HEADER HYDROLASE/HYDROLASE INHIBITOR 25-JAN-10 3LIK
TITLE HUMAN MMP12 IN COMPLEX WITH NON-ZINC CHELATING INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MACROPHAGE METALLOELASTASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: MMP-12 CATALITIC SUBUNIT (RESIDUES 106-263);
COMPND 5 SYNONYM: MME, MATRIX METALLOPROTEINASE-12, MMP-12, MACROPHAGE
COMPND 6 ELASTASE, ME, HME;
COMPND 7 EC: 3.4.24.65;
COMPND 8 ENGINEERED: YES;
COMPND 9 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: MMP12, HME;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PET24A
KEYWDS MMP12 ELASTASE NON-CHELATING INHIBITOR, HYDROLASE, HYDROLASE-
KEYWDS 2 HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR E.A.STURA,V.DIVE,L.DEVEL,B.CZARNY,L.VERA,F.BEAU
REVDAT 3 06-SEP-23 3LIK 1 REMARK SEQADV LINK
REVDAT 2 08-DEC-10 3LIK 1 JRNL
REVDAT 1 01-SEP-10 3LIK 0
JRNL AUTH L.DEVEL,S.GARCIA,B.CZARNY,F.BEAU,E.LAJEUNESSE,L.VERA,
JRNL AUTH 2 D.GEORGIADIS,E.STURA,V.DIVE
JRNL TITL INSIGHTS FROM SELECTIVE NON-PHOSPHINIC INHIBITORS OF MMP-12
JRNL TITL 2 TAILORED TO FIT WITH AN S1' LOOP CANONICAL CONFORMATION.
JRNL REF J.BIOL.CHEM. V. 285 35900 2010
JRNL REFN ISSN 0021-9258
JRNL PMID 20817735
JRNL DOI 10.1074/JBC.M110.139634
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.30
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 88.2
REMARK 3 NUMBER OF REFLECTIONS : 13436
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.160
REMARK 3 R VALUE (WORKING SET) : 0.157
REMARK 3 FREE R VALUE : 0.209
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 676
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 46.3105 - 3.0777 0.95 2910 136 0.1553 0.1874
REMARK 3 2 3.0777 - 2.4429 0.95 2739 149 0.1483 0.1999
REMARK 3 3 2.4429 - 2.1341 0.91 2619 148 0.1540 0.2340
REMARK 3 4 2.1341 - 1.9390 0.80 2276 127 0.1578 0.2237
REMARK 3 5 1.9390 - 1.8000 0.78 2216 116 0.1848 0.2580
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.37
REMARK 3 B_SOL : 47.35
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.160
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 12.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.75
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 1393
REMARK 3 ANGLE : 1.044 1887
REMARK 3 CHIRALITY : 0.070 187
REMARK 3 PLANARITY : 0.015 246
REMARK 3 DIHEDRAL : 19.599 507
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3LIK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-AUG-10.
REMARK 100 THE DEPOSITION ID IS D_1000057321.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-APR-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9334
REMARK 200 MONOCHROMATOR : DIAMOND (111), GE(220)
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13458
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 46.270
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 89.1
REMARK 200 DATA REDUNDANCY : 6.080
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : 0.08000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.2300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 79.7
REMARK 200 DATA REDUNDANCY IN SHELL : 6.30
REMARK 200 R MERGE FOR SHELL (I) : 0.23500
REMARK 200 R SYM FOR SHELL (I) : 0.30900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: RIGID BODY
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1RMZ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MMP12 AT 4MG/ML CO-CRYSTALLIZATION
REMARK 280 WITH AHA AND NON-CHELATING INHIBITOR WITH PRECIPITANT: 25% PEG
REMARK 280 10K, 100MM NACL,0.2M IMIDAZOLE MALATE, PH 8.5, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
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 34.22350
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 31.42650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 34.22350
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 31.42650
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 269 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 328 LIES ON A SPECIAL POSITION.
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 48 O HOH A 48 2555 2.04
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 110 34.45 -96.96
REMARK 500 ARG A 110 37.39 -99.02
REMARK 500 HIS A 206 -157.54 -135.90
REMARK 500 ASP A 244 112.02 -38.99
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 P6G A 303
REMARK 610 P6G A 304
REMARK 610 P6G A 305
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 266 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 17 O
REMARK 620 2 HOH A 24 O 96.1
REMARK 620 3 ASP A 158 O 86.0 84.1
REMARK 620 4 GLY A 190 O 83.0 92.3 168.1
REMARK 620 5 GLY A 192 O 176.0 80.7 95.9 94.8
REMARK 620 6 ASP A 194 OD2 93.0 167.9 88.6 96.7 90.5
REMARK 620 N 1 2 3 4 5
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 HOH A 25 O
REMARK 620 2 HOH A 36 O 80.9
REMARK 620 3 ASP A 124 OD2 92.7 135.6
REMARK 620 4 ASP A 124 OD1 82.5 85.2 50.4
REMARK 620 5 GLU A 199 O 107.9 83.1 139.4 162.8
REMARK 620 6 GLU A 199 OE2 165.9 88.6 88.2 87.3 79.9
REMARK 620 7 GLU A 201 O 77.3 143.8 74.4 119.7 76.6 116.3
REMARK 620 N 1 2 3 4 5 6
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 OD2 114.1
REMARK 620 3 HIS A 183 NE2 113.8 113.2
REMARK 620 4 HIS A 183 NE2 106.7 121.1 8.2
REMARK 620 5 HIS A 196 ND1 109.4 92.5 111.8 112.0
REMARK 620 N 1 2 3 4
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 90.8
REMARK 620 3 GLY A 178 O 88.1 90.7
REMARK 620 4 ILE A 180 O 89.7 176.8 92.4
REMARK 620 5 ASP A 198 OD1 92.3 86.7 177.4 90.2
REMARK 620 6 GLU A 201 OE2 173.3 91.8 85.8 88.0 94.0
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 102.0
REMARK 620 3 HIS A 228 NE2 102.3 95.9
REMARK 620 4 HAE A 302 O 102.6 94.6 150.2
REMARK 620 5 HAE A 302 O2 125.6 132.0 81.6 70.7
REMARK 620 N 1 2 3 4
REMARK 630
REMARK 630 MOLECULE TYPE: PEPTIDE-LIKE INHIBITOR
REMARK 630 MOLECULE NAME: N-{3-[4-(4-PHENYLTHIOPHEN-2-YL)PHENYL]PROPANOYL}-L-
REMARK 630 ALPHA-GLUTAMYL-L-ALPHA-GLUTAMYL-AMIDE
REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 630 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 630
REMARK 630 M RES C SSSEQI
REMARK 630 EEG A 301
REMARK 630 SOURCE: NULL
REMARK 630 TAXONOMY: NULL
REMARK 630 SUBCOMP: 03J GLU GLU NH2
REMARK 630 DETAILS: NULL
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 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EEG A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HAE A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P6G A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P6G A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P6G A 305
REMARK 900
REMARK 900 RELATED ENTRIES
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: 3LIL RELATED DB: PDB
REMARK 900 HUMAN MMP12 IN COMPLEX WITH NON-ZINC CHELATING INHIBITOR
REMARK 900 RELATED ID: 3LIR RELATED DB: PDB
REMARK 900 HUMAN MMP12 IN COMPLEX WITH NON-ZINC CHELATING INHIBITOR
REMARK 900 RELATED ID: 3LJG RELATED DB: PDB
REMARK 900 HUMAN MMP12 IN COMPLEX WITH NON-ZINC CHELATING INHIBITOR
DBREF 3LIK A 106 263 UNP P39900 MMP12_HUMAN 106 263
SEQADV 3LIK MET A 105 UNP P39900 EXPRESSION TAG
SEQADV 3LIK 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
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
HET EEG A 301 40
HET HAE A 302 5
HET P6G A 303 7
HET P6G A 304 7
HET P6G A 305 7
HETNAM ZN ZINC ION
HETNAM CA CALCIUM ION
HETNAM EEG N-{3-[4-(4-PHENYLTHIOPHEN-2-YL)PHENYL]PROPANOYL}-L-
HETNAM 2 EEG ALPHA-GLUTAMYL-L-ALPHA-GLUTAMYL-AMIDE
HETNAM HAE ACETOHYDROXAMIC ACID
HETNAM P6G HEXAETHYLENE GLYCOL
HETSYN P6G POLYETHYLENE GLYCOL PEG400
FORMUL 2 ZN 2(ZN 2+)
FORMUL 4 CA 3(CA 2+)
FORMUL 7 EEG C29 H31 N3 O7 S
FORMUL 8 HAE C2 H5 N O2
FORMUL 9 P6G 3(C12 H26 O7)
FORMUL 12 HOH *179(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 TYR A 262 1 12
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 O HOH A 17 CA CA A 266 1555 1555 2.45
LINK O HOH A 24 CA CA A 266 1555 1555 2.53
LINK O HOH A 25 CA CA A 267 1555 1555 2.55
LINK O HOH A 36 CA CA A 267 1555 1555 2.53
LINK OD2 ASP A 124 CA CA A 267 1555 1555 2.48
LINK OD1 ASP A 124 CA CA A 267 1555 1555 2.68
LINK O ASP A 158 CA CA A 266 1555 1555 2.40
LINK NE2 HIS A 168 ZN ZN A 265 1555 1555 2.11
LINK OD2 ASP A 170 ZN ZN A 265 1555 1555 2.02
LINK OD2 ASP A 175 CA CA A 268 1555 1555 2.39
LINK O GLY A 176 CA CA A 268 1555 1555 2.35
LINK O GLY A 178 CA CA A 268 1555 1555 2.39
LINK O ILE A 180 CA CA A 268 1555 1555 2.41
LINK NE2AHIS A 183 ZN ZN A 265 1555 1555 2.06
LINK NE2BHIS A 183 ZN ZN A 265 1555 1555 2.13
LINK O GLY A 190 CA CA A 266 1555 1555 2.37
LINK O GLY A 192 CA CA A 266 1555 1555 2.30
LINK OD2 ASP A 194 CA CA A 266 1555 1555 2.48
LINK ND1 HIS A 196 ZN ZN A 265 1555 1555 2.16
LINK OD1 ASP A 198 CA CA A 268 1555 1555 2.35
LINK O GLU A 199 CA CA A 267 1555 1555 2.40
LINK OE2 GLU A 199 CA CA A 267 1555 1555 2.52
LINK O GLU A 201 CA CA A 267 1555 1555 2.51
LINK OE2 GLU A 201 CA CA A 268 1555 1555 2.33
LINK NE2 HIS A 218 ZN ZN A 264 1555 1555 2.10
LINK NE2 HIS A 222 ZN ZN A 264 1555 1555 2.11
LINK NE2 HIS A 228 ZN ZN A 264 1555 1555 2.12
LINK ZN ZN A 264 O HAE A 302 1555 1555 2.23
LINK ZN ZN A 264 O2 HAE A 302 1555 1555 2.37
SITE 1 AC1 4 HIS A 218 HIS A 222 HIS A 228 HAE A 302
SITE 1 AC2 4 HIS A 168 ASP A 170 HIS A 183 HIS A 196
SITE 1 AC3 6 HOH A 17 HOH A 24 ASP A 158 GLY A 190
SITE 2 AC3 6 GLY A 192 ASP A 194
SITE 1 AC4 5 HOH A 25 HOH A 36 ASP A 124 GLU A 199
SITE 2 AC4 5 GLU A 201
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
SITE 1 AC6 24 HOH A 91 HOH A 102 THR A 154 GLY A 155
SITE 2 AC6 24 MET A 156 GLY A 178 GLY A 179 ILE A 180
SITE 3 AC6 24 LEU A 181 ALA A 182 HIS A 218 GLU A 219
SITE 4 AC6 24 PRO A 232 LYS A 233 ALA A 234 PHE A 237
SITE 5 AC6 24 PRO A 238 THR A 239 TYR A 240 LYS A 241
SITE 6 AC6 24 HOH A 282 HOH A 284 HOH A 292 HAE A 302
SITE 1 AC7 10 HOH A 1 HOH A 82 ALA A 182 HIS A 183
SITE 2 AC7 10 HIS A 218 GLU A 219 HIS A 222 HIS A 228
SITE 3 AC7 10 ZN A 264 EEG A 301
SITE 1 AC8 10 HOH A 11 HOH A 44 HOH A 100 SER A 150
SITE 2 AC8 10 LYS A 151 ILE A 152 ASP A 171 HIS A 172
SITE 3 AC8 10 ALA A 173 HOH A 270
SITE 1 AC9 3 HIS A 228 SER A 229 SER A 230
SITE 1 BC1 10 HOH A 83 HOH A 87 PRO A 107 VAL A 108
SITE 2 BC1 10 ASN A 126 ASP A 129 PRO A 187 THR A 205
SITE 3 BC1 10 HOH A 325 HOH A 329
CRYST1 68.447 62.853 36.629 90.00 90.00 90.00 P 21 21 2 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 0.014610 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015910 0.000000 0.00000
SCALE3 0.000000 0.000000 0.027301 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
