HEADER HYDROLASE 13-FEB-97 1HFS
TITLE CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN FIBROBLAST
TITLE 2 STROMELYSIN-1 INHIBITED WITH THE N-CARBOXY-ALKYL INHIBITOR L-764,004
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: STROMELYSIN-1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: MATRIX METALLOPROTEASE-3, PROTEOGLYCANASE;
COMPND 5 EC: 3.4.24.17;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HYDROLASE, METALLOPROTEASE, MATRIX METALLOPROTEASE-3, PROTEOGLYCANASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.W.BECKER
REVDAT 6 07-FEB-24 1HFS 1 REMARK LINK ATOM
REVDAT 5 29-NOV-17 1HFS 1 HELIX
REVDAT 4 22-FEB-12 1HFS 1 JRNL VERSN
REVDAT 3 24-FEB-09 1HFS 1 VERSN
REVDAT 2 01-APR-03 1HFS 1 JRNL
REVDAT 1 18-FEB-98 1HFS 0
JRNL AUTH C.K.ESSER,R.L.BUGIANESI,C.G.CALDWELL,K.T.CHAPMAN,
JRNL AUTH 2 P.L.DURETTE,N.N.GIROTRA,I.E.KOPKA,T.J.LANZA,D.A.LEVORSE,
JRNL AUTH 3 M.MACCOSS,K.A.OWENS,M.M.PONPIPOM,J.P.SIMEONE,R.K.HARRISON,
JRNL AUTH 4 L.NIEDZWIECKI,J.W.BECKER,A.I.MARCY,M.G.AXEL,A.J.CHRISTEN,
JRNL AUTH 5 J.MCDONNELL,V.L.MOORE,J.M.OLSZEWSKI,C.SAPHOS,D.M.VISCO,
JRNL AUTH 6 F.SHEN,A.COLLETTI,P.A.KRIETER,W.K.HAGMANN
JRNL TITL INHIBITION OF STROMELYSIN-1 (MMP-3) BY P1'-BIPHENYLYLETHYL
JRNL TITL 2 CARBOXYALKYL DIPEPTIDES.
JRNL REF J.MED.CHEM. V. 40 1026 1997
JRNL REFN ISSN 0022-2623
JRNL PMID 9083493
JRNL DOI 10.1021/JM960465T
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH P.R.GOOLEY,J.F.O'CONNELL,A.I.MARCY,G.C.CUCA,M.G.AXEL,
REMARK 1 AUTH 2 C.G.CALDWELL,W.K.HAGMANN,J.W.BECKER
REMARK 1 TITL COMPARISON OF THE STRUCTURE OF HUMAN RECOMBINANT SHORT FORM
REMARK 1 TITL 2 STROMELYSIN BY MULTIDIMENSIONAL HETERONUCLEAR NMR AND X-RAY
REMARK 1 TITL 3 CRYSTALLOGRAPHY
REMARK 1 REF J.BIOMOL.NMR V. 7 8 1996
REMARK 1 REFN ISSN 0925-2738
REMARK 1 REFERENCE 2
REMARK 1 AUTH J.W.BECKER,A.I.MARCY,L.L.ROKOSZ,M.G.AXEL,J.J.BURBAUM,
REMARK 1 AUTH 2 P.M.FITZGERALD,P.M.CAMERON,C.K.ESSER,W.K.HAGMANN,J.D.HERMES,
REMARK 1 AUTH 3 J.P.SPRINGER
REMARK 1 TITL STROMELYSIN-1: THREE-DIMENSIONAL STRUCTURE OF THE INHIBITED
REMARK 1 TITL 2 CATALYTIC DOMAIN AND OF THE C-TRUNCATED PROENZYME
REMARK 1 REF PROTEIN SCI. V. 4 1966 1995
REMARK 1 REFN ISSN 0961-8368
REMARK 1 REFERENCE 3
REMARK 1 AUTH P.R.GOOLEY,J.F.O'CONNELL,A.I.MARCY,G.C.CUCA,S.P.SALOWE,
REMARK 1 AUTH 2 B.L.BUSH,J.D.HERMES,C.K.ESSER,W.K.HAGMANN,J.P.SPRINGER,
REMARK 1 AUTH 3 B.A.JOHNSON
REMARK 1 TITL THE NMR STRUCTURE OF THE INHIBITED CATALYTIC DOMAIN OF HUMAN
REMARK 1 TITL 2 STROMELYSIN-1
REMARK 1 REF NAT.STRUCT.BIOL. V. 1 111 1994
REMARK 1 REFN ISSN 1072-8368
REMARK 1 REFERENCE 4
REMARK 1 AUTH K.T.CHAPMAN,I.E.KOPKA,P.L.DURETTE,C.K.ESSER,T.J.LANZA,
REMARK 1 AUTH 2 M.IZQUIERDO-MARTIN,L.NIEDZWIECKI,B.CHANG,R.K.HARRISON,
REMARK 1 AUTH 3 D.W.KUO,T.Y.LIN,R.L.STEIN,W.K.HAGMANN
REMARK 1 TITL INHIBITION OF MATRIX METALLOPROTEINASES BY N-CARBOXYALKYL
REMARK 1 TITL 2 PEPTIDES
REMARK 1 REF J.MED.CHEM. V. 36 4293 1993
REMARK 1 REFN ISSN 0022-2623
REMARK 1 REFERENCE 5
REMARK 1 AUTH A.I.MARCY,L.L.EIBERGER,R.HARRISON,H.K.CHAN,N.I.HUTCHINSON,
REMARK 1 AUTH 2 W.K.HAGMANN,P.M.CAMERON,D.A.BOULTON,J.D.HERMES
REMARK 1 TITL HUMAN FIBROBLAST STROMELYSIN CATALYTIC DOMAIN: EXPRESSION,
REMARK 1 TITL 2 PURIFICATION, AND CHARACTERIZATION OF A C-TERMINALLY
REMARK 1 TITL 3 TRUNCATED FORM
REMARK 1 REF BIOCHEMISTRY V. 30 6476 1991
REMARK 1 REFN ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 10000000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0010
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 91.5
REMARK 3 NUMBER OF REFLECTIONS : 20353
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) : 0.189
REMARK 3 FREE R VALUE : 0.217
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 985
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.007
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) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.73
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 76.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 800
REMARK 3 BIN R VALUE (WORKING SET) : 0.3390
REMARK 3 BIN FREE R VALUE : 0.2910
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.20
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 35
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.049
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1271
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 57
REMARK 3 SOLVENT ATOMS : 143
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 19.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.19
REMARK 3 ESD FROM SIGMAA (A) : 0.10
REMARK 3 LOW RESOLUTION CUTOFF (A) : 20.0
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.22
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.08
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.00
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.190
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) : 1.300 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.200 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.340 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.640 ; 2.500
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 : SLN004.PAR
REMARK 3 PARAMETER FILE 2 : NULL
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : SLN004.TOP
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 1HFS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000173832.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-AUG-94
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : R-AXIS
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21587
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 200 DATA REDUNDANCY : 3.170
REMARK 200 R MERGE (I) : 0.03380
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR 3.1
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.76
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 27.63000
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 27.63000
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 42.07000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 42.67500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 42.07000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 42.67500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 27.63000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 42.07000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 42.67500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 27.63000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 42.07000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 42.67500
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 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 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 85.35000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 55.26000
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 A 433 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 468 LIES ON A SPECIAL POSITION.
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 ILE A 89 87.98 39.24
REMARK 500 ARG A 149 -132.51 49.96
REMARK 500 ASN A 162 -123.82 54.21
REMARK 500 ASP A 189 -165.24 -115.67
REMARK 500 TYR A 246 -81.16 -110.18
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 CA A 261 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 107 OD2
REMARK 620 2 ASP A 107 OD1 49.7
REMARK 620 3 ASP A 182 O 147.7 155.1
REMARK 620 4 ASP A 182 OD1 87.2 93.2 74.8
REMARK 620 5 GLU A 184 O 75.8 121.5 83.2 105.2
REMARK 620 6 HOH A 313 O 95.6 85.6 104.4 175.1 79.4
REMARK 620 7 HOH A 332 O 127.0 77.9 80.1 89.0 154.4 86.2
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 260 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 141 O
REMARK 620 2 GLY A 173 O 168.6
REMARK 620 3 ASN A 175 O 103.9 87.5
REMARK 620 4 ASP A 177 OD1 84.1 95.9 95.8
REMARK 620 5 HOH A 306 O 86.0 94.7 82.4 169.2
REMARK 620 6 HOH A 312 O 87.2 81.4 167.6 91.0 92.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 258 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 151 NE2
REMARK 620 2 ASP A 153 OD2 104.9
REMARK 620 3 HIS A 166 NE2 119.0 114.2
REMARK 620 4 HIS A 179 ND1 108.5 97.9 110.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 259 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 158 OD1
REMARK 620 2 GLY A 159 O 90.5
REMARK 620 3 GLY A 161 O 89.0 92.3
REMARK 620 4 VAL A 163 O 87.2 177.7 88.1
REMARK 620 5 ASP A 181 OD2 91.0 87.0 179.4 92.5
REMARK 620 6 GLU A 184 OE2 176.3 90.4 87.4 91.9 92.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 257 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 201 NE2
REMARK 620 2 HIS A 205 NE2 103.4
REMARK 620 3 HIS A 211 NE2 108.2 99.6
REMARK 620 4 L04 A 256 O5 111.4 128.8 103.5
REMARK 620 5 L04 A 256 O4 93.3 88.2 154.4 54.4
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: L04
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR THE INHIBITOR L-764,004,
REMARK 800 DENOTED L04 256.
REMARK 800
REMARK 800 SITE_IDENTIFIER: ZN1
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: LIGANDS OF THE CATALYTIC (ZN 257) ZINC ION.
REMARK 800
REMARK 800 SITE_IDENTIFIER: ZN2
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: LIGANDS OF THE STRUCTURAL (ZN 258) ZINC ION.
REMARK 800
REMARK 800 SITE_IDENTIFIER: CA1
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: LIGANDS OF THE CALCIUM ION CA 259.
REMARK 800
REMARK 800 SITE_IDENTIFIER: CA2
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: LIGANDS OF THE CALCIUM ION CA 260.
REMARK 800
REMARK 800 SITE_IDENTIFIER: CA3
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: LIGANDS OF THE CALCIUM ION CA 261.
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 257
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 258
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 259
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 260
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 261
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE L04 A 256
DBREF 1HFS A 88 247 UNP P08254 MMP3_HUMAN 105 264
SEQRES 1 A 160 GLY ILE PRO LYS TRP ARG LYS THR HIS LEU THR TYR ARG
SEQRES 2 A 160 ILE VAL ASN TYR THR PRO ASP LEU PRO LYS ASP ALA VAL
SEQRES 3 A 160 ASP SER ALA VAL GLU LYS ALA LEU LYS VAL TRP GLU GLU
SEQRES 4 A 160 VAL THR PRO LEU THR PHE SER ARG LEU TYR GLU GLY GLU
SEQRES 5 A 160 ALA ASP ILE MET ILE SER PHE ALA VAL ARG GLU HIS GLY
SEQRES 6 A 160 ASP PHE TYR PRO PHE ASP GLY PRO GLY ASN VAL LEU ALA
SEQRES 7 A 160 HIS ALA TYR ALA PRO GLY PRO GLY ILE ASN GLY ASP ALA
SEQRES 8 A 160 HIS PHE ASP ASP ASP GLU GLN TRP THR LYS ASP THR THR
SEQRES 9 A 160 GLY THR ASN LEU PHE LEU VAL ALA ALA HIS GLU ILE GLY
SEQRES 10 A 160 HIS SER LEU GLY LEU PHE HIS SER ALA ASN THR GLU ALA
SEQRES 11 A 160 LEU MET TYR PRO LEU TYR HIS SER LEU THR ASP LEU THR
SEQRES 12 A 160 ARG PHE ARG LEU SER GLN ASP ASP ILE ASN GLY ILE GLN
SEQRES 13 A 160 SER LEU TYR GLY
HET ZN A 257 1
HET ZN A 258 1
HET CA A 259 1
HET CA A 260 1
HET CA A 261 1
HET L04 A 256 52
HETNAM ZN ZINC ION
HETNAM CA CALCIUM ION
HETNAM L04 6-(4'-FLUORO-BIPHENYL-4-YL)-4-(3-METHYL-1-
HETNAM 2 L04 PHENYLCARBAMOYL-BUTYLCARBAMOYL)-2-[4-(1-OXO-1,3-
HETNAM 3 L04 DIHYDRO-ISOINDOL-2-YL)-BUTYL]-HEXANOIC ACID
HETSYN L04 L004
FORMUL 2 ZN 2(ZN 2+)
FORMUL 4 CA 3(CA 2+)
FORMUL 7 L04 C43 H48 F N3 O5
FORMUL 8 HOH *143(H2 O)
HELIX 1 A LYS A 110 GLU A 126 1 17
HELIX 2 B LEU A 195 LEU A 207 1 13
HELIX 3 C GLN A 236 TYR A 246 1 11
SHEET 1 1 5 THR A 131 ARG A 134 0
SHEET 2 1 5 HIS A 96 ILE A 101 1 O LEU A 97 N THR A 131
SHEET 3 1 5 ILE A 142 ALA A 147 1 O ILE A 142 N ARG A 100
SHEET 4 1 5 ASP A 177 ASP A 181 1 O ALA A 178 N SER A 145
SHEET 5 1 5 ALA A 165 TYR A 168 -1 O HIS A 166 N HIS A 179
LINK OD2 ASP A 107 CA CA A 261 1555 1555 2.48
LINK OD1 ASP A 107 CA CA A 261 1555 1555 2.69
LINK O ASP A 141 CA CA A 260 1555 1555 2.38
LINK NE2 HIS A 151 ZN ZN A 258 1555 1555 1.83
LINK OD2 ASP A 153 ZN ZN A 258 1555 1555 2.00
LINK OD1 ASP A 158 CA CA A 259 1555 1555 2.49
LINK O GLY A 159 CA CA A 259 1555 1555 2.29
LINK O GLY A 161 CA CA A 259 1555 1555 2.34
LINK O VAL A 163 CA CA A 259 1555 1555 2.34
LINK NE2 HIS A 166 ZN ZN A 258 1555 1555 1.78
LINK O GLY A 173 CA CA A 260 1555 1555 2.36
LINK O ASN A 175 CA CA A 260 1555 1555 2.38
LINK OD1 ASP A 177 CA CA A 260 1555 1555 2.57
LINK ND1 HIS A 179 ZN ZN A 258 1555 1555 2.01
LINK OD2 ASP A 181 CA CA A 259 1555 1555 2.45
LINK O ASP A 182 CA CA A 261 1555 1555 2.29
LINK OD1 ASP A 182 CA CA A 261 1555 1555 2.60
LINK OE2 GLU A 184 CA CA A 259 1555 1555 2.37
LINK O GLU A 184 CA CA A 261 1555 1555 2.45
LINK NE2 HIS A 201 ZN ZN A 257 1555 1555 1.90
LINK NE2 HIS A 205 ZN ZN A 257 1555 1555 1.93
LINK NE2 HIS A 211 ZN ZN A 257 1555 1555 1.85
LINK O5 L04 A 256 ZN ZN A 257 1555 1555 1.84
LINK O4 L04 A 256 ZN ZN A 257 1555 1555 2.62
LINK CA CA A 260 O HOH A 306 1555 1555 2.29
LINK CA CA A 260 O HOH A 312 1555 1555 2.28
LINK CA CA A 261 O HOH A 313 1555 1555 2.33
LINK CA CA A 261 O HOH A 332 1555 1555 2.32
SITE 1 L04 22 TYR A 155 ASN A 162 VAL A 163 LEU A 164
SITE 2 L04 22 ALA A 165 HIS A 166 TYR A 168 LEU A 197
SITE 3 L04 22 VAL A 198 HIS A 201 GLU A 202 HIS A 205
SITE 4 L04 22 HIS A 211 ALA A 217 LEU A 218 TYR A 220
SITE 5 L04 22 PRO A 221 LEU A 222 TYR A 223 HIS A 224
SITE 6 L04 22 LEU A 226 ZN A 257
SITE 1 ZN1 4 HIS A 201 HIS A 205 HIS A 211 L04 A 256
SITE 1 ZN2 4 HIS A 151 ASP A 153 HIS A 166 HIS A 179
SITE 1 CA1 6 ASP A 158 GLY A 159 GLY A 161 VAL A 163
SITE 2 CA1 6 ASP A 181 GLU A 184
SITE 1 CA2 6 ASP A 141 GLY A 173 ASN A 175 ASP A 177
SITE 2 CA2 6 HOH A 306 HOH A 312
SITE 1 CA3 5 ASP A 107 ASP A 182 GLU A 184 HOH A 313
SITE 2 CA3 5 HOH A 332
SITE 1 AC1 4 HIS A 201 HIS A 205 HIS A 211 L04 A 256
SITE 1 AC2 4 HIS A 151 ASP A 153 HIS A 166 HIS A 179
SITE 1 AC3 6 ASP A 158 GLY A 159 GLY A 161 VAL A 163
SITE 2 AC3 6 ASP A 181 GLU A 184
SITE 1 AC4 6 ASP A 141 GLY A 173 ASN A 175 ASP A 177
SITE 2 AC4 6 HOH A 306 HOH A 312
SITE 1 AC5 5 ASP A 107 ASP A 182 GLU A 184 HOH A 313
SITE 2 AC5 5 HOH A 332
SITE 1 AC6 24 TYR A 155 ASN A 162 VAL A 163 LEU A 164
SITE 2 AC6 24 ALA A 165 HIS A 166 ALA A 167 TYR A 168
SITE 3 AC6 24 HIS A 201 GLU A 202 HIS A 205 HIS A 211
SITE 4 AC6 24 LEU A 218 TYR A 220 PRO A 221 LEU A 222
SITE 5 AC6 24 TYR A 223 HIS A 224 LEU A 226 ZN A 257
SITE 6 AC6 24 HOH A 301 HOH A 307 HOH A 323 HOH A 329
CRYST1 84.140 85.350 55.260 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 0.011885 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011716 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018096 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
