HEADER HYDROLASE (SERINE PROTEASE) 15-OCT-99 1QNJ
TITLE THE STRUCTURE OF NATIVE PORCINE PANCREATIC ELASTASE AT ATOMIC
TITLE 2 RESOLUTION (1.1 A)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ELASTASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PPE;
COMPND 5 EC: 3.4.21.36;
COMPND 6 OTHER_DETAILS: PORCINE PANCREATIC ELASTASE
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE 3 ORGANISM_COMMON: PIG;
SOURCE 4 ORGANISM_TAXID: 9823;
SOURCE 5 ORGAN: PANCREAS
KEYWDS HYDROLASE (SERINE PROTEASE), HYDROLASE(SERINE PROTEASE), ATOMIC
KEYWDS 2 RESOLUTION
EXPDTA X-RAY DIFFRACTION
AUTHOR M.WURTELE,M.HAHN,K.HILPERT,W.HOHNE
REVDAT 7 13-DEC-23 1QNJ 1 REMARK LINK
REVDAT 6 24-JUL-19 1QNJ 1 REMARK
REVDAT 5 22-MAY-19 1QNJ 1 REMARK
REVDAT 4 08-MAY-19 1QNJ 1 REMARK
REVDAT 3 24-FEB-09 1QNJ 1 VERSN
REVDAT 2 25-APR-00 1QNJ 1 PH
REVDAT 1 31-MAR-00 1QNJ 0
JRNL AUTH M.WURTELE,M.HAHN,K.HILPERT,W.HOHNE
JRNL TITL ATOMIC RESOLUTION STRUCTURE OF NATIVE PORCINE PANCREATIC
JRNL TITL 2 ELASTASE AT 1.1 A
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 56 520 2000
JRNL REFN ISSN 0907-4449
JRNL PMID 10739939
JRNL DOI 10.1107/S0907444900000299
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH R.C.WILMOUTH,N.J.WESTWOOD,K.ANDERSON,W.BROWNLEE,
REMARK 1 AUTH 2 T.D.W.CLARIDGE,I.J.CLIFTON,G.J.PRITCHARD,R.T.APLIN,
REMARK 1 AUTH 3 C.J.SCHOFIELD
REMARK 1 TITL INHIBITION OF ELASTASE BY N-SULFONYLARYL BETA-LACTAMS:
REMARK 1 TITL 2 ANATOMY OF A STABLE ACYL-ENZYME COMPLEX
REMARK 1 REF BIOCHEMISTRY V. 37 17506 1998
REMARK 1 REFN ISSN 0006-2960
REMARK 1 PMID 9860865
REMARK 1 DOI 10.1021/BI9816249
REMARK 1 REFERENCE 2
REMARK 1 AUTH E.MEYER,G.COLE,R.RADHAKRISHNAN,O.EPP
REMARK 1 TITL STRUCTURE OF NATIVE PORCINE PANCREATIC ELASTASE AT 1.65
REMARK 1 TITL 2 ANGSTROMS RESOLUTION
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.B V. 44 26 1988
REMARK 1 REFN ISSN 0108-7681
REMARK 1 PMID 3271103
REMARK 1 DOI 10.1107/S0108768187007559
REMARK 1 REFERENCE 3
REMARK 1 AUTH L.SAWYER,D.M.SHOTTON,J.W.CAMPBELL,P.L.WENDELL,H.MUIRHEAD,
REMARK 1 AUTH 2 H.C.WATSON,R.DIAMOND,R.C.LADNER
REMARK 1 TITL THE ATOMIC STRUCTURE OF CRYSTALLINE PORCINE PANCREATIC
REMARK 1 TITL 2 ELASTASE AT 2.5 ANGSTROMS RESOLUTION. COMPARISONS WITH THE
REMARK 1 TITL 3 STRUCTURE OF ALPHA- CHYMOTRYPSIN
REMARK 1 REF J.MOL.BIOL. V. 118 137 1978
REMARK 1 REFN ISSN 0022-2836
REMARK 1 PMID 628010
REMARK 1 DOI 10.1016/0022-2836(78)90412-6
REMARK 1 REFERENCE 4
REMARK 1 AUTH H.C.WATSON,D.M.SHOTTON,J.M.COX,H.MUIRHEAD
REMARK 1 TITL THREE-DIMENSIONAL FOURIER SYNTHESIS OF TOSYL-ELASTASE AT 3.5
REMARK 1 TITL 2 ANGSTROMS RESOLUTION
REMARK 1 REF NATURE V. 225 806 1970
REMARK 1 REFN ISSN 0028-0836
REMARK 1 PMID 5415109
REMARK 1 DOI 10.1038/225806A0
REMARK 2
REMARK 2 RESOLUTION. 1.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : SHELXL-97
REMARK 3 AUTHORS : G.M.SHELDRICK
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.60
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 88.2
REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.127
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.165
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.300
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 4088
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 77673
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : NULL
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : 0.109
REMARK 3 FREE R VALUE (F>4SIG(F)) : 0.148
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 5.300
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : 3204
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 60175
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1822
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 11
REMARK 3 SOLVENT ATOMS : 364
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 2177.0
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 1762.0
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 23
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 19897
REMARK 3 NUMBER OF RESTRAINTS : 24006
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.016
REMARK 3 ANGLE DISTANCES (A) : 0.033
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.029
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.079
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.094
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.088
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.005
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.026
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.103
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: MOEWS & KRETSINGER
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: ANISOTROPIC SCALING APPLIED BY THE
REMARK 3 METHOD OF PARKIN, MOEZZI & HOPE, J.APPL.CRYST.28 (1995)53-56
REMARK 4
REMARK 4 1QNJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-OCT-99.
REMARK 100 THE DEPOSITION ID IS D_1290004208.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-MAR-99
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.00
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 : X11
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9116
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
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 : 81820
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.100
REMARK 200 RESOLUTION RANGE LOW (A) : 45.600
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.7
REMARK 200 DATA REDUNDANCY : 13.10
REMARK 200 R MERGE (I) : 0.04500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.14
REMARK 200 COMPLETENESS FOR SHELL (%) : 60.4
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.35000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.020
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: SHELXL-97
REMARK 200 STARTING MODEL: 1BTU
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 32.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.06
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.25 M NA2SO4 18 DEGREES CELSIUS, PH
REMARK 280 8.00, TEMPERATURE 291K
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 24.95500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 37.13500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 28.91000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 37.13500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.95500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 28.91000
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: 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 400
REMARK 400 COMPOUND
REMARK 400 RESIDUE NUMBERING FOLLOWS THE NUMBERING OF BOVINE
REMARK 400 CHYMOTRYPSINOGEN A.
REMARK 400
REMARK 400 THE RESIDUE ASN-77 OF REFERENCE STRUCTURES WAS CHANGED TO
REMARK 400 ASP-77 IN ORDER TO MATCH WITH DNA SEQUENCE ENTRIES.
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 ASN A 245 C ASN A 245 OXT 0.392
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 ARG A 24 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 HIS A 40 CG - ND1 - CE1 ANGL. DEV. = 12.7 DEGREES
REMARK 500 HIS A 40 ND1 - CE1 - NE2 ANGL. DEV. = -7.6 DEGREES
REMARK 500 HIS A 91 CG - ND1 - CE1 ANGL. DEV. = 8.1 DEGREES
REMARK 500 ASP A 97 CB - CG - OD1 ANGL. DEV. = 6.7 DEGREES
REMARK 500 ASP A 97 CB - CG - OD2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 ARG A 107 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ARG A 107 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ARG A 125 CD - NE - CZ ANGL. DEV. = 22.8 DEGREES
REMARK 500 ARG A 188A CG - CD - NE ANGL. DEV. = 34.1 DEGREES
REMARK 500 ARG A 217A CD - NE - CZ ANGL. DEV. = 13.8 DEGREES
REMARK 500 ARG A 217A NE - CZ - NH1 ANGL. DEV. = 9.5 DEGREES
REMARK 500 ARG A 217A NE - CZ - NH2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 ARG A 223 CD - NE - CZ ANGL. DEV. = 10.3 DEGREES
REMARK 500 ARG A 223 NH1 - CZ - NH2 ANGL. DEV. = -7.1 DEGREES
REMARK 500 ARG A 223 NE - CZ - NH1 ANGL. DEV. = 4.9 DEGREES
REMARK 500 ARG A 223 NE - CZ - NH2 ANGL. DEV. = 7.6 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 HIS A 71 -54.30 -126.37
REMARK 500 TYR A 171 -112.87 -94.41
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 280 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 70 OE1
REMARK 620 2 ASN A 72 O 83.6
REMARK 620 3 GLN A 75 O 165.5 83.0
REMARK 620 4 ASP A 77 OD2 76.9 89.9 97.5
REMARK 620 5 GLU A 80 OE2 99.2 176.5 94.0 88.7
REMARK 620 6 HOH A2108 O 98.5 93.5 87.8 174.0 88.2
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 280
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 290
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 295
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1EST RELATED DB: PDB
REMARK 900 TOSYL-ELASTASE
REMARK 900 RELATED ID: 2EST RELATED DB: PDB
REMARK 900 ELASTASE COMPLEX WITH TFAP
REMARK 900 RELATED ID: 3EST RELATED DB: PDB
REMARK 900 NATIVE ELASTASE
REMARK 900 RELATED ID: 4EST RELATED DB: PDB
REMARK 900 PORCINE PANCREATIC ELASTASE COMPLEX WITH ACE-*ALA-*PRO-*VAL-*
REMARK 900 DIFLUORO-*N-*PHENYLETHYLACETAMIDE
REMARK 900 RELATED ID: 5EST RELATED DB: PDB
REMARK 900 PORCINE PANCREATIC ELASTASE COMPLEX WITH CARBOBENZOXY-*ALANYL-*
REMARK 900 ISOLEUCYLBORONIC ACID
REMARK 900 RELATED ID: 6EST RELATED DB: PDB
REMARK 900 ELASTASE CRYSTALLIZED IN 10% DMF
REMARK 900 RELATED ID: 7EST RELATED DB: PDB
REMARK 900 ELASTASE COMPLEX WITH TFAP
REMARK 900 RELATED ID: 8EST RELATED DB: PDB
REMARK 900 PORCINE PANCREATIC ELASTASE COMPLEX WITH GUANIDINIUM ISOCOUMARIN
REMARK 900 RELATED ID: 9EST RELATED DB: PDB
REMARK 900 PORCINE PANCREATIC ELASTASE COMPLEX WITH GUANIDINIUM ISOCOUMARIN
REMARK 900 RELATED ID: 1INC RELATED DB: PDB
REMARK 900 PORCINE PANCREATIC ELASTASE COMPLEX WITH BENZOXAZINONE INHIBITOR
REMARK 900 RELATED ID: 1JIM RELATED DB: PDB
REMARK 900 PORCINE PANCREATIC ELASTASE COMPLEX WITH THE HETEROCYCLIC INHIBITOR
REMARK 900 3-METHOXY-4-CHLORO-7-AMINOISOCOUMARIN
REMARK 900 RELATED ID: 1ELA RELATED DB: PDB
REMARK 900 ELASTASE COMPLEXED WITH TRIFLUOROACETYL-L- LYSYL-L-PROLYL-P-
REMARK 900 ISOPROPYLANILIDE
REMARK 900 RELATED ID: 1ELB RELATED DB: PDB
REMARK 900 ELASTASE COMPLEXED WITH TRIFLUOROACETYL-L- LYSYL-L-LEUCYL-P-
REMARK 900 ISOPROPYLANILIDE
REMARK 900 RELATED ID: 1ELC RELATED DB: PDB
REMARK 900 ELASTASE COMPLEXED WITH TRIFLUOROACETYL-L- PHENYLALANYL-P-
REMARK 900 ISOPROPYLANILIDE
REMARK 900 RELATED ID: 1ELD RELATED DB: PDB
REMARK 900 ELASTASE COMPLEXED WITH TRIFLUOROACETYL-L- PHENYLALANYL-L-ALANYL-P-
REMARK 900 TRIFLUOROMETHYLANINIDE
REMARK 900 RELATED ID: 1ELE RELATED DB: PDB
REMARK 900 ELASTASE COMPLEXED WITH TRIFLUOROACETYL-L- VALYL-L-ALANYL-P-
REMARK 900 TRIFLUOROMETHYLANINIDE
REMARK 900 RELATED ID: 1ELF RELATED DB: PDB
REMARK 900 ELASTASE COMPLEXED WITH N-(TERT-BUTOXYCARBONYL- ALANYL-ALANYL)-O-(P-
REMARK 900 NITROBENZOYL) HYDROXYLAMINE
REMARK 900 RELATED ID: 1ELG RELATED DB: PDB
REMARK 900 ELASTASE COMPLEXED WITH N-(TERT-BUTOXYCARBONYL- ALANYL-ALANYL)-O-(P-
REMARK 900 NITROBENZOYL) HYDROXYLAMINE AT PH5
REMARK 900 RELATED ID: 1ESA RELATED DB: PDB
REMARK 900 ELASTASE LOW TEMPERATURE FORM (-45 C)
REMARK 900 RELATED ID: 1ESB RELATED DB: PDB
REMARK 900 ELASTASE COMPLEXED WITH N-CARBOBENZOXY-L- ALANYL-P-NITROPHENOL ESTER
REMARK 900 RELATED ID: 1EAI RELATED DB: PDB
REMARK 900 COMPLEX OF ASCARIS CHYMOTRPSIN/ELASTASE INHIBITOR WITH PORCINE
REMARK 900 ELASTASE
REMARK 900 RELATED ID: 1EAS RELATED DB: PDB
REMARK 900 ELASTASE COMPLEXED WITH 3-[[(METHYLAMINO) SULFONYL]AMINO]-2-OXO-6-
REMARK 900 PHENYL-N-[3,3,3- TRIFLUORO-1-(1-METHYLETHYL)-2-OXOPROPYL]-1(2H)-
REMARK 900 PYRIDINEACETAMIDE
REMARK 900 RELATED ID: 1EAT RELATED DB: PDB
REMARK 900 ELASTASE COMPLEXED WITH 2-[5-METHANESULFONYLAMINO-2-(4-AMINOPHENYL)-
REMARK 900 6- OXO-1,6-DIHYDRO-1-PYRIMIDINYL]-N-(3,3,3- TRIFLUORO-1-ISOPROPYL-2-
REMARK 900 OXOPROPYL)ACETAMIDE
REMARK 900 RELATED ID: 1EAU RELATED DB: PDB
REMARK 900 ELASTASE COMPLEXED WITH 2-[5-AMINO-6-OXO-2-(2- THIENYL)-1,6-
REMARK 900 DIHYDROPYRIMIDIN-1-YL)-N-[3,3- DIFLUORO-1-ISOPROPYL-2-OXO-3-(N-(2-
REMARK 900 MORPHOLINOETHYL)CARBAMOYL]PROPYL]ACETAMIDE
REMARK 900 RELATED ID: 1BMA RELATED DB: PDB
REMARK 900 BENZYL METHYL AMINIMIDE INHIBITOR COMPLEXED TO PORCINE PANCREATIC
REMARK 900 ELASTASE
REMARK 900 RELATED ID: 1LVY RELATED DB: PDB
REMARK 900 PORCINE ELASTASE
REMARK 900 RELATED ID: 1NES RELATED DB: PDB
REMARK 900 ELASTASE COMPLEXED WITH ACETYL-ALA-PRO-ALA
REMARK 900 RELATED ID: 1B0E RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PORCINE PANCREATIC ELASTASE MDL 101,146
REMARK 900 RELATED ID: 1BTU RELATED DB: PDB
REMARK 900 PORCINE PANCREATIC ELASTASE COMPLEXED WITH (3S,4R)-1-
REMARK 900 TOLUENESULPHONYL-3-ETHYL-AZETIDIN- 2-ONE-4-CARBOXYLIC ACID
DBREF 1QNJ A 16 245 UNP P00772 EL1_PIG 27 266
SEQRES 1 A 240 VAL VAL GLY GLY THR GLU ALA GLN ARG ASN SER TRP PRO
SEQRES 2 A 240 SER GLN ILE SER LEU GLN TYR ARG SER GLY SER SER TRP
SEQRES 3 A 240 ALA HIS THR CYS GLY GLY THR LEU ILE ARG GLN ASN TRP
SEQRES 4 A 240 VAL MET THR ALA ALA HIS CYS VAL ASP ARG GLU LEU THR
SEQRES 5 A 240 PHE ARG VAL VAL VAL GLY GLU HIS ASN LEU ASN GLN ASN
SEQRES 6 A 240 ASP GLY THR GLU GLN TYR VAL GLY VAL GLN LYS ILE VAL
SEQRES 7 A 240 VAL HIS PRO TYR TRP ASN THR ASP ASP VAL ALA ALA GLY
SEQRES 8 A 240 TYR ASP ILE ALA LEU LEU ARG LEU ALA GLN SER VAL THR
SEQRES 9 A 240 LEU ASN SER TYR VAL GLN LEU GLY VAL LEU PRO ARG ALA
SEQRES 10 A 240 GLY THR ILE LEU ALA ASN ASN SER PRO CYS TYR ILE THR
SEQRES 11 A 240 GLY TRP GLY LEU THR ARG THR ASN GLY GLN LEU ALA GLN
SEQRES 12 A 240 THR LEU GLN GLN ALA TYR LEU PRO THR VAL ASP TYR ALA
SEQRES 13 A 240 ILE CYS SER SER SER SER TYR TRP GLY SER THR VAL LYS
SEQRES 14 A 240 ASN SER MET VAL CYS ALA GLY GLY ASP GLY VAL ARG SER
SEQRES 15 A 240 GLY CYS GLN GLY ASP SER GLY GLY PRO LEU HIS CYS LEU
SEQRES 16 A 240 VAL ASN GLY GLN TYR ALA VAL HIS GLY VAL THR SER PHE
SEQRES 17 A 240 VAL SER ARG LEU GLY CYS ASN VAL THR ARG LYS PRO THR
SEQRES 18 A 240 VAL PHE THR ARG VAL SER ALA TYR ILE SER TRP ILE ASN
SEQRES 19 A 240 ASN VAL ILE ALA SER ASN
HET NA A 280 1
HET SO4 A 290 5
HET SO4 A 295 5
HETNAM NA SODIUM ION
HETNAM SO4 SULFATE ION
FORMUL 2 NA NA 1+
FORMUL 3 SO4 2(O4 S 2-)
FORMUL 5 HOH *364(H2 O)
HELIX 1 1 ALA A 55 ASP A 60 5 6
HELIX 2 2 ASP A 98 GLY A 100 5 5
HELIX 3 3 ASP A 164 SER A 169 1 6
HELIX 4 4 TRP A 172 VAL A 176 5 5
HELIX 5 5 TYR A 234 ASN A 245 1 12
SHEET 1 A 7 GLN A 81 GLY A 84 0
SHEET 2 A 7 PHE A 65 VAL A 68 -1 N VAL A 68 O GLN A 81
SHEET 3 A 7 GLN A 30 SER A 36A-1 N GLN A 34 O ARG A 65A
SHEET 4 A 7 SER A 37 ARG A 48 -1 N GLY A 44 O ILE A 31
SHEET 5 A 7 TRP A 51 THR A 54 -1 N MET A 53 O THR A 45
SHEET 6 A 7 ALA A 104 LEU A 108 -1 N LEU A 106 O VAL A 52
SHEET 7 A 7 VAL A 85 VAL A 90 -1 N VAL A 89 O LEU A 105
SHEET 1 B 6 GLN A 156 TYR A 159 0
SHEET 2 B 6 CYS A 136 GLY A 140 -1 N GLY A 140 O GLN A 156
SHEET 3 B 6 PRO A 198 VAL A 203 -1 N HIS A 200 O TYR A 137
SHEET 4 B 6 GLN A 206 PHE A 215 -1 N GLY A 211 O LEU A 199
SHEET 5 B 6 THR A 226 ARG A 230 -1 N THR A 229 O VAL A 212
SHEET 6 B 6 MET A 180 ALA A 183 -1 N ALA A 183 O THR A 226
SSBOND 1 CYS A 42 CYS A 58 1555 1555 2.05
SSBOND 2 CYS A 136 CYS A 201 1555 1555 2.04
SSBOND 3 CYS A 168 CYS A 182 1555 1555 2.05
SSBOND 4 CYS A 191 CYS A 220 1555 1555 2.04
LINK OE1 GLU A 70 NA NA A 280 1555 1555 2.30
LINK O ASN A 72 NA NA A 280 1555 1555 2.34
LINK O GLN A 75 NA NA A 280 1555 1555 2.32
LINK OD2 ASP A 77 NA NA A 280 1555 1555 2.40
LINK OE2 GLU A 80 NA NA A 280 1555 1555 2.30
LINK NA NA A 280 O BHOH A2108 1555 1555 2.39
SITE 1 AC1 6 GLU A 70 ASN A 72 GLN A 75 ASP A 77
SITE 2 AC1 6 GLU A 80 HOH A2108
SITE 1 AC2 10 HIS A 57 GLN A 192 GLY A 193 SER A 195
SITE 2 AC2 10 HOH A2052 HOH A2359 HOH A2360 HOH A2361
SITE 3 AC2 10 HOH A2362 HOH A2363
SITE 1 AC3 8 GLY A 127 ARG A 145 ARG A 230 SER A 232
SITE 2 AC3 8 ALA A 233 HOH A2205 HOH A2344 HOH A2364
CRYST1 49.910 57.820 74.270 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 0.020036 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017295 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013464 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
