HEADER HYDROLASE 08-SEP-05 2C0Y
TITLE THE CRYSTAL STRUCTURE OF A CYS25ALA MUTANT OF HUMAN PROCATHEPSIN S
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROCATHEPSIN S;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PROENZYME, RESIDUES 17-331;
COMPND 5 EC: 3.4.22.27;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 ORGAN: TESTIS;
SOURCE 6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HIGH FIVE;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS PROCATHEPSIN S, PROENZYME, PROTEINASE, HYDROLASE, THIOL PROTEASE,
KEYWDS 2 PROSEGMENT BINDING LOOP, GLYCOPROTEIN, LYSOSOME, PROTEASE, ZYMOGEN
EXPDTA X-RAY DIFFRACTION
AUTHOR G.KAULMANN,G.J.PALM,K.SCHILLING,R.HILGENFELD,B.WIEDERANDERS
REVDAT 6 13-DEC-23 2C0Y 1 REMARK
REVDAT 5 24-JUL-19 2C0Y 1 REMARK
REVDAT 4 29-MAY-19 2C0Y 1 REMARK
REVDAT 3 03-APR-19 2C0Y 1 SOURCE
REVDAT 2 24-FEB-09 2C0Y 1 VERSN
REVDAT 1 08-NOV-06 2C0Y 0
JRNL AUTH G.KAULMANN,G.J.PALM,K.SCHILLING,R.HILGENFELD,B.WIEDERANDERS
JRNL TITL THE CRYSTAL STRUCTURE OF A CYS25 -> ALA MUTANT OF HUMAN
JRNL TITL 2 PROCATHEPSIN S ELUCIDATES ENZYME-PROSEQUENCE INTERACTIONS.
JRNL REF PROTEIN SCI. V. 15 2619 2006
JRNL REFN ISSN 0961-8368
JRNL PMID 17075137
JRNL DOI 10.1110/PS.062401806
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.E.MCGRATH,J.T.PALMER,D.BROMME,J.R.SOMOZA
REMARK 1 TITL CRYSTAL STRUCTURE OF HUMAN CATHEPSIN S
REMARK 1 REF PROTEIN SCI. V. 7 1294 1998
REMARK 1 REFN ISSN 0961-8368
REMARK 1 PMID 9655332
REMARK 1 REFERENCE 2
REMARK 1 AUTH J.P.TURKENBURG,M.B.LAMERS,A.M.BRZOZOWSKI,L.M.WRIGHT,
REMARK 1 AUTH 2 R.E.HUBBARD,S.L.STURT,D.H.WILLIAMS
REMARK 1 TITL STRUCTURE OF A CYS25 TO SER MUTANT OF HUMAN CATHEPSIN S
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 58 451 2002
REMARK 1 REFN ISSN 0907-4449
REMARK 1 PMID 11856830
REMARK 1 DOI 10.1107/S0907444901021825
REMARK 1 REFERENCE 3
REMARK 1 AUTH T.A.PAULY,T.SULEA,M.AMMIRATI,J.SIVARAMAN,D.E.DANLEY,
REMARK 1 AUTH 2 M.C.GRIFFOR,A.V.KAMATH,I.K.WANG,E.R.LAIRD,A.P.SEDDON,
REMARK 1 AUTH 3 R.MENARD,M.CYGLER,V.L.RATH
REMARK 1 TITL SPECIFICITY DETERMINANTS OF HUMAN CATHEPSIN S REVEALED BY
REMARK 1 TITL 2 CRYSTAL STRUCTURES OF COMPLEXES
REMARK 1 REF BIOCHEMISTRY V. 42 3203 2003
REMARK 1 REFN ISSN 0006-2960
REMARK 1 PMID 12641451
REMARK 1 DOI 10.1021/BI027308I
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.76
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1874964.900
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.9
REMARK 3 NUMBER OF REFLECTIONS : 19350
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 SET) : 0.198
REMARK 3 FREE R VALUE : 0.242
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 972
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.008
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.14
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1691
REMARK 3 BIN R VALUE (WORKING SET) : 0.2470
REMARK 3 BIN FREE R VALUE : 0.2850
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 87
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.031
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2459
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 242
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.02000
REMARK 3 B22 (A**2) : -0.48000
REMARK 3 B33 (A**2) : 0.50000
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) : 0.23
REMARK 3 ESD FROM SIGMAA (A) : 0.17
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.31
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.23
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.90
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.850
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.770 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.530 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.900 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.920 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.41
REMARK 3 BSOL : 62.27
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2C0Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-SEP-05.
REMARK 100 THE DEPOSITION ID IS D_1290025086.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-JUN-01
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : X13
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.803
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : TRIANGULAR SI (111)
REMARK 200 MONOCHROMATOR AND A CONTINUOUS
REMARK 200 BENT RH-COATED MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19350
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 200 DATA REDUNDANCY : 6.400
REMARK 200 R MERGE (I) : 0.09000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.14
REMARK 200 COMPLETENESS FOR SHELL (%) : 88.5
REMARK 200 DATA REDUNDANCY IN SHELL : 4.10
REMARK 200 R MERGE FOR SHELL (I) : 0.47000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1BY8
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALLISATION WAS PERFORMED BY THE
REMARK 280 HANGING-DROP VAPOUR DIFFUSION METHOD. EQUAL VOLUMES PROCATHEPSIN
REMARK 280 S (CYS25ALA) AT 7.0 MG/ML AND WELL SOLUTION WERE COMBINED AND
REMARK 280 PLACED OVER A WELL CONTAINING 0.1M TRIS/HCL, 0.2M MAGNESIUM
REMARK 280 ACETATE AND 20% PEG 8000, PH 7.5, PH 7.50, VAPOR DIFFUSION,
REMARK 280 HANGING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
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 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
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
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 39.30500
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 39.30500
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 29.93000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 70.27000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 29.93000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 70.27000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 39.30500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 29.93000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 70.27000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 39.30500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 29.93000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 70.27000
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A2053 LIES ON A SPECIAL POSITION.
REMARK 400
REMARK 400 COMPOUND
REMARK 400 PROTEASE RESPONSIBLE FOR THE REMOVAL OF THE INVARIANT CHAIN
REMARK 400 FROM MHC CLASS II MOLECULES
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, CYS 139 TO ALA
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 GLN A 2
REMARK 465 LYS A 93
REMARK 465 SER A 94
REMARK 465 ASN A 95
REMARK 465 PRO A 96
REMARK 465 ASN A 97
REMARK 465 ARG A 98
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 ASN A 28 -5.85 75.53
REMARK 500 ASN A 63 -167.27 -78.93
REMARK 500 ARG A 81 71.81 -105.75
REMARK 500 THR A 91 -98.86 -123.62
REMARK 500 SER A 120 40.20 -97.15
REMARK 500 THR A 157 -135.45 -105.35
REMARK 500 ARG A 240 53.01 -66.52
REMARK 500 ASN A 262 -1.21 -150.00
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A2075 DISTANCE = 6.76 ANGSTROMS
REMARK 700
REMARK 700 SHEET
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
REMARK 700 TWO SHEETS ARE DEFINED.
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1BXF RELATED DB: PDB
REMARK 900 THREE-DIMENSIONAL STRUCTURES OF THE CYSTEINE- PROTEASES CATHEPSINS
REMARK 900 K AND S DEDUCED BY KNOWLEDGE-BASED MODELLING AND ACTIVE-SITE
REMARK 900 CHARACTERISTICS
REMARK 900 RELATED ID: 1GLO RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CYS25SER MUTANT OF HUMAN CATHEPSIN S
REMARK 900 RELATED ID: 1MS6 RELATED DB: PDB
REMARK 900 DIPEPTIDE NITRILE INHIBITOR BOUND TO CATHEPSIN S.
REMARK 900 RELATED ID: 1NPZ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURES OF CATHEPSIN S INHIBITOR COMPLEXES
REMARK 900 RELATED ID: 1NQC RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURES OF CATHEPSIN S INHIBITOR COMPLEXES
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 CLONED WITHOUT SIGNAL PEPTIDE
DBREF 2C0Y A 2 316 UNP P25774 CATS_HUMAN 17 331
SEQADV 2C0Y ALA A 124 UNP P25774 CYS 139 ENGINEERED MUTATION
SEQADV 2C0Y SER A 146 UNP P25774 THR 161 VARIANT
SEQRES 1 A 315 GLN LEU HIS LYS ASP PRO THR LEU ASP HIS HIS TRP HIS
SEQRES 2 A 315 LEU TRP LYS LYS THR TYR GLY LYS GLN TYR LYS GLU LYS
SEQRES 3 A 315 ASN GLU GLU ALA VAL ARG ARG LEU ILE TRP GLU LYS ASN
SEQRES 4 A 315 LEU LYS PHE VAL MET LEU HIS ASN LEU GLU HIS SER MET
SEQRES 5 A 315 GLY MET HIS SER TYR ASP LEU GLY MET ASN HIS LEU GLY
SEQRES 6 A 315 ASP MET THR SER GLU GLU VAL MET SER LEU MET SER SER
SEQRES 7 A 315 LEU ARG VAL PRO SER GLN TRP GLN ARG ASN ILE THR TYR
SEQRES 8 A 315 LYS SER ASN PRO ASN ARG ILE LEU PRO ASP SER VAL ASP
SEQRES 9 A 315 TRP ARG GLU LYS GLY CYS VAL THR GLU VAL LYS TYR GLN
SEQRES 10 A 315 GLY SER CYS GLY ALA ALA TRP ALA PHE SER ALA VAL GLY
SEQRES 11 A 315 ALA LEU GLU ALA GLN LEU LYS LEU LYS THR GLY LYS LEU
SEQRES 12 A 315 VAL SER LEU SER ALA GLN ASN LEU VAL ASP CYS SER THR
SEQRES 13 A 315 GLU LYS TYR GLY ASN LYS GLY CYS ASN GLY GLY PHE MET
SEQRES 14 A 315 THR THR ALA PHE GLN TYR ILE ILE ASP ASN LYS GLY ILE
SEQRES 15 A 315 ASP SER ASP ALA SER TYR PRO TYR LYS ALA MET ASP GLN
SEQRES 16 A 315 LYS CYS GLN TYR ASP SER LYS TYR ARG ALA ALA THR CYS
SEQRES 17 A 315 SER LYS TYR THR GLU LEU PRO TYR GLY ARG GLU ASP VAL
SEQRES 18 A 315 LEU LYS GLU ALA VAL ALA ASN LYS GLY PRO VAL SER VAL
SEQRES 19 A 315 GLY VAL ASP ALA ARG HIS PRO SER PHE PHE LEU TYR ARG
SEQRES 20 A 315 SER GLY VAL TYR TYR GLU PRO SER CYS THR GLN ASN VAL
SEQRES 21 A 315 ASN HIS GLY VAL LEU VAL VAL GLY TYR GLY ASP LEU ASN
SEQRES 22 A 315 GLY LYS GLU TYR TRP LEU VAL LYS ASN SER TRP GLY HIS
SEQRES 23 A 315 ASN PHE GLY GLU GLU GLY TYR ILE ARG MET ALA ARG ASN
SEQRES 24 A 315 LYS GLY ASN HIS CYS GLY ILE ALA SER PHE PRO SER TYR
SEQRES 25 A 315 PRO GLU ILE
FORMUL 2 HOH *242(H2 O)
HELIX 1 1 ASP A 6 THR A 8 5 3
HELIX 2 2 LEU A 9 GLY A 21 1 13
HELIX 3 3 ASN A 28 MET A 53 1 26
HELIX 4 4 ASN A 63 MET A 68 5 6
HELIX 5 5 THR A 69 MET A 77 1 9
HELIX 6 6 SER A 84 ARG A 88 5 5
HELIX 7 7 ALA A 123 GLY A 142 1 20
HELIX 8 8 SER A 148 SER A 156 1 9
HELIX 9 9 THR A 157 GLY A 161 5 5
HELIX 10 10 LYS A 163 GLY A 167 5 5
HELIX 11 11 PHE A 169 LYS A 181 1 13
HELIX 12 12 ASP A 201 LYS A 203 5 3
HELIX 13 13 ARG A 219 LYS A 230 1 12
HELIX 14 14 HIS A 241 LEU A 246 1 6
HELIX 15 15 ASN A 303 ILE A 307 5 5
SHEET 1 AA 6 TYR A 58 LEU A 60 0
SHEET 2 AA 6 TYR A 247 TYR A 252 -1 N ARG A 248 O ASP A 59
SHEET 3 AA 6 TYR A 294 ALA A 298 1 O ARG A 296 N TYR A 252
SHEET 4 AA 6 LYS A 276 LYS A 282 -1 O TRP A 279 N MET A 297
SHEET 5 AA 6 HIS A 263 LEU A 273 -1 O LEU A 266 N LYS A 282
SHEET 6 AA 6 VAL A 104 ASP A 105 -1 O VAL A 104 N TYR A 270
SHEET 1 AB 6 TYR A 58 LEU A 60 0
SHEET 2 AB 6 TYR A 247 TYR A 252 -1 N ARG A 248 O ASP A 59
SHEET 3 AB 6 TYR A 294 ALA A 298 1 O ARG A 296 N TYR A 252
SHEET 4 AB 6 LYS A 276 LYS A 282 -1 O TRP A 279 N MET A 297
SHEET 5 AB 6 HIS A 263 LEU A 273 -1 O LEU A 266 N LYS A 282
SHEET 6 AB 6 VAL A 233 VAL A 237 -1 O VAL A 233 N VAL A 267
SHEET 1 AC 2 ILE A 183 ASP A 184 0
SHEET 2 AC 2 ARG A 205 ALA A 207 -1 N ALA A 206 O ILE A 183
SHEET 1 AD 2 LYS A 211 GLU A 214 0
SHEET 2 AD 2 SER A 312 GLU A 315 -1 O TYR A 313 N THR A 213
SSBOND 1 CYS A 121 CYS A 165 1555 1555 2.04
SSBOND 2 CYS A 155 CYS A 198 1555 1555 2.04
SSBOND 3 CYS A 257 CYS A 305 1555 1555 2.04
CRYST1 59.860 140.540 78.610 90.00 90.00 90.00 C 2 2 21 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 0.016706 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007115 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012721 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
