HEADER HYDROLASE 22-OCT-99 1D8F
TITLE CRYSTAL STRUCTURE OF MMP3 COMPLEXED WITH A PIPERAZINE BASED INHIBITOR.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: STROMELYSIN-1 PRECURSOR;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN;
COMPND 5 SYNONYM: MMP-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 CELL: FIBROBLAST;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS MIXED ALPHA BETA STRUCTURE, ZINC PROTEASE, INHIBITED, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.Y.CHENG,B.DE,S.PIKUL,N.G.ALMSTEAD,M.G.NATCHUS,M.V.ANASTASIO,
AUTHOR 2 S.J.MCPHAIL,C.E.SNIDER,Y.O.TAIWO,L.Y.CHEN
REVDAT 4 07-FEB-24 1D8F 1 REMARK LINK
REVDAT 3 24-FEB-09 1D8F 1 VERSN
REVDAT 2 01-APR-03 1D8F 1 JRNL
REVDAT 1 23-OCT-00 1D8F 0
JRNL AUTH M.CHENG,B.DE,S.PIKUL,N.G.ALMSTEAD,M.G.NATCHUS,M.V.ANASTASIO,
JRNL AUTH 2 S.J.MCPHAIL,C.E.SNIDER,Y.O.TAIWO,L.CHEN,C.M.DUNAWAY,F.GU,
JRNL AUTH 3 M.E.DOWTY,G.E.MIELING,M.J.JANUSZ,S.WANG-WEIGAND
JRNL TITL DESIGN AND SYNTHESIS OF PIPERAZINE-BASED MATRIX
JRNL TITL 2 METALLOPROTEINASE INHIBITORS.
JRNL REF J.MED.CHEM. V. 43 369 2000
JRNL REFN ISSN 0022-2623
JRNL PMID 10669564
JRNL DOI 10.1021/JM990366Q
REMARK 2
REMARK 2 RESOLUTION. 2.40 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) : 2.40
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) (%) : 97.7
REMARK 3 NUMBER OF REFLECTIONS : 12388
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.294
REMARK 3 FREE R VALUE : 0.252
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1225
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 : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
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 : 2722
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 41
REMARK 3 SOLVENT ATOMS : 35
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 8.53
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) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.600
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: EXAMPLES OF _REFINE.DETAILS
REMARK 3
REMARK 3 EXAMPLE 1:
REMARK 3
REMARK 3
REMARK 3 USED WEIGHTED FULL MATRIX LEAST SQUARES PROCEDURE.
REMARK 4
REMARK 4 1D8F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-OCT-99.
REMARK 100 THE DEPOSITION ID IS D_1000009883.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-FEB-96
REMARK 200 TEMPERATURE (KELVIN) : 173
REMARK 200 PH : 8.5
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 RU300
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.548
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 : 14271
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 200 DATA REDUNDANCY : 5.400
REMARK 200 R MERGE (I) : 0.13200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 25.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 82.8
REMARK 200 DATA REDUNDANCY IN SHELL : 4.30
REMARK 200 R MERGE FOR SHELL (I) : 0.23900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.32
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.06
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 6000, SODIUM CHLORIDE, MAGNESIUM
REMARK 280 CHLORIDE, TRIS, PH 8.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K
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 19.13500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 53.29000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.27000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 53.29000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 19.13500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.27000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A MONOMER CONSTRUCTED FROM CHAIN
REMARK 300 A OR CHAIN B.
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 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 SER A 252
REMARK 465 PRO A 253
REMARK 465 GLU A 254
REMARK 465 THR A 255
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 LEU A 108 CA - CB - CG ANGL. DEV. = 16.7 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 ARG A 149 -125.65 40.03
REMARK 500 HIS A 151 -147.13 -140.66
REMARK 500 ASN A 162 -117.15 62.55
REMARK 500 ALA A 213 -14.79 -48.56
REMARK 500 PRO A 221 -5.14 -58.88
REMARK 500 SER A 225 80.61 -69.42
REMARK 500 THR A 227 -39.08 87.34
REMARK 500 ARG B 649 -121.09 40.91
REMARK 500 ASP B 658 -157.74 -87.15
REMARK 500 ASN B 662 -126.28 60.17
REMARK 500 ASP B 689 -154.38 -140.00
REMARK 500 PHE B 710 -158.65 -99.77
REMARK 500 PRO B 721 40.42 -63.98
REMARK 500 THR B 727 -29.78 65.69
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 HOH A 5 O
REMARK 620 2 ASP A 141 O 84.0
REMARK 620 3 GLY A 173 O 101.3 174.2
REMARK 620 4 ASN A 175 O 93.7 99.7 82.6
REMARK 620 5 ASP A 177 OD1 167.7 83.9 90.8 90.3
REMARK 620 N 1 2 3 4
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 HOH A 22 O
REMARK 620 2 ASP A 107 OD2 97.6
REMARK 620 3 ASP A 107 OD1 118.1 50.6
REMARK 620 4 ASP A 182 O 88.5 154.8 144.5
REMARK 620 5 ASP A 182 OD1 160.7 100.3 79.3 72.2
REMARK 620 6 GLU A 184 O 74.3 116.5 77.8 88.7 103.7
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 98.8
REMARK 620 3 HIS A 166 NE2 107.4 121.6
REMARK 620 4 HIS A 179 ND1 99.2 94.5 129.7
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 95.2
REMARK 620 3 GLY A 161 O 85.6 95.4
REMARK 620 4 VAL A 163 O 86.4 174.9 89.5
REMARK 620 5 ASP A 181 OD2 108.4 73.2 162.4 101.7
REMARK 620 6 GLU A 184 OE2 171.6 81.5 87.0 97.6 78.2
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 111.5
REMARK 620 3 HIS A 211 NE2 113.7 92.4
REMARK 620 4 THR B 755 O 135.9 109.1 80.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 805 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 10 O
REMARK 620 2 ASP B 641 O 97.4
REMARK 620 3 GLY B 673 O 76.4 169.3
REMARK 620 4 ASN B 675 O 150.6 95.4 86.4
REMARK 620 5 ASP B 677 OD1 111.6 88.6 101.8 95.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 804 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 607 OD2
REMARK 620 2 ASP B 607 OD1 53.6
REMARK 620 3 ASP B 682 OD1 90.4 94.4
REMARK 620 4 ASP B 682 O 140.8 161.3 76.2
REMARK 620 5 GLU B 684 O 70.9 119.9 108.3 78.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 802 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 651 NE2
REMARK 620 2 ASP B 653 OD2 107.2
REMARK 620 3 HIS B 666 NE2 110.4 117.8
REMARK 620 4 HIS B 679 ND1 104.5 96.9 118.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 803 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 658 OD1
REMARK 620 2 GLY B 659 O 84.6
REMARK 620 3 GLY B 661 O 83.5 80.6
REMARK 620 4 VAL B 663 O 88.4 173.0 97.9
REMARK 620 5 ASP B 681 OD2 97.0 92.2 172.7 89.3
REMARK 620 6 GLU B 684 OE2 166.8 91.1 83.5 95.6 95.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 801 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 701 NE2
REMARK 620 2 HIS B 705 NE2 95.1
REMARK 620 3 HIS B 711 NE2 111.5 97.8
REMARK 620 4 SPI B 901 OA 118.1 97.7 126.0
REMARK 620 5 SPI B 901 OB 109.8 155.1 72.3 72.3
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
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 ZN B 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 805
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SPI B 901
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1CQR RELATED DB: PDB
REMARK 900 1CQR CONTAINS THE SAME PROTEIN COMPLEXED WITH A DIFFERENT INHIBITOR.
REMARK 900 RELATED ID: 1D5J RELATED DB: PDB
REMARK 900 1D5J CONTAINS THE SAME PROTEIN COMPLEXED WITH A DIFFERENT INHIBITOR.
REMARK 900 RELATED ID: 1D7X RELATED DB: PDB
REMARK 900 1D7X CONTAINS THE SAME PROTEIN COMPLEXED WITH A DIFFERENT INHIBITOR.
DBREF 1D8F A 83 255 UNP P08254 MMP3_HUMAN 100 272
DBREF 1D8F B 583 755 UNP P08254 MMP3_HUMAN 100 272
SEQRES 1 A 173 PHE ARG THR PHE PRO GLY ILE PRO LYS TRP ARG LYS THR
SEQRES 2 A 173 HIS LEU THR TYR ARG ILE VAL ASN TYR THR PRO ASP LEU
SEQRES 3 A 173 PRO LYS ASP ALA VAL ASP SER ALA VAL GLU LYS ALA LEU
SEQRES 4 A 173 LYS VAL TRP GLU GLU VAL THR PRO LEU THR PHE SER ARG
SEQRES 5 A 173 LEU TYR GLU GLY GLU ALA ASP ILE MET ILE SER PHE ALA
SEQRES 6 A 173 VAL ARG GLU HIS GLY ASP PHE TYR PRO PHE ASP GLY PRO
SEQRES 7 A 173 GLY ASN VAL LEU ALA HIS ALA TYR ALA PRO GLY PRO GLY
SEQRES 8 A 173 ILE ASN GLY ASP ALA HIS PHE ASP ASP ASP GLU GLN TRP
SEQRES 9 A 173 THR LYS ASP THR THR GLY THR ASN LEU PHE LEU VAL ALA
SEQRES 10 A 173 ALA HIS GLU ILE GLY HIS SER LEU GLY LEU PHE HIS SER
SEQRES 11 A 173 ALA ASN THR GLU ALA LEU MET TYR PRO LEU TYR HIS SER
SEQRES 12 A 173 LEU THR ASP LEU THR ARG PHE ARG LEU SER GLN ASP ASP
SEQRES 13 A 173 ILE ASN GLY ILE GLN SER LEU TYR GLY PRO PRO PRO ASP
SEQRES 14 A 173 SER PRO GLU THR
SEQRES 1 B 173 PHE ARG THR PHE PRO GLY ILE PRO LYS TRP ARG LYS THR
SEQRES 2 B 173 HIS LEU THR TYR ARG ILE VAL ASN TYR THR PRO ASP LEU
SEQRES 3 B 173 PRO LYS ASP ALA VAL ASP SER ALA VAL GLU LYS ALA LEU
SEQRES 4 B 173 LYS VAL TRP GLU GLU VAL THR PRO LEU THR PHE SER ARG
SEQRES 5 B 173 LEU TYR GLU GLY GLU ALA ASP ILE MET ILE SER PHE ALA
SEQRES 6 B 173 VAL ARG GLU HIS GLY ASP PHE TYR PRO PHE ASP GLY PRO
SEQRES 7 B 173 GLY ASN VAL LEU ALA HIS ALA TYR ALA PRO GLY PRO GLY
SEQRES 8 B 173 ILE ASN GLY ASP ALA HIS PHE ASP ASP ASP GLU GLN TRP
SEQRES 9 B 173 THR LYS ASP THR THR GLY THR ASN LEU PHE LEU VAL ALA
SEQRES 10 B 173 ALA HIS GLU ILE GLY HIS SER LEU GLY LEU PHE HIS SER
SEQRES 11 B 173 ALA ASN THR GLU ALA LEU MET TYR PRO LEU TYR HIS SER
SEQRES 12 B 173 LEU THR ASP LEU THR ARG PHE ARG LEU SER GLN ASP ASP
SEQRES 13 B 173 ILE ASN GLY ILE GLN SER LEU TYR GLY PRO PRO PRO ASP
SEQRES 14 B 173 SER PRO GLU THR
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 ZN B 801 1
HET ZN B 802 1
HET CA B 803 1
HET CA B 804 1
HET CA B 805 1
HET SPI B 901 31
HETNAM ZN ZINC ION
HETNAM CA CALCIUM ION
HETNAM SPI N-HYDROXY-1-(4-METHOXYPHENYL)SULFONYL-4-
HETNAM 2 SPI BENZYLOXYCARBONYL-PIPERAZINE-2-CARBOXAMIDE
FORMUL 3 ZN 4(ZN 2+)
FORMUL 5 CA 6(CA 2+)
FORMUL 13 SPI C20 H23 N3 O7 S
FORMUL 14 HOH *35(H2 O)
HELIX 1 1 PRO A 109 GLU A 126 1 18
HELIX 2 2 LEU A 195 GLY A 208 1 14
HELIX 3 3 ASP A 228 PHE A 232 5 5
HELIX 4 4 SER A 235 GLY A 247 1 13
HELIX 5 5 PRO B 609 GLU B 626 1 18
HELIX 6 6 LEU B 695 GLY B 708 1 14
HELIX 7 7 SER B 735 SER B 744 1 10
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 THR A 98
SHEET 4 A 5 ALA A 178 ASP A 181 1 N ALA A 178 O MET A 143
SHEET 5 A 5 ALA A 165 ALA A 167 -1 O HIS A 166 N HIS A 179
SHEET 1 B 2 TRP A 186 THR A 187 0
SHEET 2 B 2 THR A 193 ASN A 194 1 O THR A 193 N THR A 187
SHEET 1 C 5 THR B 631 ARG B 634 0
SHEET 2 C 5 HIS B 596 ILE B 601 1 N LEU B 597 O THR B 631
SHEET 3 C 5 ILE B 642 ALA B 647 1 N ILE B 642 O THR B 598
SHEET 4 C 5 ALA B 678 ASP B 681 1 O ALA B 678 N SER B 645
SHEET 5 C 5 ALA B 665 ALA B 667 -1 O HIS B 666 N HIS B 679
SHEET 1 D 2 TRP B 686 THR B 687 0
SHEET 2 D 2 THR B 693 ASN B 694 1 O THR B 693 N THR B 687
LINK O HOH A 5 CA CA A 305 1555 1555 3.14
LINK O HOH A 22 CA CA A 304 1555 1555 3.37
LINK OD2 ASP A 107 CA CA A 304 1555 1555 2.64
LINK OD1 ASP A 107 CA CA A 304 1555 1555 2.34
LINK O ASP A 141 CA CA A 305 1555 1555 2.36
LINK NE2 HIS A 151 ZN ZN A 302 1555 1555 2.27
LINK OD2 ASP A 153 ZN ZN A 302 1555 1555 1.97
LINK OD1 ASP A 158 CA CA A 303 1555 1555 2.54
LINK O GLY A 159 CA CA A 303 1555 1555 2.33
LINK O GLY A 161 CA CA A 303 1555 1555 2.42
LINK O VAL A 163 CA CA A 303 1555 1555 2.32
LINK NE2 HIS A 166 ZN ZN A 302 1555 1555 2.58
LINK O GLY A 173 CA CA A 305 1555 1555 2.48
LINK O ASN A 175 CA CA A 305 1555 1555 2.36
LINK OD1 ASP A 177 CA CA A 305 1555 1555 2.60
LINK ND1 HIS A 179 ZN ZN A 302 1555 1555 2.16
LINK OD2 ASP A 181 CA CA A 303 1555 1555 2.37
LINK O ASP A 182 CA CA A 304 1555 1555 2.34
LINK OD1 ASP A 182 CA CA A 304 1555 1555 2.84
LINK OE2 GLU A 184 CA CA A 303 1555 1555 2.40
LINK O GLU A 184 CA CA A 304 1555 1555 2.47
LINK NE2 HIS A 201 ZN ZN A 301 1555 1555 2.39
LINK NE2 HIS A 205 ZN ZN A 301 1555 1555 2.36
LINK NE2 HIS A 211 ZN ZN A 301 1555 1555 2.42
LINK ZN ZN A 301 O THR B 755 1555 2464 1.80
LINK O HOH B 10 CA CA B 805 1555 1555 2.40
LINK OD2 ASP B 607 CA CA B 804 1555 1555 2.36
LINK OD1 ASP B 607 CA CA B 804 1555 1555 2.41
LINK O ASP B 641 CA CA B 805 1555 1555 2.40
LINK NE2 HIS B 651 ZN ZN B 802 1555 1555 2.24
LINK OD2 ASP B 653 ZN ZN B 802 1555 1555 1.92
LINK OD1 ASP B 658 CA CA B 803 1555 1555 2.26
LINK O GLY B 659 CA CA B 803 1555 1555 2.39
LINK O GLY B 661 CA CA B 803 1555 1555 2.58
LINK O VAL B 663 CA CA B 803 1555 1555 2.37
LINK NE2 HIS B 666 ZN ZN B 802 1555 1555 2.40
LINK O GLY B 673 CA CA B 805 1555 1555 2.35
LINK O ASN B 675 CA CA B 805 1555 1555 2.50
LINK OD1 ASP B 677 CA CA B 805 1555 1555 2.38
LINK ND1 HIS B 679 ZN ZN B 802 1555 1555 2.18
LINK OD2 ASP B 681 CA CA B 803 1555 1555 2.31
LINK OD1 ASP B 682 CA CA B 804 1555 1555 2.62
LINK O ASP B 682 CA CA B 804 1555 1555 2.38
LINK OE2 GLU B 684 CA CA B 803 1555 1555 2.26
LINK O GLU B 684 CA CA B 804 1555 1555 2.69
LINK NE2 HIS B 701 ZN ZN B 801 1555 1555 2.28
LINK NE2 HIS B 705 ZN ZN B 801 1555 1555 2.38
LINK NE2 HIS B 711 ZN ZN B 801 1555 1555 2.66
LINK ZN ZN B 801 OA SPI B 901 1555 1555 1.85
LINK ZN ZN B 801 OB SPI B 901 1555 1555 2.33
SITE 1 AC1 4 HIS A 201 HIS A 205 HIS A 211 THR B 755
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 3 ASP A 107 ASP A 182 GLU A 184
SITE 1 AC5 4 ASP A 141 GLY A 173 ASN A 175 ASP A 177
SITE 1 AC6 4 HIS B 701 HIS B 705 HIS B 711 SPI B 901
SITE 1 AC7 4 HIS B 651 ASP B 653 HIS B 666 HIS B 679
SITE 1 AC8 6 ASP B 658 GLY B 659 GLY B 661 VAL B 663
SITE 2 AC8 6 ASP B 681 GLU B 684
SITE 1 AC9 3 ASP B 607 ASP B 682 GLU B 684
SITE 1 BC1 5 HOH B 10 ASP B 641 GLY B 673 ASN B 675
SITE 2 BC1 5 ASP B 677
SITE 1 BC2 12 GLY B 588 ASN B 662 LEU B 664 ALA B 665
SITE 2 BC2 12 VAL B 698 HIS B 701 GLU B 702 HIS B 705
SITE 3 BC2 12 HIS B 711 PRO B 721 TYR B 723 ZN B 801
CRYST1 38.270 78.540 106.580 90.00 90.00 90.00 P 21 21 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 0.026130 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012732 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009383 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
