HEADER HYDROLASE/HYDROLASE INHIBITOR 15-FEB-07 2OW1
TITLE MMP-9 ACTIVE SITE MUTANT WITH TRIFLUOROMETHYL HYDROXAMATE INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MATRIX METALLOPROTEINASE-9 (MMP-9) (92 KDA TYPE IV
COMPND 3 COLLAGENASE) (92 KDA GELATINASE) (GELATINASE B) (GELB);
COMPND 4 CHAIN: A, B;
COMPND 5 FRAGMENT: CATALYTIC DOMAIN RESIDUES: 110-215, 391-443;
COMPND 6 EC: 3.4.24.35;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: MMP9, CLG4B;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS MATRIX METALLOPROTEINASE, S1-PRIME POCKET, HYDROLASE-HYDROLASE
KEYWDS 2 INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.TOCHOWICZ,W.BODE,K.MASKOS,P.GOETTIG
REVDAT 7 21-FEB-24 2OW1 1 REMARK
REVDAT 6 20-OCT-21 2OW1 1 REMARK SEQADV LINK
REVDAT 5 16-AUG-17 2OW1 1 SOURCE REMARK
REVDAT 4 13-JUL-11 2OW1 1 VERSN
REVDAT 3 24-FEB-09 2OW1 1 VERSN
REVDAT 2 14-AUG-07 2OW1 1 JRNL
REVDAT 1 19-JUN-07 2OW1 0
JRNL AUTH A.TOCHOWICZ,K.MASKOS,R.HUBER,R.OLTENFREITER,V.DIVE,
JRNL AUTH 2 A.YIOTAKIS,M.ZANDA,W.BODE,P.GOETTIG
JRNL TITL CRYSTAL STRUCTURES OF MMP-9 COMPLEXES WITH FIVE INHIBITORS:
JRNL TITL 2 CONTRIBUTION OF THE FLEXIBLE ARG424 SIDE-CHAIN TO
JRNL TITL 3 SELECTIVITY.
JRNL REF J.MOL.BIOL. V. 371 989 2007
JRNL REFN ISSN 0022-2836
JRNL PMID 17599356
JRNL DOI 10.1016/J.JMB.2007.05.068
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.79
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1446123.950
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 89.4
REMARK 3 NUMBER OF REFLECTIONS : 19604
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) : 0.217
REMARK 3 FREE R VALUE : 0.267
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 950
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.009
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.34
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 84.50
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2875
REMARK 3 BIN R VALUE (WORKING SET) : 0.2100
REMARK 3 BIN FREE R VALUE : 0.3010
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.30
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 130
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.026
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2510
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 69
REMARK 3 SOLVENT ATOMS : 209
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 19.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.14000
REMARK 3 B22 (A**2) : 3.14000
REMARK 3 B33 (A**2) : -6.28000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.26
REMARK 3 ESD FROM SIGMAA (A) : 0.13
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.34
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.26
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.100
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.50
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.760
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) : 1.280 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.950 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.870 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.680 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.38
REMARK 3 BSOL : 46.03
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : DRGCNSB.PAR
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : DRGCNSB.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2OW1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-FEB-07.
REMARK 100 THE DEPOSITION ID IS D_1000041654.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-MAR-05
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : MPG/DESY, HAMBURG
REMARK 200 BEAMLINE : BW6
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0500
REMARK 200 MONOCHROMATOR : SI 111 DOUBLE CHANNEL
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19793
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.150
REMARK 200 RESOLUTION RANGE LOW (A) : 99.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 77.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.04300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 64.8
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.16300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.47
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.83
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 130.22500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 27.86000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 27.86000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 65.11250
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 27.86000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 27.86000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 195.33750
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 27.86000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 27.86000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 65.11250
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 27.86000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 27.86000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 195.33750
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 130.22500
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 350
REMARK 350 BIOMOLECULE: 2
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: 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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10390 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26370 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -380.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350 BIOMT1 2 0.000000 -1.000000 0.000000 55.72000
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 55.72000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 130.22500
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 PHE B 110
REMARK 465 GLU B 111
REMARK 465 GLY B 112
REMARK 465 ASP B 113
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 GLU A 111 CB CG CD OE1 OE2
REMARK 480 ARG A 162 CB CG CD NE CZ NH1 NH2
REMARK 480 GLU A 174 CG CD OE1 OE2
REMARK 480 MET A 422 CG
REMARK 480 ARG A 424 CG CD NE CZ NH1 NH2
REMARK 480 LYS A 433 CG CD CE NZ
REMARK 480 ARG B 162 CB CG CD NE CZ NH1 NH2
REMARK 480 GLU B 174 CG
REMARK 480 LYS B 184 CE NZ
REMARK 480 GLN B 391 CD OE1 NE2
REMARK 480 MET B 422 CG SD CE
REMARK 480 ARG B 424 CD NE CZ NH1 NH2
REMARK 480 LYS B 433 CG CD CE NZ
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 GLU A 111 CD GLU A 111 OE2 0.075
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 ALA A 173 -132.97 54.11
REMARK 500 ASP A 185 -159.98 64.42
REMARK 500 ARG A 424 130.59 -170.97
REMARK 500 ALA B 173 -131.74 48.09
REMARK 500 ASP B 177 12.30 -143.65
REMARK 500 ASP B 185 -169.75 68.44
REMARK 500 SER B 211 -159.19 -146.07
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 448 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 131 OD2
REMARK 620 2 ASP A 206 OD1 120.1
REMARK 620 3 ASP A 206 O 169.1 70.5
REMARK 620 4 GLU A 208 O 79.2 136.7 91.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 449 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 149 O
REMARK 620 2 THR A 152 O 77.1
REMARK 620 3 HOH A 532 O 91.9 80.7
REMARK 620 4 HOH A 576 O 93.7 87.8 165.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 447 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 165 O
REMARK 620 2 GLY A 197 O 171.9
REMARK 620 3 GLN A 199 O 99.9 87.9
REMARK 620 4 ASP A 201 OD1 84.3 97.1 96.1
REMARK 620 5 HOH A 505 O 88.9 90.3 79.5 171.3
REMARK 620 6 HOH A 594 O 85.8 86.2 169.2 93.5 91.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 445 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 175 NE2
REMARK 620 2 ASP A 177 OD2 107.9
REMARK 620 3 HIS A 190 NE2 111.0 120.4
REMARK 620 4 HIS A 203 ND1 106.5 95.9 113.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 446 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 182 OD1
REMARK 620 2 GLY A 183 O 100.2
REMARK 620 3 ASP A 185 O 95.1 84.6
REMARK 620 4 LEU A 187 O 93.1 166.7 94.1
REMARK 620 5 ASP A 205 OD2 90.3 85.5 169.4 94.6
REMARK 620 6 GLU A 208 OE2 167.2 75.1 72.7 91.9 101.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 444 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 401 NE2
REMARK 620 2 HIS A 405 NE2 94.1
REMARK 620 3 HIS A 411 NE2 111.0 94.7
REMARK 620 4 7MR A 501 OAB 103.0 162.7 81.2
REMARK 620 5 7MR A 501 OAA 110.6 94.8 136.5 77.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 448 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 131 OD2
REMARK 620 2 ASP B 206 OD1 92.2
REMARK 620 3 ASP B 206 O 165.7 74.1
REMARK 620 4 GLU B 208 O 89.1 111.3 92.1
REMARK 620 5 HOH B 568 O 102.8 156.2 91.5 87.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 449 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER B 149 O
REMARK 620 2 THR B 152 O 80.5
REMARK 620 3 HOH B 543 O 92.9 91.5
REMARK 620 4 HOH B 583 O 82.5 160.4 79.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 447 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 165 O
REMARK 620 2 GLY B 197 O 164.5
REMARK 620 3 GLN B 199 O 95.8 87.6
REMARK 620 4 ASP B 201 OD1 90.9 103.5 99.1
REMARK 620 5 HOH B 508 O 81.3 83.9 85.0 171.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 445 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 177 OD2
REMARK 620 2 HIS B 190 NE2 113.0
REMARK 620 3 HIS B 203 ND1 93.8 108.7
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 446 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 182 OD1
REMARK 620 2 GLY B 183 O 87.3
REMARK 620 3 ASP B 185 O 83.6 81.1
REMARK 620 4 LEU B 187 O 91.7 179.0 98.6
REMARK 620 5 ASP B 205 OD2 96.1 86.9 168.0 93.4
REMARK 620 6 GLU B 208 OE2 165.7 92.0 82.2 88.9 98.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 444 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 401 NE2
REMARK 620 2 HIS B 405 NE2 96.7
REMARK 620 3 HIS B 411 NE2 106.8 97.4
REMARK 620 4 7MR B 502 OAA 117.2 96.4 131.7
REMARK 620 5 7MR B 502 OAB 98.5 164.7 79.3 75.5
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 444
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 445
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 444
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 445
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 446
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 447
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 448
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 449
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 446
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 447
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 448
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 449
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 450
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 451
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 452
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 7MR A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 7MR B 502
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1GKC RELATED DB: PDB
REMARK 900 RELATED ID: 1GKD RELATED DB: PDB
DBREF 2OW1 A 110 215 UNP P14780 MMP9_HUMAN 110 215
DBREF 2OW1 A 391 443 UNP P14780 MMP9_HUMAN 391 443
DBREF 2OW1 B 110 215 UNP P14780 MMP9_HUMAN 110 215
DBREF 2OW1 B 391 443 UNP P14780 MMP9_HUMAN 391 443
SEQADV 2OW1 GLN A 402 UNP P14780 GLU 402 ENGINEERED MUTATION
SEQADV 2OW1 GLN B 402 UNP P14780 GLU 402 ENGINEERED MUTATION
SEQRES 1 A 159 PHE GLU GLY ASP LEU LYS TRP HIS HIS HIS ASN ILE THR
SEQRES 2 A 159 TYR TRP ILE GLN ASN TYR SER GLU ASP LEU PRO ARG ALA
SEQRES 3 A 159 VAL ILE ASP ASP ALA PHE ALA ARG ALA PHE ALA LEU TRP
SEQRES 4 A 159 SER ALA VAL THR PRO LEU THR PHE THR ARG VAL TYR SER
SEQRES 5 A 159 ARG ASP ALA ASP ILE VAL ILE GLN PHE GLY VAL ALA GLU
SEQRES 6 A 159 HIS GLY ASP GLY TYR PRO PHE ASP GLY LYS ASP GLY LEU
SEQRES 7 A 159 LEU ALA HIS ALA PHE PRO PRO GLY PRO GLY ILE GLN GLY
SEQRES 8 A 159 ASP ALA HIS PHE ASP ASP ASP GLU LEU TRP SER LEU GLY
SEQRES 9 A 159 LYS GLY GLN GLY TYR SER LEU PHE LEU VAL ALA ALA HIS
SEQRES 10 A 159 GLN PHE GLY HIS ALA LEU GLY LEU ASP HIS SER SER VAL
SEQRES 11 A 159 PRO GLU ALA LEU MET TYR PRO MET TYR ARG PHE THR GLU
SEQRES 12 A 159 GLY PRO PRO LEU HIS LYS ASP ASP VAL ASN GLY ILE ARG
SEQRES 13 A 159 HIS LEU TYR
SEQRES 1 B 159 PHE GLU GLY ASP LEU LYS TRP HIS HIS HIS ASN ILE THR
SEQRES 2 B 159 TYR TRP ILE GLN ASN TYR SER GLU ASP LEU PRO ARG ALA
SEQRES 3 B 159 VAL ILE ASP ASP ALA PHE ALA ARG ALA PHE ALA LEU TRP
SEQRES 4 B 159 SER ALA VAL THR PRO LEU THR PHE THR ARG VAL TYR SER
SEQRES 5 B 159 ARG ASP ALA ASP ILE VAL ILE GLN PHE GLY VAL ALA GLU
SEQRES 6 B 159 HIS GLY ASP GLY TYR PRO PHE ASP GLY LYS ASP GLY LEU
SEQRES 7 B 159 LEU ALA HIS ALA PHE PRO PRO GLY PRO GLY ILE GLN GLY
SEQRES 8 B 159 ASP ALA HIS PHE ASP ASP ASP GLU LEU TRP SER LEU GLY
SEQRES 9 B 159 LYS GLY GLN GLY TYR SER LEU PHE LEU VAL ALA ALA HIS
SEQRES 10 B 159 GLN PHE GLY HIS ALA LEU GLY LEU ASP HIS SER SER VAL
SEQRES 11 B 159 PRO GLU ALA LEU MET TYR PRO MET TYR ARG PHE THR GLU
SEQRES 12 B 159 GLY PRO PRO LEU HIS LYS ASP ASP VAL ASN GLY ILE ARG
SEQRES 13 B 159 HIS LEU TYR
HET ZN A 444 1
HET ZN A 445 1
HET CA A 446 1
HET CA A 447 1
HET CA A 448 1
HET CA A 449 1
HET CL A 450 1
HET CL A 451 1
HET CL A 452 1
HET 7MR A 501 27
HET ZN B 444 1
HET ZN B 445 1
HET CA B 446 1
HET CA B 447 1
HET CA B 448 1
HET CA B 449 1
HET 7MR B 502 27
HETNAM ZN ZINC ION
HETNAM CA CALCIUM ION
HETNAM CL CHLORIDE ION
HETNAM 7MR (2R)-2-AMINO-3,3,3-TRIFLUORO-N-HYDROXY-2-{[(4-
HETNAM 2 7MR PHENOXYPHENYL)SULFONYL]METHYL}PROPANAMIDE
FORMUL 3 ZN 4(ZN 2+)
FORMUL 5 CA 8(CA 2+)
FORMUL 9 CL 3(CL 1-)
FORMUL 12 7MR 2(C16 H15 F3 N2 O5 S)
FORMUL 20 HOH *209(H2 O)
HELIX 1 1 PRO A 133 ALA A 150 1 18
HELIX 2 2 LEU A 395 LEU A 407 1 13
HELIX 3 3 HIS A 432 TYR A 443 1 12
HELIX 4 4 PRO B 133 VAL B 151 1 19
HELIX 5 5 LEU B 395 LEU B 407 1 13
HELIX 6 6 HIS B 432 TYR B 443 1 12
SHEET 1 A 5 THR A 155 ARG A 158 0
SHEET 2 A 5 ASN A 120 ILE A 125 1 N ILE A 121 O THR A 157
SHEET 3 A 5 ILE A 166 GLY A 171 1 O ILE A 168 N TRP A 124
SHEET 4 A 5 ALA A 202 ASP A 205 1 O PHE A 204 N GLY A 171
SHEET 5 A 5 ALA A 189 ALA A 191 -1 N HIS A 190 O HIS A 203
SHEET 1 B 2 TRP A 210 SER A 211 0
SHEET 2 B 2 TYR A 393 SER A 394 1 O TYR A 393 N SER A 211
SHEET 1 C 5 THR B 155 VAL B 159 0
SHEET 2 C 5 ASN B 120 ILE B 125 1 N TYR B 123 O VAL B 159
SHEET 3 C 5 ILE B 166 GLY B 171 1 O ILE B 168 N TRP B 124
SHEET 4 C 5 ALA B 202 ASP B 205 1 O PHE B 204 N GLN B 169
SHEET 5 C 5 ALA B 189 ALA B 191 -1 N HIS B 190 O HIS B 203
SHEET 1 D 2 TRP B 210 SER B 211 0
SHEET 2 D 2 TYR B 393 SER B 394 1 O TYR B 393 N SER B 211
LINK OD2 ASP A 131 CA CA A 448 1555 1555 2.44
LINK O SER A 149 CA CA A 449 1555 1555 2.32
LINK O THR A 152 CA CA A 449 1555 1555 2.35
LINK O ASP A 165 CA CA A 447 1555 1555 2.43
LINK NE2 HIS A 175 ZN ZN A 445 1555 1555 1.95
LINK OD2 ASP A 177 ZN ZN A 445 1555 1555 1.94
LINK OD1 ASP A 182 CA CA A 446 1555 1555 2.48
LINK O GLY A 183 CA CA A 446 1555 1555 2.17
LINK O ASP A 185 CA CA A 446 1555 1555 2.37
LINK O LEU A 187 CA CA A 446 1555 1555 2.40
LINK NE2 HIS A 190 ZN ZN A 445 1555 1555 2.01
LINK O GLY A 197 CA CA A 447 1555 1555 2.38
LINK O GLN A 199 CA CA A 447 1555 1555 2.43
LINK OD1 ASP A 201 CA CA A 447 1555 1555 2.48
LINK ND1 HIS A 203 ZN ZN A 445 1555 1555 2.09
LINK OD2 ASP A 205 CA CA A 446 1555 1555 2.38
LINK OD1 ASP A 206 CA CA A 448 1555 1555 2.80
LINK O ASP A 206 CA CA A 448 1555 1555 2.41
LINK OE2 GLU A 208 CA CA A 446 1555 1555 2.13
LINK O GLU A 208 CA CA A 448 1555 1555 2.43
LINK NE2 HIS A 401 ZN ZN A 444 1555 1555 2.08
LINK NE2 HIS A 405 ZN ZN A 444 1555 1555 2.17
LINK NE2 HIS A 411 ZN ZN A 444 1555 1555 2.08
LINK ZN ZN A 444 OAB 7MR A 501 1555 1555 2.23
LINK ZN ZN A 444 OAA 7MR A 501 1555 1555 2.14
LINK CA CA A 447 O HOH A 505 1555 1555 2.50
LINK CA CA A 447 O HOH A 594 1555 1555 2.31
LINK CA CA A 449 O HOH A 532 1555 1555 2.40
LINK CA CA A 449 O HOH A 576 1555 1555 2.54
LINK OD2 ASP B 131 CA CA B 448 1555 1555 2.44
LINK O SER B 149 CA CA B 449 1555 1555 2.34
LINK O THR B 152 CA CA B 449 1555 1555 2.21
LINK O ASP B 165 CA CA B 447 1555 1555 2.47
LINK OD2 ASP B 177 ZN ZN B 445 1555 1555 2.05
LINK OD1 ASP B 182 CA CA B 446 1555 1555 2.32
LINK O GLY B 183 CA CA B 446 1555 1555 2.19
LINK O ASP B 185 CA CA B 446 1555 1555 2.29
LINK O LEU B 187 CA CA B 446 1555 1555 2.28
LINK NE2 HIS B 190 ZN ZN B 445 1555 1555 2.00
LINK O GLY B 197 CA CA B 447 1555 1555 2.47
LINK O GLN B 199 CA CA B 447 1555 1555 2.34
LINK OD1 ASP B 201 CA CA B 447 1555 1555 2.44
LINK ND1 HIS B 203 ZN ZN B 445 1555 1555 2.06
LINK OD2 ASP B 205 CA CA B 446 1555 1555 2.37
LINK OD1 ASP B 206 CA CA B 448 1555 1555 2.70
LINK O ASP B 206 CA CA B 448 1555 1555 2.40
LINK OE2 GLU B 208 CA CA B 446 1555 1555 2.23
LINK O GLU B 208 CA CA B 448 1555 1555 2.33
LINK NE2 HIS B 401 ZN ZN B 444 1555 1555 2.01
LINK NE2 HIS B 405 ZN ZN B 444 1555 1555 2.24
LINK NE2 HIS B 411 ZN ZN B 444 1555 1555 2.05
LINK ZN ZN B 444 OAA 7MR B 502 1555 1555 2.11
LINK ZN ZN B 444 OAB 7MR B 502 1555 1555 2.34
LINK CA CA B 447 O HOH B 508 1555 1555 2.69
LINK CA CA B 448 O HOH B 568 1555 1555 2.40
LINK CA CA B 449 O HOH B 543 1555 1555 2.47
LINK CA CA B 449 O HOH B 583 1555 1555 2.52
SITE 1 AC1 4 HIS A 401 HIS A 405 HIS A 411 7MR A 501
SITE 1 AC2 4 HIS A 175 ASP A 177 HIS A 190 HIS A 203
SITE 1 AC3 4 HIS B 401 HIS B 405 HIS B 411 7MR B 502
SITE 1 AC4 4 HIS B 175 ASP B 177 HIS B 190 HIS B 203
SITE 1 AC5 6 ASP A 182 GLY A 183 ASP A 185 LEU A 187
SITE 2 AC5 6 ASP A 205 GLU A 208
SITE 1 AC6 6 ASP A 165 GLY A 197 GLN A 199 ASP A 201
SITE 2 AC6 6 HOH A 505 HOH A 594
SITE 1 AC7 4 SER A 129 ASP A 131 ASP A 206 GLU A 208
SITE 1 AC8 4 SER A 149 THR A 152 HOH A 532 HOH A 576
SITE 1 AC9 6 ASP B 182 GLY B 183 ASP B 185 LEU B 187
SITE 2 AC9 6 ASP B 205 GLU B 208
SITE 1 BC1 5 ASP B 165 GLY B 197 GLN B 199 ASP B 201
SITE 2 BC1 5 HOH B 508
SITE 1 BC2 4 ASP B 131 ASP B 206 GLU B 208 HOH B 568
SITE 1 BC3 4 SER B 149 THR B 152 HOH B 543 HOH B 583
SITE 1 BC4 3 ASN A 127 TYR A 128 TYR B 128
SITE 1 BC5 4 ASN A 127 GLN A 169 PHE A 170 HOH A 543
SITE 1 BC6 3 GLY A 213 SER A 394 HOH B 509
SITE 1 BC7 15 GLY A 186 LEU A 188 ALA A 189 HIS A 401
SITE 2 BC7 15 GLN A 402 HIS A 405 HIS A 411 LEU A 418
SITE 3 BC7 15 TYR A 420 PRO A 421 MET A 422 TYR A 423
SITE 4 BC7 15 ARG A 424 ZN A 444 HOH A 551
SITE 1 BC8 15 LEU B 187 LEU B 188 ALA B 189 HIS B 401
SITE 2 BC8 15 GLN B 402 HIS B 405 HIS B 411 LEU B 418
SITE 3 BC8 15 TYR B 420 PRO B 421 MET B 422 TYR B 423
SITE 4 BC8 15 ARG B 424 ZN B 444 HOH B 532
CRYST1 55.720 55.720 260.450 90.00 90.00 90.00 P 41 21 2 16
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 0.017947 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017947 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003840 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
