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HEADER HYDROLASE 06-DEC-13 4CI9
TITLE CRYSTAL STRUCTURE OF CATHEPSIN A, APO-STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LYSOSOMAL PROTECTIVE PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CARBOXYPEPTIDASE C, CARBOXYPEPTIDASE L, CATHEPSIN A,
COMPND 5 PROTECTIVE PROTEIN CATHEPSIN A, PPCA, PROTECTIVE PROTEIN FOR
COMPND 6 BETA-GALACTOSIDASE;
COMPND 7 EC: 3.4.16.5;
COMPND 8 ENGINEERED: YES;
COMPND 9 OTHER_DETAILS: ACTIVATED WITH TRYPSIN-SEPHAROSE
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: BACULOVIRUS PVL1393
KEYWDS HYDROLASE, DRUG DISCOVERY, SERINE CARBOXYPEPTIDASE, CARDIOVASCULAR
KEYWDS 2 DRUG, HEART FAILURE, ENDOTHELIN, TETRAHEDRAL INTERMEDIATE, COVALENT
KEYWDS 3 INHIBITOR
EXPDTA X-RAY DIFFRACTION
AUTHOR H.A.SCHREUDER,A.LIESUM,K.KROLL,B.BOEHNISCH,C.BUNING,S.RUF,C.BUNING,
AUTHOR 2 T.SADOWSKI
REVDAT 2 02-APR-14 4CI9 1 JRNL
REVDAT 1 26-FEB-14 4CI9 0
JRNL AUTH H.A.SCHREUDER,A.LIESUM,K.KROLL,B.BOEHNISCH,C.BUNING,S.RUF,
JRNL AUTH 2 T.SADOWSKI
JRNL TITL CRYSTAL STRUCTURE OF CATHEPSIN A, A NOVEL TARGET FOR THE
JRNL TITL 2 TREATMENT OF CARDIOVASCULAR DISEASES.
JRNL REF BIOCHEM.BIOPHYS.RES.COMMUN. V. 445 451 2014
JRNL REFN ISSN 0006-291X
JRNL PMID 24530914
JRNL DOI 10.1016/J.BBRC.2014.02.014
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.RUF,C.BUNING,H.SCHREUDER,G.HORSTICK,W.LINZ,T.OLPP,
REMARK 1 AUTH 2 J.PERNERSTORFER,K.HISS,K.KROLL,A.KANNT,M.KOHLMANN,D.LINZ,
REMARK 1 AUTH 3 T.HUBSCHLE,H.RUTTEN,K.WIRTH,T.SCHMIDT,T.SADOWSKI
REMARK 1 TITL NOVEL BETA-AMINO ACID DERIVATIVES AS INHIBITORS OF
REMARK 1 TITL 2 CATHEPSIN A.
REMARK 1 REF J.MED.CHEM. V. 55 7636 2012
REMARK 1 REFN ISSN 0022-2623
REMARK 1 PMID 22861813
REMARK 1 DOI 10.1021/JM300663N
REMARK 2
REMARK 2 RESOLUTION. 1.58 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.2
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,WOMACK;
REMARK 3 : MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.58
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.44
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.52
REMARK 3 NUMBER OF REFLECTIONS : 56890
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) : 0.1662
REMARK 3 R VALUE (WORKING SET) : 0.1649
REMARK 3 FREE R VALUE : 0.1905
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.00
REMARK 3 FREE R VALUE TEST SET COUNT : 2843
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.58
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.62
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.52
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 3982
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2204
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3780
REMARK 3 BIN R VALUE (WORKING SET) : 0.2196
REMARK 3 BIN FREE R VALUE : 0.2340
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.07
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 202
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3302
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 84
REMARK 3 SOLVENT ATOMS : 614
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 19.14
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.01
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.1215
REMARK 3 B22 (A**2) : 0.3008
REMARK 3 B33 (A**2) : -3.4223
REMARK 3 B12 (A**2) : 0.0000
REMARK 3 B13 (A**2) : 2.4778
REMARK 3 B23 (A**2) : 0.0000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.165
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.089
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.085
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.083
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.081
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.9584
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.9471
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 3576 ; 2.00 ; HARMONIC
REMARK 3 BOND ANGLES : 4882 ; 2.00 ; HARMONIC
REMARK 3 TORSION ANGLES : 1213 ; 2.00 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 99 ; 2.00 ; HARMONIC
REMARK 3 GENERAL PLANES : 520 ; 5.00 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 3576 ; 20.00 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 441 ; 5.00 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : 12 ; 1.00 ; HARMONIC
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 4641 ; 4.00 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 0.91
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.84
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 16.59
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4CI9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-DEC-13.
REMARK 100 THE PDBE ID CODE IS EBI-59176.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-MAR-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL (PILATUS)
REMARK 200 DETECTOR MANUFACTURER : DECTRIS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 56973
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.58
REMARK 200 RESOLUTION RANGE LOW (A) : 33.44
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.6
REMARK 200 DATA REDUNDANCY : 3.3
REMARK 200 R MERGE (I) : 0.04
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 18.10
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.58
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.66
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.3
REMARK 200 DATA REDUNDANCY IN SHELL : 2.3
REMARK 200 R MERGE FOR SHELL (I) : 0.35
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.30
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 4AZ0
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.4
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CATHEPSIN A WAS CRYSTALLIZED
REMARK 280 USING THE HANGING DROP METHOD: 1 UL OF PROTEIN SOLUTION,
REMARK 280 CONTAINING 6.5 MG/ML CATHEPSIN A, 25 MM TRIS-HCL (PH 8.0)
REMARK 280 AND 300 MM NACL, WAS MIXED WITH 1 UL RESERVOIR SOLUTION,
REMARK 280 CONTAINING 100 MM NAACETATE (PH 4.5), 18-20% PEG400 AND
REMARK 280 100 MM CDCL2, AND SET TO EQUILIBRATE AT 4DEG.C. ROD-SHAPED
REMARK 280 CRYSTALS APPEARED IN ABOUT ONE WEEK.
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 X+1/2,Y+1/2,Z
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 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 1.000000 0.000000 0.000000 45.15500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 51.01500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 45.15500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 51.01500
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8430 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33550 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.5 KCAL/MOL
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 BIOMT1 2 -1.000000 0.000000 0.000000 -90.31000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 A2130 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A2350 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A2385 LIES ON A SPECIAL POSITION.
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 HIS A 260
REMARK 465 PHE A 261
REMARK 465 ARG A 262
REMARK 465 TYR A 263
REMARK 465 GLU A 264
REMARK 465 LYS A 265
REMARK 465 ASP A 266
REMARK 465 THR A 267
REMARK 465 VAL A 268
REMARK 465 VAL A 269
REMARK 465 VAL A 270
REMARK 465 GLN A 271
REMARK 465 ASP A 272
REMARK 465 LEU A 273
REMARK 465 GLY A 274
REMARK 465 ASN A 275
REMARK 465 ILE A 276
REMARK 465 PHE A 277
REMARK 465 THR A 278
REMARK 465 ARG A 279
REMARK 465 LEU A 280
REMARK 465 PRO A 281
REMARK 465 LEU A 282
REMARK 465 LYS A 283
REMARK 465 ARG A 284
REMARK 465 MET A 285
REMARK 465 TRP A 286
REMARK 465 HIS A 287
REMARK 465 GLN A 288
REMARK 465 ALA A 289
REMARK 465 LEU A 290
REMARK 465 LEU A 291
REMARK 465 ARG A 292
REMARK 465 SER A 293
REMARK 465 GLY A 294
REMARK 465 ASP A 295
REMARK 465 LYS A 296
REMARK 465 VAL A 297
REMARK 465 ARG A 298
REMARK 465 MET A 299
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 ARG A 9 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 46 CG CD OE1 OE2
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 GLU A 69 -75.21 -109.15
REMARK 500 SER A 150 -114.45 56.79
REMARK 500 GLN A 215 -120.52 64.64
REMARK 500 TYR A 221 -66.26 -97.95
REMARK 500 ASN A 248 97.10 -165.96
REMARK 500 TYR A 402 59.34 -100.01
REMARK 500 MET A 430 79.16 -107.59
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 DMS A 1454
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CAT
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: CATALYTIC TRIAD DOES THE PROTEOLYTIC CLEAVAGE
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A1454
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A1455
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A1456
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1457
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1458
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1459
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR POLY-SACCHARIDE
REMARK 800 RESIDUES NAG A3010 THROUGH NAG A3011 BOUND TO ASN A 117
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR POLY-SACCHARIDE
REMARK 800 RESIDUES NAG A3020 THROUGH NAG A3021 BOUND TO ASN A 305
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4CIA RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CATHEPSIN A, COMPLEXED WITH
REMARK 900 COMPOUND 1
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 AT THE C-TERMINUS, ONE EXTRA GLU IS PRESENT AS A LEFTOVER
REMARK 999 FROM A MYC-TAG
DBREF 4CI9 A 1 452 UNP P10619 PPGB_HUMAN 29 480
SEQADV 4CI9 SER A -1 UNP P10619 EXPRESSION TAG
SEQADV 4CI9 ARG A 0 UNP P10619 EXPRESSION TAG
SEQADV 4CI9 GLU A 453 UNP P10619 EXPRESSION TAG
SEQRES 1 A 455 SER ARG ALA PRO ASP GLN ASP GLU ILE GLN ARG LEU PRO
SEQRES 2 A 455 GLY LEU ALA LYS GLN PRO SER PHE ARG GLN TYR SER GLY
SEQRES 3 A 455 TYR LEU LYS GLY SER GLY SER LYS HIS LEU HIS TYR TRP
SEQRES 4 A 455 PHE VAL GLU SER GLN LYS ASP PRO GLU ASN SER PRO VAL
SEQRES 5 A 455 VAL LEU TRP LEU ASN GLY GLY PRO GLY CYS SER SER LEU
SEQRES 6 A 455 ASP GLY LEU LEU THR GLU HIS GLY PRO PHE LEU VAL GLN
SEQRES 7 A 455 PRO ASP GLY VAL THR LEU GLU TYR ASN PRO TYR SER TRP
SEQRES 8 A 455 ASN LEU ILE ALA ASN VAL LEU TYR LEU GLU SER PRO ALA
SEQRES 9 A 455 GLY VAL GLY PHE SER TYR SER ASP ASP LYS PHE TYR ALA
SEQRES 10 A 455 THR ASN ASP THR GLU VAL ALA GLN SER ASN PHE GLU ALA
SEQRES 11 A 455 LEU GLN ASP PHE PHE ARG LEU PHE PRO GLU TYR LYS ASN
SEQRES 12 A 455 ASN LYS LEU PHE LEU THR GLY GLU SER TYR ALA GLY ILE
SEQRES 13 A 455 TYR ILE PRO THR LEU ALA VAL LEU VAL MET GLN ASP PRO
SEQRES 14 A 455 SER MET ASN LEU GLN GLY LEU ALA VAL GLY ASN GLY LEU
SEQRES 15 A 455 SER SER TYR GLU GLN ASN ASP ASN SER LEU VAL TYR PHE
SEQRES 16 A 455 ALA TYR TYR HIS GLY LEU LEU GLY ASN ARG LEU TRP SER
SEQRES 17 A 455 SER LEU GLN THR HIS CYS CYS SER GLN ASN LYS CYS ASN
SEQRES 18 A 455 PHE TYR ASP ASN LYS ASP LEU GLU CYS VAL THR ASN LEU
SEQRES 19 A 455 GLN GLU VAL ALA ARG ILE VAL GLY ASN SER GLY LEU ASN
SEQRES 20 A 455 ILE TYR ASN LEU TYR ALA PRO CYS ALA GLY GLY VAL PRO
SEQRES 21 A 455 SER HIS PHE ARG TYR GLU LYS ASP THR VAL VAL VAL GLN
SEQRES 22 A 455 ASP LEU GLY ASN ILE PHE THR ARG LEU PRO LEU LYS ARG
SEQRES 23 A 455 MET TRP HIS GLN ALA LEU LEU ARG SER GLY ASP LYS VAL
SEQRES 24 A 455 ARG MET ASP PRO PRO CYS THR ASN THR THR ALA ALA SER
SEQRES 25 A 455 THR TYR LEU ASN ASN PRO TYR VAL ARG LYS ALA LEU ASN
SEQRES 26 A 455 ILE PRO GLU GLN LEU PRO GLN TRP ASP MET CYS ASN PHE
SEQRES 27 A 455 LEU VAL ASN LEU GLN TYR ARG ARG LEU TYR ARG SER MET
SEQRES 28 A 455 ASN SER GLN TYR LEU LYS LEU LEU SER SER GLN LYS TYR
SEQRES 29 A 455 GLN ILE LEU LEU TYR ASN GLY ASP VAL ASP MET ALA CYS
SEQRES 30 A 455 ASN PHE MET GLY ASP GLU TRP PHE VAL ASP SER LEU ASN
SEQRES 31 A 455 GLN LYS MET GLU VAL GLN ARG ARG PRO TRP LEU VAL LYS
SEQRES 32 A 455 TYR GLY ASP SER GLY GLU GLN ILE ALA GLY PHE VAL LYS
SEQRES 33 A 455 GLU PHE SER HIS ILE ALA PHE LEU THR ILE LYS GLY ALA
SEQRES 34 A 455 GLY HIS MET VAL PRO THR ASP LYS PRO LEU ALA ALA PHE
SEQRES 35 A 455 THR MET PHE SER ARG PHE LEU ASN LYS GLN PRO TYR GLU
HET NAG A3010 14
HET NAG A3011 14
HET NAG A3020 14
HET NAG A3021 14
HET DMS A1454 3
HET ACT A1455 4
HET ACT A1456 4
HET GOL A1457 6
HET GOL A1458 6
HET SO4 A1459 5
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETNAM DMS DIMETHYL SULFOXIDE
HETNAM ACT ACETATE ION
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 SO4 O4 S 2-
FORMUL 3 GOL 2(C3 H8 O3)
FORMUL 4 DMS C2 H6 O S
FORMUL 5 ACT 2(C2 H3 O2 1-)
FORMUL 6 NAG 4(C8 H15 N O6)
FORMUL 7 HOH *614(H2 O)
HELIX 1 1 PRO A 2 ASP A 5 5 4
HELIX 2 2 SER A 62 GLU A 69 1 8
HELIX 3 3 SER A 88 ILE A 92 5 5
HELIX 4 4 ASN A 117 PHE A 136 1 20
HELIX 5 5 PRO A 137 LYS A 140 5 4
HELIX 6 6 TYR A 151 GLN A 165 1 15
HELIX 7 7 SER A 182 HIS A 197 1 16
HELIX 8 8 GLY A 201 CYS A 212 1 12
HELIX 9 9 ASP A 225 ASN A 241 1 17
HELIX 10 10 THR A 306 ASN A 314 1 9
HELIX 11 11 ASN A 315 LEU A 322 1 8
HELIX 12 12 ASN A 335 TYR A 342 1 8
HELIX 13 13 MET A 349 SER A 359 1 11
HELIX 14 14 ASN A 376 LEU A 387 1 12
HELIX 15 15 GLY A 403 SER A 405 5 3
HELIX 16 16 MET A 430 LYS A 435 1 6
HELIX 17 17 LYS A 435 ASN A 448 1 14
SHEET 1 AA 2 GLN A 21 LYS A 27 0
SHEET 2 AA 2 LYS A 32 VAL A 39 -1 O LEU A 34 N LEU A 26
SHEET 1 AB 2 TYR A 108 SER A 109 0
SHEET 2 AB 2 LYS A 32 VAL A 39 1 O HIS A 33 N TYR A 108
SHEET 1 AC10 ARG A 396 LYS A 401 0
SHEET 2 AC10 GLU A 407 PHE A 416 -1 O GLN A 408 N VAL A 400
SHEET 3 AC10 ILE A 419 ILE A 424 -1 O ILE A 419 N PHE A 416
SHEET 4 AC10 GLN A 363 GLY A 369 1 O ILE A 364 N ALA A 420
SHEET 5 AC10 LEU A 171 GLY A 177 1 O GLN A 172 N GLN A 363
SHEET 6 AC10 LEU A 144 GLU A 149 1 O LEU A 144 N GLN A 172
SHEET 7 AC10 VAL A 50 LEU A 54 1 O VAL A 50 N PHE A 145
SHEET 8 AC10 ASN A 94 LEU A 98 1 O ASN A 94 N VAL A 51
SHEET 9 AC10 LYS A 32 VAL A 39 -1 O TRP A 37 N TYR A 97
SHEET 10 AC10 TYR A 108 SER A 109 1 O TYR A 108 N HIS A 33
SHEET 1 AD10 ARG A 396 LYS A 401 0
SHEET 2 AD10 GLU A 407 PHE A 416 -1 O GLN A 408 N VAL A 400
SHEET 3 AD10 ILE A 419 ILE A 424 -1 O ILE A 419 N PHE A 416
SHEET 4 AD10 GLN A 363 GLY A 369 1 O ILE A 364 N ALA A 420
SHEET 5 AD10 LEU A 171 GLY A 177 1 O GLN A 172 N GLN A 363
SHEET 6 AD10 LEU A 144 GLU A 149 1 O LEU A 144 N GLN A 172
SHEET 7 AD10 VAL A 50 LEU A 54 1 O VAL A 50 N PHE A 145
SHEET 8 AD10 ASN A 94 LEU A 98 1 O ASN A 94 N VAL A 51
SHEET 9 AD10 LYS A 32 VAL A 39 -1 O TRP A 37 N TYR A 97
SHEET 10 AD10 GLN A 21 LYS A 27 -1 O TYR A 22 N PHE A 38
SHEET 1 AE 2 PHE A 73 VAL A 75 0
SHEET 2 AE 2 LEU A 82 TYR A 84 -1 O GLU A 83 N LEU A 74
SHEET 1 AF 2 CYS A 213 SER A 214 0
SHEET 2 AF 2 LYS A 217 CYS A 218 -1 O LYS A 217 N SER A 214
SSBOND 1 CYS A 60 CYS A 334 1555 1555 2.04
SSBOND 2 CYS A 212 CYS A 228 1555 1555 2.03
SSBOND 3 CYS A 213 CYS A 218 1555 1555 2.03
SSBOND 4 CYS A 253 CYS A 303 1555 1555 2.04
LINK ND2 ASN A 117 C1 NAG A3010 1555 1555 1.43
LINK ND2 ASN A 305 C1 NAG A3020 1555 1555 1.43
LINK O4 NAG A3010 C1 NAG A3011 1555 1555 1.42
LINK O4 NAG A3020 C1 NAG A3021 1555 1555 1.42
CISPEP 1 GLY A 57 PRO A 58 0 -2.06
CISPEP 2 SER A 100 PRO A 101 0 -1.58
SITE 1 CAT 3 SER A 150 ASP A 372 HIS A 429
SITE 1 AC1 3 PRO A 86 LEU A 437 PHE A 440
SITE 1 AC2 3 TYR A 183 ARG A 344 ARG A 347
SITE 1 AC3 4 ASN A 55 GLY A 56 GLU A 149 HIS A 429
SITE 1 AC4 8 TYR A 247 ASN A 248 GLY A 428 HIS A 429
SITE 2 AC4 8 MET A 430 ASP A 434 HOH A2592 HOH A2593
SITE 1 AC5 8 SER A 182 GLN A 185 SER A 348 ASN A 350
SITE 2 AC5 8 PHE A 383 SER A 386 HOH A2327 HOH A2594
SITE 1 AC6 8 GLY A 201 ARG A 203 LEU A 204 GLN A 394
SITE 2 AC6 8 ARG A 395 LYS A 414 HOH A2355 HOH A2558
SITE 1 AC7 9 ASN A 117 GLU A 120 ARG A 343 HOH A2238
SITE 2 AC7 9 HOH A2248 HOH A2595 HOH A2598 HOH A2600
SITE 3 AC7 9 HOH A2601
SITE 1 AC8 11 PRO A 77 ASP A 78 GLY A 255 ASN A 305
SITE 2 AC8 11 HOH A2428 HOH A2603 HOH A2604 HOH A2605
SITE 3 AC8 11 HOH A2606 HOH A2608 HOH A2609
CRYST1 90.310 102.030 48.550 90.00 101.27 90.00 C 1 2 1 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 0.011073 0.000000 0.002207 0.00000
SCALE2 0.000000 0.009801 0.000000 0.00000
SCALE3 0.000000 0.000000 0.021002 0.00000
TER 3389 GLU A 453
MASTER 378 0 10 17 28 0 16 6 4086 1 94 35
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