HEADER HYDROLASE 03-FEB-99 1B8Y
TITLE X-RAY STRUCTURE OF HUMAN STROMELYSIN CATALYTIC DOMAIN COMPLEXED WITH
TITLE 2 NON-PEPTIDE INHIBITORS: IMPLICATIONS FOR INHIBITOR SELECTIVITY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (STROMELYSIN-1);
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN;
COMPND 5 SYNONYM: MATRIX METALLOPROTEINASE-3;
COMPND 6 EC: 3.4.24.17;
COMPND 7 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, MATRIX METALLOPROTEINASE-3, STROMELYSIN-1
EXPDTA X-RAY DIFFRACTION
AUTHOR A.G.PAVLOVSKY,M.G.WILLIAMS,Q.-Z.YE,D.F.ORTWINE,C.F.PURCHASE II,
AUTHOR 2 A.D.WHITE,V.DHANARAJ,B.D.ROTH,L.L.JOHNSON,D.HUPE,C.HUMBLET,
AUTHOR 3 T.L.BLUNDELL
REVDAT 8 27-DEC-23 1B8Y 1 REMARK LINK
REVDAT 7 31-JAN-18 1B8Y 1 JRNL
REVDAT 6 24-JAN-18 1B8Y 1 JRNL
REVDAT 5 04-OCT-17 1B8Y 1 REMARK
REVDAT 4 13-JUL-11 1B8Y 1 VERSN
REVDAT 3 24-FEB-09 1B8Y 1 VERSN
REVDAT 2 01-APR-03 1B8Y 1 JRNL
REVDAT 1 31-AUG-99 1B8Y 0
JRNL AUTH A.G.PAVLOVSKY,M.G.WILLIAMS,Q.Z.YE,D.F.ORTWINE,
JRNL AUTH 2 C.F.PURCHASE II,A.D.WHITE,V.DHANARAJ,B.D.ROTH,L.L.JOHNSON,
JRNL AUTH 3 D.HUPE,C.HUMBLET,T.L.BLUNDELL
JRNL TITL X-RAY STRUCTURE OF HUMAN STROMELYSIN CATALYTIC DOMAIN
JRNL TITL 2 COMPLEXED WITH NONPEPTIDE INHIBITORS: IMPLICATIONS FOR
JRNL TITL 3 INHIBITOR SELECTIVITY.
JRNL REF PROTEIN SCI. V. 8 1455 1999
JRNL REFN ISSN 0961-8368
JRNL PMID 10422833
REMARK 2
REMARK 2 RESOLUTION. 2.00 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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.4
REMARK 3 NUMBER OF REFLECTIONS : 12936
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) : 0.197
REMARK 3 FREE R VALUE : 0.214
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1269
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 : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.09
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1379
REMARK 3 BIN R VALUE (WORKING SET) : 0.2150
REMARK 3 BIN FREE R VALUE : 0.2490
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 13.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 180
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 : 1332
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 36
REMARK 3 SOLVENT ATOMS : 86
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.011
REMARK 3 BOND ANGLES (DEGREES) : 2.600
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 27.10
REMARK 3 IMPROPER ANGLES (DEGREES) : 2.000
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
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 : PARAM19X.PRO
REMARK 3 PARAMETER FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPH19X.PRO
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 SIDE CHAINS OF RESIDUES PHE 154, GLU 216 AND ARG 233 ARE
REMARK 3 DISORDERED. TO REFLECT THIS, THEIR SIDE CHAIN ATOM
REMARK 3 OCCUPANCIES ARE SET TO ZERO. THE C TERMINAL PRO 250 IS NOT
REMARK 3 INCLUDED IN THE MODEL BECAUSE OF THE LACK OF ELECTRON
REMARK 3 DENSITY CORRESPONDING TO THIS RESIDUE.
REMARK 4
REMARK 4 1B8Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-FEB-99.
REMARK 100 THE DEPOSITION ID IS D_1000000441.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JUN-95
REMARK 200 TEMPERATURE (KELVIN) : 293
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS, AUTOMAR
REMARK 200 DATA SCALING SOFTWARE : MARSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13572
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 29.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 10.50
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.09100
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) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.10
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 9.10
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.34500
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.35
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.5, VAPOR DIFFUSION, HANGING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
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 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 38.83500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 34.98500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 34.98500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 19.41750
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 34.98500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 34.98500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 58.25250
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 34.98500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 34.98500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 19.41750
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 34.98500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 34.98500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 58.25250
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 38.83500
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 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
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 4080 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14980 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -161.0 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 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 77.67000
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 S SO4 A 501 LIES ON A SPECIAL POSITION.
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 PHE A 154 CG CD1 CD2 CE1 CE2 CZ
REMARK 480 GLU A 216 CG CD OE1 OE2
REMARK 480 ARG A 233 CD NE CZ NH1 NH2
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 93 CD - NE - CZ ANGL. DEV. = 8.7 DEGREES
REMARK 500 ARG A 93 NE - CZ - NH1 ANGL. DEV. = 4.9 DEGREES
REMARK 500 ARG A 93 NE - CZ - NH2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 ARG A 100 NE - CZ - NH1 ANGL. DEV. = 3.6 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 ILE A 89 68.20 33.48
REMARK 500 ARG A 93 65.72 -106.45
REMARK 500 ARG A 149 -128.80 52.43
REMARK 500 HIS A 151 20.80 -145.03
REMARK 500 ASN A 162 -123.93 60.74
REMARK 500 PHE A 210 -149.51 -105.86
REMARK 500 SER A 225 -160.99 -117.07
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 305 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 107 OD2
REMARK 620 2 ASP A 107 OD1 41.1
REMARK 620 3 ASP A 182 O 166.8 152.0
REMARK 620 4 ASP A 182 OD1 97.8 108.9 77.2
REMARK 620 5 GLU A 184 O 75.4 106.5 95.2 113.3
REMARK 620 6 HOH A 401 O 97.8 56.7 95.3 106.3 140.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 304 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 141 O
REMARK 620 2 GLY A 173 O 176.1
REMARK 620 3 ASN A 175 O 98.3 85.5
REMARK 620 4 ASP A 177 OD1 84.4 96.5 96.1
REMARK 620 5 HOH A 403 O 88.2 91.7 73.4 166.2
REMARK 620 6 HOH A 404 O 96.2 79.8 160.5 98.2 94.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 302 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 151 NE2
REMARK 620 2 ASP A 153 OD2 111.7
REMARK 620 3 HIS A 166 NE2 117.8 110.2
REMARK 620 4 HIS A 179 ND1 109.9 97.6 107.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 303 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 158 OD1
REMARK 620 2 GLY A 159 O 85.5
REMARK 620 3 GLY A 161 O 86.1 90.3
REMARK 620 4 VAL A 163 O 88.0 172.8 92.2
REMARK 620 5 ASP A 181 OD2 92.3 87.9 177.7 89.5
REMARK 620 6 GLU A 184 OE2 175.0 93.0 89.1 93.8 92.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 301 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 201 NE2
REMARK 620 2 HIS A 205 NE2 105.2
REMARK 620 3 HIS A 211 NE2 105.7 109.3
REMARK 620 4 IN7 A 502 O4 117.3 123.8 93.3
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: IN7
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: IN7 IS THE BINDING SITE FOR THE
REMARK 800 DIPHENYLPIPERIDINE SULFONAMIDE INHIBITOR.
REMARK 800
REMARK 800 SITE_IDENTIFIER: ZN1
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: ZN1 IS THE CATALYTIC ZINC BINDING SITE OF ZN
REMARK 800 301.
REMARK 800
REMARK 800 SITE_IDENTIFIER: ZN2
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: ZN2 IS THE STRUCTURAL ZINC BINDING SITE OF ZN
REMARK 800 302.
REMARK 800
REMARK 800 SITE_IDENTIFIER: CA1
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: CA1 IS THE FIRST CALCIUM BINDING SITE OF CA 303.
REMARK 800
REMARK 800 SITE_IDENTIFIER: CA2
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: CA2 IS THE SECOND CALCIUM BINDING SITE OF CA
REMARK 800 304.
REMARK 800
REMARK 800 SITE_IDENTIFIER: CA3
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: CA3 IS THE THIRD CALCIUM BINDING SITE OF CA 305.
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IN7 A 502
DBREF 1B8Y A 83 249 UNP P08254 MMP3_HUMAN 100 266
SEQRES 1 A 167 PHE ARG THR PHE PRO GLY ILE PRO LYS TRP ARG LYS THR
SEQRES 2 A 167 HIS LEU THR TYR ARG ILE VAL ASN TYR THR PRO ASP LEU
SEQRES 3 A 167 PRO LYS ASP ALA VAL ASP SER ALA VAL GLU LYS ALA LEU
SEQRES 4 A 167 LYS VAL TRP GLU GLU VAL THR PRO LEU THR PHE SER ARG
SEQRES 5 A 167 LEU TYR GLU GLY GLU ALA ASP ILE MET ILE SER PHE ALA
SEQRES 6 A 167 VAL ARG GLU HIS GLY ASP PHE TYR PRO PHE ASP GLY PRO
SEQRES 7 A 167 GLY ASN VAL LEU ALA HIS ALA TYR ALA PRO GLY PRO GLY
SEQRES 8 A 167 ILE ASN GLY ASP ALA HIS PHE ASP ASP ASP GLU GLN TRP
SEQRES 9 A 167 THR LYS ASP THR THR GLY THR ASN LEU PHE LEU VAL ALA
SEQRES 10 A 167 ALA HIS GLU ILE GLY HIS SER LEU GLY LEU PHE HIS SER
SEQRES 11 A 167 ALA ASN THR GLU ALA LEU MET TYR PRO LEU TYR HIS SER
SEQRES 12 A 167 LEU THR ASP LEU THR ARG PHE ARG LEU SER GLN ASP ASP
SEQRES 13 A 167 ILE ASN GLY ILE GLN SER LEU TYR GLY PRO PRO
HET ZN A 301 1
HET ZN A 302 1
HET CA A 303 1
HET CA A 304 1
HET CA A 305 1
HET SO4 A 501 5
HET IN7 A 502 26
HETNAM ZN ZINC ION
HETNAM CA CALCIUM ION
HETNAM SO4 SULFATE ION
HETNAM IN7 [4-(4-PHENYL-PIPERIDIN-1-YL)-BENZENESULFONYLAMINO]-
HETNAM 2 IN7 ACETIC ACID
FORMUL 2 ZN 2(ZN 2+)
FORMUL 4 CA 3(CA 2+)
FORMUL 7 SO4 O4 S 2-
FORMUL 8 IN7 C19 H22 N2 O4 S
FORMUL 9 HOH *86(H2 O)
HELIX 1 1 LYS A 110 VAL A 127 1 18
HELIX 2 2 LEU A 195 SER A 206 1 12
HELIX 3 3 LEU A 229 ARG A 231 5 3
HELIX 4 4 GLN A 236 TYR A 246 1 11
SHEET 1 A 5 THR A 131 ARG A 134 0
SHEET 2 A 5 HIS A 96 ILE A 101 1 N LEU A 97 O THR A 131
SHEET 3 A 5 ILE A 142 ALA A 147 1 N ILE A 142 O ARG A 100
SHEET 4 A 5 ALA A 178 ASP A 181 1 N ALA A 178 O SER A 145
SHEET 5 A 5 ALA A 165 ALA A 167 -1 N HIS A 166 O HIS A 179
LINK OD2 ASP A 107 CA CA A 305 1555 1555 2.63
LINK OD1 ASP A 107 CA CA A 305 1555 1555 3.24
LINK O ASP A 141 CA CA A 304 1555 1555 2.42
LINK NE2 HIS A 151 ZN ZN A 302 1555 1555 2.17
LINK OD2 ASP A 153 ZN ZN A 302 1555 1555 2.17
LINK OD1 ASP A 158 CA CA A 303 1555 1555 2.52
LINK O GLY A 159 CA CA A 303 1555 1555 2.38
LINK O GLY A 161 CA CA A 303 1555 1555 2.49
LINK O VAL A 163 CA CA A 303 1555 1555 2.44
LINK NE2 HIS A 166 ZN ZN A 302 1555 1555 2.15
LINK O GLY A 173 CA CA A 304 1555 1555 2.44
LINK O ASN A 175 CA CA A 304 1555 1555 2.44
LINK OD1 ASP A 177 CA CA A 304 1555 1555 2.49
LINK ND1 HIS A 179 ZN ZN A 302 1555 1555 2.22
LINK OD2 ASP A 181 CA CA A 303 1555 1555 2.49
LINK O ASP A 182 CA CA A 305 1555 1555 2.68
LINK OD1 ASP A 182 CA CA A 305 1555 1555 2.64
LINK OE2 GLU A 184 CA CA A 303 1555 1555 2.42
LINK O GLU A 184 CA CA A 305 1555 1555 2.50
LINK NE2 HIS A 201 ZN ZN A 301 1555 1555 2.22
LINK NE2 HIS A 205 ZN ZN A 301 1555 1555 2.21
LINK NE2 HIS A 211 ZN ZN A 301 1555 1555 2.22
LINK ZN ZN A 301 O4 IN7 A 502 1555 1555 2.02
LINK CA CA A 304 O HOH A 403 1555 1555 2.56
LINK CA CA A 304 O HOH A 404 1555 1555 2.53
LINK CA CA A 305 O HOH A 401 1555 1555 2.53
SITE 1 IN7 1 IN7 A 502
SITE 1 ZN1 4 HIS A 201 HIS A 205 HIS A 211 IN7 A 502
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 403 HOH A 404
SITE 1 CA3 4 ASP A 107 ASP A 182 GLU A 184 HOH A 401
SITE 1 AC1 4 HIS A 201 HIS A 205 HIS A 211 IN7 A 502
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 403 HOH A 404
SITE 1 AC5 4 ASP A 107 ASP A 182 GLU A 184 HOH A 401
SITE 1 AC6 3 PRO A 109 LYS A 110 HOH A 444
SITE 1 AC7 14 LEU A 164 ALA A 165 HIS A 201 GLU A 202
SITE 2 AC7 14 HIS A 211 ALA A 217 LEU A 218 TYR A 220
SITE 3 AC7 14 PRO A 221 LEU A 222 TYR A 223 HIS A 224
SITE 4 AC7 14 ZN A 301 HOH A 406
CRYST1 69.970 69.970 77.670 90.00 90.00 90.00 P 41 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 0.014292 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014292 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012875 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
