HEADER HYDROLASE 13-JUL-10 3NX7
TITLE CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN MMP12 COMPLEXED
TITLE 2 WITH THE INHIBITOR N-HYDROXY-2-(N-(2-HYDROXYETHYL)4-
TITLE 3 METHOXYPHENYLSULFONAMIDO)ACETAMIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MACROPHAGE METALLOELASTASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN (UNP RESIDUES 106 TO 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: HME, MMP12;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET21
KEYWDS MATRIX METALLOPROTEINASE, MMP12, ELASTASE, COMPLEX (ELASTASE-
KEYWDS 2 INHIBITOR), HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR I.BERTINI,V.CALDERONE,M.FRAGAI,A.GIACHETTI,M.LOCONTE,C.LUCHINAT,
AUTHOR 2 M.MALETTA,C.NATIVI,K.J.YEO
REVDAT 3 06-SEP-23 3NX7 1 REMARK SEQADV LINK
REVDAT 2 08-NOV-17 3NX7 1 REMARK
REVDAT 1 28-JUL-10 3NX7 0
JRNL AUTH I.BERTINI,V.CALDERONE,M.FRAGAI,A.GIACHETTI,M.LOCONTE,
JRNL AUTH 2 C.LUCHINAT,M.MALETTA,C.NATIVI,K.J.YEO
JRNL TITL EXPLORING THE SUBTLETIES OF DRUG-RECEPTOR INTERACTIONS: THE
JRNL TITL 2 CASE OF MATRIX METALLOPROTEINASES
JRNL REF J.AM.CHEM.SOC. V. 129 2466 2007
JRNL REFN ISSN 0002-7863
JRNL PMID 17269766
JRNL DOI 10.1021/JA065156Z
REMARK 2
REMARK 2 RESOLUTION. 1.80 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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.21
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 11991
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) : 0.166
REMARK 3 R VALUE (WORKING SET) : 0.162
REMARK 3 FREE R VALUE : 0.200
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1180
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) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.85
REMARK 3 REFLECTION IN BIN (WORKING SET) : 520
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.1850
REMARK 3 BIN FREE R VALUE SET COUNT : 55
REMARK 3 BIN FREE R VALUE : 0.2840
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1238
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 25
REMARK 3 SOLVENT ATOMS : 142
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 10.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 11.04
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.08000
REMARK 3 B22 (A**2) : 0.23000
REMARK 3 B33 (A**2) : -0.65000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.41000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.127
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.075
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.329
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.948
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.925
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1295 ; 0.012 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1757 ; 1.305 ; 1.931
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 157 ; 5.893 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 63 ;32.764 ;23.175
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 188 ;11.297 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 7 ;14.747 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 179 ; 0.090 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1025 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 620 ; 0.193 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 906 ; 0.307 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 92 ; 0.128 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 12 ; 0.089 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 48 ; 0.220 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 16 ; 0.251 ; 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): 793 ; 0.833 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1242 ; 1.343 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 576 ; 2.090 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 515 ; 2.991 ; 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): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
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 3NX7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-JUL-10.
REMARK 100 THE DEPOSITION ID IS D_1000060391.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-MAY-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : SEALED TUBE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : OXFORD DIFFRACTION ENHANCE ULTRA
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54056
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : OXFORD ONYX CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13172
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 30.210
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.0
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : 0.04300
REMARK 200 R SYM (I) : 0.04300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.3000
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 (%) : 68.4
REMARK 200 DATA REDUNDANCY IN SHELL : 1.90
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 7.800
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 (%): 43.22
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS, 30% PEG 6000, PH 8.0, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293K
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 25.65800
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.20000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 25.65800
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 30.20000
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 20 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 77 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 87 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 97 LIES ON A SPECIAL POSITION.
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 25.45 -143.42
REMARK 500 HIS A 206 -156.19 -130.40
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 ZN A 264 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 NHK A 0 O1
REMARK 620 2 NHK A 0 O2 78.1
REMARK 620 3 HIS A 218 NE2 107.8 108.4
REMARK 620 4 HIS A 222 NE2 155.1 92.1 97.0
REMARK 620 5 HIS A 228 NE2 82.3 146.2 103.7 94.3
REMARK 620 N 1 2 3 4
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 11 O
REMARK 620 2 ASP A 158 O 78.8
REMARK 620 3 GLY A 190 O 81.3 160.0
REMARK 620 4 GLY A 192 O 77.4 80.6 96.5
REMARK 620 5 ASP A 194 OD2 164.5 89.7 110.2 90.6
REMARK 620 N 1 2 3 4
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 16 O
REMARK 620 2 HOH A 72 O 77.3
REMARK 620 3 ASP A 124 OD2 98.6 136.1
REMARK 620 4 ASP A 124 OD1 85.6 83.7 52.4
REMARK 620 5 GLU A 199 O 101.8 83.8 138.7 163.6
REMARK 620 6 GLU A 199 OE2 161.1 85.2 89.1 85.5 83.0
REMARK 620 7 GLU A 201 O 77.8 141.9 76.1 122.4 73.7 121.0
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 OD1 107.8
REMARK 620 3 HIS A 183 NE2 115.4 115.6
REMARK 620 4 HIS A 196 ND1 110.6 94.8 110.9
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 88.7
REMARK 620 3 GLY A 178 O 84.5 86.2
REMARK 620 4 ILE A 180 O 90.2 177.3 96.1
REMARK 620 5 ASP A 198 OD1 94.9 88.5 174.7 89.2
REMARK 620 6 GLU A 201 OE2 173.8 93.2 89.7 88.2 91.1
REMARK 620 N 1 2 3 4 5
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 NHK A 0
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3F15 RELATED DB: PDB
REMARK 900 RELATED ID: 3F16 RELATED DB: PDB
REMARK 900 RELATED ID: 3F17 RELATED DB: PDB
REMARK 900 RELATED ID: 3F19 RELATED DB: PDB
REMARK 900 RELATED ID: 3F1A RELATED DB: PDB
DBREF 3NX7 A 106 263 UNP P39900 MMP12_HUMAN 106 263
SEQADV 3NX7 ASP A 171 UNP P39900 PHE 171 ENGINEERED MUTATION
SEQRES 1 A 158 GLY PRO VAL TRP ARG LYS HIS TYR ILE THR TYR ARG ILE
SEQRES 2 A 158 ASN ASN TYR THR PRO ASP MET ASN ARG GLU ASP VAL ASP
SEQRES 3 A 158 TYR ALA ILE ARG LYS ALA PHE GLN VAL TRP SER ASN VAL
SEQRES 4 A 158 THR PRO LEU LYS PHE SER LYS ILE ASN THR GLY MET ALA
SEQRES 5 A 158 ASP ILE LEU VAL VAL PHE ALA ARG GLY ALA HIS GLY ASP
SEQRES 6 A 158 ASP HIS ALA PHE ASP GLY LYS GLY GLY ILE LEU ALA HIS
SEQRES 7 A 158 ALA PHE GLY PRO GLY SER GLY ILE GLY GLY ASP ALA HIS
SEQRES 8 A 158 PHE ASP GLU ASP GLU PHE TRP THR THR HIS SER GLY GLY
SEQRES 9 A 158 THR ASN LEU PHE LEU THR ALA VAL HIS GLU ILE GLY HIS
SEQRES 10 A 158 SER LEU GLY LEU GLY HIS SER SER ASP PRO LYS ALA VAL
SEQRES 11 A 158 MET PHE PRO THR TYR LYS TYR VAL ASP ILE ASN THR PHE
SEQRES 12 A 158 ARG LEU SER ALA ASP ASP ILE ARG GLY ILE GLN SER LEU
SEQRES 13 A 158 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 NHK A 0 20
HETNAM ZN ZINC ION
HETNAM CA CALCIUM ION
HETNAM NHK N-HYDROXY-N~2~-(2-HYDROXYETHYL)-N~2~-[(4-
HETNAM 2 NHK METHOXYPHENYL)SULFONYL]GLYCINAMIDE
FORMUL 2 ZN 2(ZN 2+)
FORMUL 4 CA 3(CA 2+)
FORMUL 7 NHK C11 H16 N2 O6 S
FORMUL 8 HOH *142(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 O1 NHK A 0 ZN ZN A 264 1555 1555 2.12
LINK O2 NHK A 0 ZN ZN A 264 1555 1555 2.18
LINK O HOH A 11 CA CA A 266 1555 1555 2.55
LINK O HOH A 16 CA CA A 267 1555 1555 2.47
LINK O HOH A 72 CA CA A 267 1555 1555 2.46
LINK OD2 ASP A 124 CA CA A 267 1555 1555 2.37
LINK OD1 ASP A 124 CA CA A 267 1555 1555 2.56
LINK O ASP A 158 CA CA A 266 1555 1555 2.51
LINK NE2 HIS A 168 ZN ZN A 265 1555 1555 2.06
LINK OD1 ASP A 170 ZN ZN A 265 1555 1555 1.96
LINK OD2 ASP A 175 CA CA A 268 1555 1555 2.34
LINK O GLY A 176 CA CA A 268 1555 1555 2.26
LINK O GLY A 178 CA CA A 268 1555 1555 2.38
LINK O ILE A 180 CA CA A 268 1555 1555 2.31
LINK NE2 HIS A 183 ZN ZN A 265 1555 1555 2.04
LINK O GLY A 190 CA CA A 266 1555 1555 2.45
LINK O GLY A 192 CA CA A 266 1555 1555 2.38
LINK OD2 ASP A 194 CA CA A 266 1555 1555 2.59
LINK ND1 HIS A 196 ZN ZN A 265 1555 1555 2.11
LINK OD1 ASP A 198 CA CA A 268 1555 1555 2.35
LINK O GLU A 199 CA CA A 267 1555 1555 2.35
LINK OE2 GLU A 199 CA CA A 267 1555 1555 2.43
LINK O GLU A 201 CA CA A 267 1555 1555 2.46
LINK OE2 GLU A 201 CA CA A 268 1555 1555 2.25
LINK NE2 HIS A 218 ZN ZN A 264 1555 1555 2.06
LINK NE2 HIS A 222 ZN ZN A 264 1555 1555 2.14
LINK NE2 HIS A 228 ZN ZN A 264 1555 1555 2.11
SITE 1 AC1 4 NHK A 0 HIS A 218 HIS A 222 HIS A 228
SITE 1 AC2 4 HIS A 168 ASP A 170 HIS A 183 HIS A 196
SITE 1 AC3 5 HOH A 11 ASP A 158 GLY A 190 GLY A 192
SITE 2 AC3 5 ASP A 194
SITE 1 AC4 5 HOH A 16 HOH A 72 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 13 HOH A 4 GLY A 179 ILE A 180 LEU A 181
SITE 2 AC6 13 ALA A 182 THR A 215 HIS A 218 GLU A 219
SITE 3 AC6 13 HIS A 222 HIS A 228 PRO A 238 TYR A 240
SITE 4 AC6 13 ZN A 264
CRYST1 51.316 60.400 53.719 90.00 114.50 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 0.019487 0.000000 0.008881 0.00000
SCALE2 0.000000 0.016556 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020457 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
