HEADER HYDROLASE 21-FEB-07 2OXW
TITLE HUMAN MMP-12 COMPLEXED WITH THE PEPTIDE IAG
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MACROPHAGE METALLOELASTASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN;
COMPND 5 SYNONYM: HME, MATRIX METALLOPROTEINASE-12, MMP-12, MACROPHAGE
COMPND 6 ELASTASE, ME;
COMPND 7 EC: 3.4.24.65;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES;
COMPND 10 MOL_ID: 2;
COMPND 11 MOLECULE: ILE-ALA-GLY PEPTIDE;
COMPND 12 CHAIN: X;
COMPND 13 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: MMP12, HME;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21DE3;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET21;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES
KEYWDS MMP-12, MATRIX METALLOPROTEINASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR V.CALDERONE,I.BERTINI,M.FRAGAI,C.LUCHINAT,M.MALETTA,K.J.YEO
REVDAT 5 30-AUG-23 2OXW 1 REMARK
REVDAT 4 20-OCT-21 2OXW 1 REMARK SEQADV LINK
REVDAT 3 24-FEB-09 2OXW 1 VERSN
REVDAT 2 13-MAR-07 2OXW 1 REMARK
REVDAT 1 06-MAR-07 2OXW 0
JRNL AUTH I.BERTINI,V.CALDERONE,M.FRAGAI,C.LUCHINAT,M.MALETTA,K.J.YEO
JRNL TITL SNAPSHOTS OF THE REACTION MECHANISM OF MATRIX
JRNL TITL 2 METALLOPROTEINASES.
JRNL REF ANGEW.CHEM.INT.ED.ENGL. V. 45 7952 2006
JRNL REFN ESSN 0570-0833
JRNL PMID 17096442
JRNL DOI 10.1002/ANIE.200603100
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH I.BERTINI,V.CALDERONE,M.COSENZA,M.FRAGAI,Y.-M.LEE,
REMARK 1 AUTH 2 C.LUCHINAT,S.MANGANI,B.TERNI,P.TURANO
REMARK 1 TITL CONFORMATIONAL VARIABILITY OF MATRIX METALLOPROTEINASES:
REMARK 1 TITL 2 BEYOND A SINGLE 3D STRUCTURE.
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 102 5334 2005
REMARK 1 REFN ISSN 0027-8424
REMARK 2
REMARK 2 RESOLUTION. 1.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.96
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 46196
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 + TEST SET) : 0.199
REMARK 3 R VALUE (WORKING SET) : 0.197
REMARK 3 FREE R VALUE : 0.223
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.200
REMARK 3 FREE R VALUE TEST SET COUNT : 4653
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) : 1.15
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.18
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3279
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2760
REMARK 3 BIN FREE R VALUE SET COUNT : 365
REMARK 3 BIN FREE R VALUE : 0.2900
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1255
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 5
REMARK 3 SOLVENT ATOMS : 199
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 11.08
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.16
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.07000
REMARK 3 B22 (A**2) : 0.11000
REMARK 3 B33 (A**2) : -0.12000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.08000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.049
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.047
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.024
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.055
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.947
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1291 ; 0.007 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 1117 ; 0.009 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1750 ; 1.093 ; 1.915
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2586 ; 0.978 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 159 ; 5.769 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 63 ;33.255 ;23.175
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 190 ;10.507 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 7 ;10.841 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 181 ; 0.067 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1476 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 292 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 300 ; 0.223 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 1132 ; 0.186 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 653 ; 0.185 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 659 ; 0.084 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 103 ; 0.097 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 20 ; 0.084 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 12 ; 0.195 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 47 ; 0.200 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 24 ; 0.158 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 806 ; 0.897 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 340 ; 0.357 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1260 ; 1.315 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 554 ; 1.655 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 490 ; 2.304 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 2730 ; 1.756 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 204 ; 3.282 ; 3.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 2372 ; 2.019 ; 3.000
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2OXW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-07.
REMARK 100 THE DEPOSITION ID IS D_1000041720.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-MAY-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.07225
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL, SI(111) OR
REMARK 200 SI(311)
REMARK 200 OPTICS : DOUBLE CRYSTAL, SI(111) OR
REMARK 200 SI(311)
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 50850
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.150
REMARK 200 RESOLUTION RANGE LOW (A) : 49.080
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.6
REMARK 200 DATA REDUNDANCY : 6.800
REMARK 200 R MERGE (I) : 0.05900
REMARK 200 R SYM (I) : 0.05900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 4.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.21
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.1
REMARK 200 DATA REDUNDANCY IN SHELL : 6.80
REMARK 200 R MERGE FOR SHELL (I) : 0.15600
REMARK 200 R SYM FOR SHELL (I) : 0.15600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1Y93
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.81
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS-HCL, 30% PEG6000, PH 8.0,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 25.94400
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.17900
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 25.94400
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 30.17900
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 860 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 8150 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -65.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, X
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 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 312 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 360 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 386 LIES ON A SPECIAL POSITION.
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 MET A 105
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 HIS A 168 34.19 -146.47
REMARK 500 HIS A 206 -155.37 -134.77
REMARK 500 PRO A 238 31.49 -85.42
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 267 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 124 OD1
REMARK 620 2 ASP A 124 OD2 52.3
REMARK 620 3 GLU A 199 O 160.6 139.3
REMARK 620 4 GLU A 199 OE2 85.7 85.0 80.9
REMARK 620 5 GLU A 201 O 122.4 76.8 76.7 118.1
REMARK 620 6 HOH A 277 O 89.0 102.2 100.5 165.8 75.8
REMARK 620 7 HOH A 278 O 83.5 135.7 82.0 88.4 142.2 77.9
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 266 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 158 O
REMARK 620 2 GLY A 190 O 169.3
REMARK 620 3 GLY A 192 O 90.2 91.0
REMARK 620 4 ASP A 194 OD2 89.2 101.5 86.6
REMARK 620 5 HOH A 281 O 85.0 84.9 78.7 164.1
REMARK 620 6 HOH A 321 O 94.9 82.8 171.6 100.2 95.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 265 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 168 NE2
REMARK 620 2 ASP A 170 OD1 108.7
REMARK 620 3 HIS A 183 NE2 147.2 83.5
REMARK 620 4 HIS A 196 ND1 107.4 98.2 100.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 268 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 175 OD2
REMARK 620 2 GLY A 176 O 88.3
REMARK 620 3 GLY A 178 O 89.5 87.0
REMARK 620 4 ILE A 180 O 87.7 176.0 92.6
REMARK 620 5 ASP A 198 OD1 91.6 88.4 175.2 92.1
REMARK 620 6 GLU A 201 OE2 178.2 93.4 89.9 90.6 89.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 264 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 218 NE2
REMARK 620 2 HIS A 222 NE2 97.5
REMARK 620 3 HIS A 228 NE2 106.2 98.5
REMARK 620 4 HOH A 314 O 95.7 93.9 153.0
REMARK 620 N 1 2 3
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 264
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 265
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 266
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 267
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 268
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2OXU RELATED DB: PDB
REMARK 900 UNINHIBITED FORM OF HUMAN MMP-12
REMARK 900 RELATED ID: 1Y93 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN MMP12 COMPLEXED
REMARK 900 WITH ACETOHYDROXAMIC ACID AT ATOMIC RESOLUTION
REMARK 900 RELATED ID: 1RMZ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN MMP12 COMPLEXED
REMARK 900 WITH THE INHIBITOR NNGH AT 1.3 A RESOLUTION
REMARK 900 RELATED ID: 2OXZ RELATED DB: PDB
REMARK 900 RELATED ID: 2OY2 RELATED DB: PDB
REMARK 900 RELATED ID: 2OY4 RELATED DB: PDB
DBREF 2OXW A 106 263 UNP P39900 MMP12_HUMAN 106 263
DBREF 2OXW X 207 209 PDB 2OXW 2OXW 207 209
SEQADV 2OXW MET A 105 UNP P39900 INITIATING METHIONINE
SEQADV 2OXW ASP A 171 UNP P39900 PHE 171 ENGINEERED MUTATION
SEQRES 1 A 159 MET GLY PRO VAL TRP ARG LYS HIS TYR ILE THR TYR ARG
SEQRES 2 A 159 ILE ASN ASN TYR THR PRO ASP MET ASN ARG GLU ASP VAL
SEQRES 3 A 159 ASP TYR ALA ILE ARG LYS ALA PHE GLN VAL TRP SER ASN
SEQRES 4 A 159 VAL THR PRO LEU LYS PHE SER LYS ILE ASN THR GLY MET
SEQRES 5 A 159 ALA ASP ILE LEU VAL VAL PHE ALA ARG GLY ALA HIS GLY
SEQRES 6 A 159 ASP ASP HIS ALA PHE ASP GLY LYS GLY GLY ILE LEU ALA
SEQRES 7 A 159 HIS ALA PHE GLY PRO GLY SER GLY ILE GLY GLY ASP ALA
SEQRES 8 A 159 HIS PHE ASP GLU ASP GLU PHE TRP THR THR HIS SER GLY
SEQRES 9 A 159 GLY THR ASN LEU PHE LEU THR ALA VAL HIS GLU ILE GLY
SEQRES 10 A 159 HIS SER LEU GLY LEU GLY HIS SER SER ASP PRO LYS ALA
SEQRES 11 A 159 VAL MET PHE PRO THR TYR LYS TYR VAL ASP ILE ASN THR
SEQRES 12 A 159 PHE ARG LEU SER ALA ASP ASP ILE ARG GLY ILE GLN SER
SEQRES 13 A 159 LEU TYR GLY
SEQRES 1 X 3 ILE ALA GLY
HET ZN A 264 1
HET ZN A 265 1
HET CA A 266 1
HET CA A 267 1
HET CA A 268 1
HETNAM ZN ZINC ION
HETNAM CA CALCIUM ION
FORMUL 3 ZN 2(ZN 2+)
FORMUL 5 CA 3(CA 2+)
FORMUL 8 HOH *199(H2 O)
HELIX 1 1 ASN A 126 ASN A 143 1 18
HELIX 2 2 LEU A 212 LEU A 224 1 13
HELIX 3 3 ASP A 244 PHE A 248 5 5
HELIX 4 4 SER A 251 SER A 260 1 10
SHEET 1 A 5 LYS A 148 LYS A 151 0
SHEET 2 A 5 TYR A 113 ILE A 118 1 N ILE A 114 O LYS A 148
SHEET 3 A 5 ILE A 159 ALA A 164 1 O VAL A 161 N ARG A 117
SHEET 4 A 5 ALA A 195 ASP A 198 1 O PHE A 197 N VAL A 162
SHEET 5 A 5 ALA A 182 ALA A 184 -1 N HIS A 183 O HIS A 196
SHEET 1 B 2 TRP A 203 THR A 204 0
SHEET 2 B 2 THR A 210 ASN A 211 1 O THR A 210 N THR A 204
LINK OD1 ASP A 124 CA CA A 267 1555 1555 2.57
LINK OD2 ASP A 124 CA CA A 267 1555 1555 2.39
LINK O ASP A 158 CA CA A 266 1555 1555 2.31
LINK NE2 HIS A 168 ZN ZN A 265 1555 1555 1.99
LINK OD1 ASP A 170 ZN ZN A 265 1555 1555 1.91
LINK OD2 ASP A 175 CA CA A 268 1555 1555 2.38
LINK O GLY A 176 CA CA A 268 1555 1555 2.31
LINK O GLY A 178 CA CA A 268 1555 1555 2.31
LINK O ILE A 180 CA CA A 268 1555 1555 2.32
LINK NE2 HIS A 183 ZN ZN A 265 1555 1555 2.75
LINK O GLY A 190 CA CA A 266 1555 1555 2.34
LINK O GLY A 192 CA CA A 266 1555 1555 2.35
LINK OD2 ASP A 194 CA CA A 266 1555 1555 2.48
LINK ND1 HIS A 196 ZN ZN A 265 1555 1555 2.04
LINK OD1 ASP A 198 CA CA A 268 1555 1555 2.30
LINK O GLU A 199 CA CA A 267 1555 1555 2.35
LINK OE2 GLU A 199 CA CA A 267 1555 1555 2.39
LINK O GLU A 201 CA CA A 267 1555 1555 2.40
LINK OE2 GLU A 201 CA CA A 268 1555 1555 2.27
LINK NE2 HIS A 218 ZN ZN A 264 1555 1555 2.04
LINK NE2 HIS A 222 ZN ZN A 264 1555 1555 2.08
LINK NE2 HIS A 228 ZN ZN A 264 1555 1555 2.04
LINK ZN ZN A 264 O HOH A 314 1555 1555 2.28
LINK CA CA A 266 O HOH A 281 1555 1555 2.48
LINK CA CA A 266 O HOH A 321 1555 1555 2.29
LINK CA CA A 267 O HOH A 277 1555 1555 2.39
LINK CA CA A 267 O HOH A 278 1555 1555 2.43
SITE 1 AC1 4 HIS A 218 HIS A 222 HIS A 228 HOH A 314
SITE 1 AC2 4 HIS A 168 ASP A 170 HIS A 183 HIS A 196
SITE 1 AC3 6 ASP A 158 GLY A 190 GLY A 192 ASP A 194
SITE 2 AC3 6 HOH A 281 HOH A 321
SITE 1 AC4 5 ASP A 124 GLU A 199 GLU A 201 HOH A 277
SITE 2 AC4 5 HOH A 278
SITE 1 AC5 6 ASP A 175 GLY A 176 GLY A 178 ILE A 180
SITE 2 AC5 6 ASP A 198 GLU A 201
CRYST1 51.888 60.358 54.521 90.00 115.73 90.00 C 1 2 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.019272 0.000000 0.009288 0.00000
SCALE2 0.000000 0.016568 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020360 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
