL. DEV. = -19.1 DEGREES
REMARK 500 VAL A 112 N - CA - C ANGL. DEV. = 40.5 DEGREES
REMARK 500 CYS A 128 CA - CB - SG ANGL. DEV. = 7.0 DEGREES
REMARK 500 TYR A 148 CB - CA - C ANGL. DEV. = -15.3 DEGREES
REMARK 500 SER A 156 CB - CA - C ANGL. DEV. = 17.7 DEGREES
REMARK 500 GLU A 194 CB - CA - C ANGL. DEV. = 12.1 DEGREES
REMARK 500 SER B 2 CB - CA - C ANGL. DEV. = 12.7 DEGREES
REMARK 500 LYS B 7 CB - CA - C ANGL. DEV. = -12.8 DEGREES
REMARK 500 ALA B 17 CB - CA - C ANGL. DEV. = 9.6 DEGREES
REMARK 500 GLU B 23 CG - CD - OE1 ANGL. DEV. = -12.7 DEGREES
REMARK 500 GLU B 23 CG - CD - OE2 ANGL. DEV. = 14.5 DEGREES
REMARK 500 ILE B 24 N - CA - C ANGL. DEV. = -19.2 DEGREES
REMARK 500 ASP B 61 CB - CG - OD2 ANGL. DEV. = 6.9 DEGREES
REMARK 500 ASP B 61 N - CA - C ANGL. DEV. = -18.9 DEGREES
REMARK 500 LYS B 63 CB - CA - C ANGL. DEV. = -12.1 DEGREES
REMARK 500 HIS B 74 N - CA - C ANGL. DEV. = -17.7 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
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 PRO A 107 -167.46 -67.65
REMARK 500 ASN A 113 -74.62 -94.87
REMARK 500 ARG A 116 -151.83 63.44
REMARK 500 PRO A 118 -153.93 -83.25
REMARK 500 CYS A 119 54.25 -118.75
REMARK 500 THR A 120 -155.30 -73.55
REMARK 500 GLU A 122 51.26 -111.61
REMARK 500 PRO A 134 153.44 -49.89
REMARK 500 THR A 139 175.74 -59.29
REMARK 500 ASP A 179 -9.86 -52.97
REMARK 500 ASN A 222 -168.09 64.65
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2NQD RELATED DB: PDB
REMARK 900 CHAGASIN-CATHEPSIN L
REMARK 900 RELATED ID: 2NNR RELATED DB: PDB
REMARK 900 NATIVE CHAGASIN
REMARK 900 RELATED ID: 1HUC RELATED DB: PDB
REMARK 900 NATIVE CATHEPSIN B
REMARK 900 RELATED ID: 3PBH RELATED DB: PDB
REMARK 900 PROCATHEPSIN B
REMARK 900 RELATED ID: 3CBJ RELATED DB: PDB
REMARK 900 CHAGASIN-CATHESPIN B
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 IN THE CHAIN A, PHE 57P, THR 58P, GLU 59P, ASP 60P, LEU 61P, LYS
REMARK 999 62P BELONG TO PROSEGMENT SEQUENCE.
DBREF 3CBK A 57P 260 UNP P07858 CATB_HUMAN 74 339
DBREF 3CBK B 1 110 UNP Q966X9 CHAG_TRYCR 1 110
SEQADV 3CBK ALA A 29 UNP P07858 CYS 108 ENGINEERED MUTATION
SEQADV 3CBK ALA A 110 UNP P07858 HIS 189 ENGINEERED MUTATION
SEQADV 3CBK ALA A 115 UNP P07858 SER 194 ENGINEERED MUTATION
SEQRES 1 A 266 PHE THR GLU ASP LEU LYS LEU PRO ALA SER PHE ASP ALA
SEQRES 2 A 266 ARG GLU GLN TRP PRO GLN CYS PRO THR ILE LYS GLU ILE
SEQRES 3 A 266 ARG ASP GLN GLY SER CYS GLY SER ALA TRP ALA PHE GLY
SEQRES 4 A 266 ALA VAL GLU ALA ILE SER ASP ARG ILE CYS ILE HIS THR
SEQRES 5 A 266 ASN ALA HIS VAL SER VAL GLU VAL SER ALA GLU ASP LEU
SEQRES 6 A 266 LEU THR CYS CYS GLY SER MET CYS GLY ASP GLY CYS ASN
SEQRES 7 A 266 GLY GLY TYR PRO ALA GLU ALA TRP ASN PHE TRP THR ARG
SEQRES 8 A 266 LYS GLY LEU VAL SER GLY GLY LEU TYR GLU SER HIS VAL
SEQRES 9 A 266 GLY CYS ARG PRO TYR SER ILE PRO PRO CYS GLU ALA HIS
SEQRES 10 A 266 VAL ASN GLY ALA ARG PRO PRO CYS THR GLY GLU GLY ASP
SEQRES 11 A 266 THR PRO LYS CYS SER LYS ILE CYS GLU PRO GLY TYR SER
SEQRES 12 A 266 PRO THR TYR LYS GLN ASP LYS HIS TYR GLY TYR ASN SER
SEQRES 13 A 266 TYR SER VAL SER ASN SER GLU LYS ASP ILE MET ALA GLU
SEQRES 14 A 266 ILE TYR LYS ASN GLY PRO VAL GLU GLY ALA PHE SER VAL
SEQRES 15 A 266 TYR SER ASP PHE LEU LEU TYR LYS SER GLY VAL TYR GLN
SEQRES 16 A 266 HIS VAL THR GLY GLU MET MET GLY GLY HIS ALA ILE ARG
SEQRES 17 A 266 ILE LEU GLY TRP GLY VAL GLU ASN GLY THR PRO TYR TRP
SEQRES 18 A 266 LEU VAL ALA ASN SER TRP ASN THR ASP TRP GLY ASP ASN
SEQRES 19 A 266 GLY PHE PHE LYS ILE LEU ARG GLY GLN ASP HIS CYS GLY
SEQRES 20 A 266 ILE GLU SER GLU VAL VAL ALA GLY ILE PRO ARG THR ASP
SEQRES 21 A 266 GLN TYR TRP GLU LYS ILE
SEQRES 1 B 110 MET SER HIS LYS VAL THR LYS ALA HIS ASN GLY ALA THR
SEQRES 2 B 110 LEU THR VAL ALA VAL GLY GLU LEU VAL GLU ILE GLN LEU
SEQRES 3 B 110 PRO SER ASN PRO THR THR GLY PHE ALA TRP TYR PHE GLU
SEQRES 4 B 110 GLY GLY THR LYS GLU SER PRO ASN GLU SER MET PHE THR
SEQRES 5 B 110 VAL GLU ASN LYS TYR PHE PRO PRO ASP SER LYS LEU LEU
SEQRES 6 B 110 GLY ALA GLY GLY THR GLU HIS PHE HIS VAL THR VAL LYS
SEQRES 7 B 110 ALA ALA GLY THR HIS ALA VAL ASN LEU THR TYR MET ARG
SEQRES 8 B 110 PRO TRP THR GLY PRO SER HIS ASP SER GLU ARG PHE THR
SEQRES 9 B 110 VAL TYR LEU LYS ALA ASN
FORMUL 3 HOH *63(H2 O)
HELIX 1 1 ALA A 7 TRP A 11 1 5
HELIX 2 2 CYS A 14 GLU A 19 5 6
HELIX 3 3 SER A 28 HIS A 45 1 18
HELIX 4 4 SER A 55 CYS A 63 1 9
HELIX 5 5 GLY A 64 CYS A 67 5 4
HELIX 6 6 ASP A 69 GLY A 73 5 5
HELIX 7 7 TYR A 75 LYS A 86 1 12
HELIX 8 8 THR A 139 ASP A 143 5 5
HELIX 9 9 GLU A 157 GLY A 168 1 12
HELIX 10 10 SER A 178 TYR A 183 1 6
HELIX 11 11 ASP A 238 ILE A 242 5 5
HELIX 12 12 THR B 6 ASN B 10 5 5
HELIX 13 13 ASN B 29 GLY B 33 5 5
HELIX 14 14 PHE B 38 THR B 42 5 5
SHEET 1 A 5 PHE A 5 ASP A 6 0
SHEET 2 A 5 MET A 195 GLU A 209 -1 O TRP A 206 N PHE A 5
SHEET 3 A 5 VAL A 170 TYR A 177 -1 N GLY A 172 O ILE A 201
SHEET 4 A 5 VAL A 246 ALA A 248 -1 O VAL A 247 N GLU A 171
SHEET 5 A 5 TYR A 151 VAL A 153 -1 N VAL A 153 O VAL A 246
SHEET 1 B 5 PHE A 5 ASP A 6 0
SHEET 2 B 5 MET A 195 GLU A 209 -1 O TRP A 206 N PHE A 5
SHEET 3 B 5 THR A 212 ALA A 218 -1 O THR A 212 N GLU A 209
SHEET 4 B 5 PHE A 230 LEU A 234 -1 O PHE A 231 N VAL A 217
SHEET 5 B 5 VAL A 187 TYR A 188 1 N TYR A 188 O LYS A 232
SHEET 1 C 4 HIS B 3 VAL B 5 0
SHEET 2 C 4 LEU B 21 SER B 28 1 O GLU B 23 N VAL B 5
SHEET 3 C 4 GLY B 69 VAL B 77 -1 O GLU B 71 N LEU B 26
SHEET 4 C 4 PHE B 51 PHE B 58 -1 N GLU B 54 O HIS B 74
SHEET 1 D 4 THR B 13 VAL B 16 0
SHEET 2 D 4 GLU B 101 ALA B 109 1 O LYS B 108 N VAL B 16
SHEET 3 D 4 GLY B 81 MET B 90 -1 N LEU B 87 O PHE B 103
SHEET 4 D 4 ALA B 35 TYR B 37 -1 N TYR B 37 O THR B 88
SSBOND 1 CYS A 14 CYS A 43 1555 1555 2.10
SSBOND 2 CYS A 26 CYS A 71 1555 1555 2.09
SSBOND 3 CYS A 62 CYS A 128 1555 1555 2.04
SSBOND 4 CYS A 63 CYS A 67 1555 1555 2.05
SSBOND 5 CYS A 100 CYS A 132 1555 1555 2.13
SSBOND 6 CYS A 108 CYS A 119 1555 1555 2.03
CRYST1 85.066 85.066 115.691 90.00 90.00 90.00 P 42 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 0.011756 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011756 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008644 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
