HEADER HYDROLASE 18-DEC-14 4XCT
TITLE CRYSTAL STRUCTURE OF A HYDROXAMATE BASED INHIBITOR ARP101 (EN73) IN
TITLE 2 COMPLEX WITH THE MMP-9 CATALYTIC DOMAIN.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MATRIX METALLOPROTEINASE-9,MATRIX METALLOPROTEINASE-9;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 113-216,UNP RESIDUES 392-444;
COMPND 5 SYNONYM: MMP-9,92 KDA GELATINASE,92 KDA TYPE IV COLLAGENASE,
COMPND 6 GELATINASE B,GELB;
COMPND 7 EC: 3.4.24.35;
COMPND 8 ENGINEERED: YES;
COMPND 9 OTHER_DETAILS: N73 ZINC CHELATING INHIBITOR - HUMAN WILD-TYPE MMP-9
COMPND 10 CATALYTIC DOMAIN UNP RESIDUES 107-215/391-443
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 BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: STAR;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-14B
KEYWDS INHIBITOR-COMPLEX, METALLOPROTEASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.A.STURA,L.TEPSHI,E.NUTI,V.DIVE,E.CASSAR-LAJEUNESSE,L.VERA,
AUTHOR 2 A.ROSSELLO
REVDAT 5 10-JAN-24 4XCT 1 LINK
REVDAT 4 29-MAY-19 4XCT 1 COMPND REMARK HETNAM FORMUL
REVDAT 4 2 1 LINK SITE ATOM
REVDAT 3 07-OCT-15 4XCT 1 JRNL
REVDAT 2 26-AUG-15 4XCT 1 JRNL
REVDAT 1 22-APR-15 4XCT 0
JRNL AUTH E.NUTI,A.R.CANTELMO,C.GALLO,A.BRUNO,B.BASSANI,C.CAMODECA,
JRNL AUTH 2 T.TUCCINARDI,L.VERA,E.ORLANDINI,S.NENCETTI,E.A.STURA,
JRNL AUTH 3 A.MARTINELLI,V.DIVE,A.ALBINI,A.ROSSELLO
JRNL TITL N-O-ISOPROPYL SULFONAMIDO-BASED HYDROXAMATES AS MATRIX
JRNL TITL 2 METALLOPROTEINASE INHIBITORS: HIT SELECTION AND IN VIVO
JRNL TITL 3 ANTIANGIOGENIC ACTIVITY.
JRNL REF J.MED.CHEM. V. 58 7224 2015
JRNL REFN ISSN 0022-2623
JRNL PMID 26263024
JRNL DOI 10.1021/ACS.JMEDCHEM.5B00367
REMARK 2
REMARK 2 RESOLUTION. 1.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.9_1692)
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) : 1.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.30
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 37897
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.170
REMARK 3 R VALUE (WORKING SET) : 0.167
REMARK 3 FREE R VALUE : 0.231
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 1892
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 34.3065 - 3.1315 1.00 2803 148 0.1443 0.2063
REMARK 3 2 3.1315 - 2.4858 1.00 2645 138 0.1680 0.2244
REMARK 3 3 2.4858 - 2.1716 1.00 2627 138 0.1575 0.2219
REMARK 3 4 2.1716 - 1.9731 1.00 2564 135 0.1529 0.2057
REMARK 3 5 1.9731 - 1.8317 1.00 2589 137 0.1583 0.2284
REMARK 3 6 1.8317 - 1.7237 1.00 2523 133 0.1653 0.2518
REMARK 3 7 1.7237 - 1.6374 1.00 2574 135 0.1746 0.2284
REMARK 3 8 1.6374 - 1.5661 1.00 2536 134 0.1856 0.2768
REMARK 3 9 1.5661 - 1.5058 1.00 2572 135 0.2085 0.2735
REMARK 3 10 1.5058 - 1.4539 1.00 2506 130 0.2258 0.3337
REMARK 3 11 1.4539 - 1.4084 1.00 2525 133 0.2502 0.3349
REMARK 3 12 1.4084 - 1.3681 1.00 2504 131 0.2631 0.3288
REMARK 3 13 1.3681 - 1.3321 1.00 2564 134 0.2723 0.3198
REMARK 3 14 1.3321 - 1.2996 0.98 2473 131 0.2760 0.3203
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 : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.150
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.170
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
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 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 : 0.006 1497
REMARK 3 ANGLE : 1.049 2047
REMARK 3 CHIRALITY : 0.053 198
REMARK 3 PLANARITY : 0.005 273
REMARK 3 DIHEDRAL : 14.462 548
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 4XCT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-DEC-14.
REMARK 100 THE DEPOSITION ID IS D_1000205450.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-DEC-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0-8.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SOLEIL
REMARK 200 BEAMLINE : PROXIMA 1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97857
REMARK 200 MONOCHROMATOR : CHANNEL CUT SI(111)
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38007
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.300
REMARK 200 RESOLUTION RANGE LOW (A) : 52.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 6.200
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : 0.05500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.6200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.1
REMARK 200 DATA REDUNDANCY IN SHELL : 6.16
REMARK 200 R MERGE FOR SHELL (I) : 1.39200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.120
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: 4H3X
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.47
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN: HMMP-9-WT AT 337 MICRO-M WITH
REMARK 280 120 MILLI-M ACETOHYDROXAMIC ACID. PRECIPITANT: 40.5% MPEG 5,000,
REMARK 280 180 MM IMIDAZOLE PIPERIDINE, PH 8.5. CRYOPROTECTANT: 40%
REMARK 280 CRYOPROTX-C1, 10% PEG 10K, 10% PCTP 50/50, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 293.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 109.30667
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 54.65333
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 54.65333
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 109.30667
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 TOTAL BURIED SURFACE AREA: 1750 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 8150 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL
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 494 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 611 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 627 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 TYR A 160 66.28 -114.98
REMARK 500 ALA A 173 -136.70 49.34
REMARK 500 ASP A 185 -161.01 57.35
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 630 DISTANCE = 6.22 ANGSTROMS
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 306 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 131 OD1
REMARK 620 2 ASP A 131 OD2 52.2
REMARK 620 3 ASP A 206 O 151.5 149.3
REMARK 620 4 ASP A 206 OD1 92.3 91.3 73.5
REMARK 620 5 GLU A 208 O 126.3 77.4 82.0 107.6
REMARK 620 6 HOH A 512 O 87.1 93.3 104.3 173.7 77.7
REMARK 620 7 HOH A 515 O 78.6 130.6 75.9 86.1 149.6 87.7
REMARK 620 N 1 2 3 4 5 6
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 ASP A 165 O
REMARK 620 2 GLY A 197 O 172.8
REMARK 620 3 GLN A 199 O 102.8 83.8
REMARK 620 4 ASP A 201 OD1 86.2 96.2 96.0
REMARK 620 5 HOH A 415 O 88.3 84.7 164.2 95.9
REMARK 620 6 HOH A 452 O 86.5 91.1 84.4 172.6 85.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 303 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 175 NE2
REMARK 620 2 ASP A 177 OD2 109.7
REMARK 620 3 HIS A 190 NE2 114.0 114.0
REMARK 620 4 HIS A 203 ND1 108.8 92.2 116.1
REMARK 620 N 1 2 3
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 ASP A 182 OD1
REMARK 620 2 GLY A 183 O 88.6
REMARK 620 3 ASP A 185 O 84.0 85.1
REMARK 620 4 LEU A 187 O 92.4 177.6 92.9
REMARK 620 5 ASP A 205 OD2 91.6 88.1 171.9 94.1
REMARK 620 6 GLU A 208 OE2 170.1 94.3 86.8 84.4 97.9
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 226 NE2
REMARK 620 2 HIS A 230 NE2 93.6
REMARK 620 3 HIS A 236 NE2 108.6 94.3
REMARK 620 4 N73 A 301 O8 136.4 126.9 85.9
REMARK 620 5 N73 A 301 OA8 98.2 88.6 152.7 70.9
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 N73 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 ZN 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 CA A 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 308
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 309
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 310
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 311
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 312
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 313
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGO A 314
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGO A 315
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BUD A 316
DBREF 4XCT A 113 216 UNP P14780 MMP9_HUMAN 113 216
DBREF 4XCT A 217 269 UNP P14780 MMP9_HUMAN 392 444
SEQRES 1 A 157 ASP LEU LYS TRP HIS HIS HIS ASN ILE THR TYR TRP ILE
SEQRES 2 A 157 GLN ASN TYR SER GLU ASP LEU PRO ARG ALA VAL ILE ASP
SEQRES 3 A 157 ASP ALA PHE ALA ARG ALA PHE ALA LEU TRP SER ALA VAL
SEQRES 4 A 157 THR PRO LEU THR PHE THR ARG VAL TYR SER ARG ASP ALA
SEQRES 5 A 157 ASP ILE VAL ILE GLN PHE GLY VAL ALA GLU HIS GLY ASP
SEQRES 6 A 157 GLY TYR PRO PHE ASP GLY LYS ASP GLY LEU LEU ALA HIS
SEQRES 7 A 157 ALA PHE PRO PRO GLY PRO GLY ILE GLN GLY ASP ALA HIS
SEQRES 8 A 157 PHE ASP ASP ASP GLU LEU TRP SER LEU GLY LYS GLY VAL
SEQRES 9 A 157 GLY TYR SER LEU PHE LEU VAL ALA ALA HIS GLU PHE GLY
SEQRES 10 A 157 HIS ALA LEU GLY LEU ASP HIS SER SER VAL PRO GLU ALA
SEQRES 11 A 157 LEU MET TYR PRO MET TYR ARG PHE THR GLU GLY PRO PRO
SEQRES 12 A 157 LEU HIS LYS ASP ASP VAL ASN GLY ILE ARG HIS LEU TYR
SEQRES 13 A 157 GLY
HET N73 A 301 28
HET ZN A 302 1
HET ZN A 303 1
HET CA A 304 1
HET CA A 305 1
HET CA A 306 1
HET DMS A 307 4
HET DMS A 308 4
HET EDO A 309 4
HET EDO A 310 4
HET EDO A 311 4
HET EDO A 312 4
HET GOL A 313 6
HET PGO A 314 5
HET PGO A 315 5
HET BUD A 316 6
HETNAM N73 (2~{R})-3-METHYL-~{N}-OXIDANYLIDENE-2-[(4-
HETNAM 2 N73 PHENYLPHENYL)SULFONYL-PROPAN-2-YLOXY-AMINO]BUTANAMIDE
HETNAM ZN ZINC ION
HETNAM CA CALCIUM ION
HETNAM DMS DIMETHYL SULFOXIDE
HETNAM EDO 1,2-ETHANEDIOL
HETNAM GOL GLYCEROL
HETNAM PGO S-1,2-PROPANEDIOL
HETNAM BUD (2S,3S)-BUTANE-2,3-DIOL
HETSYN EDO ETHYLENE GLYCOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 N73 C20 H24 N2 O5 S
FORMUL 3 ZN 2(ZN 2+)
FORMUL 5 CA 3(CA 2+)
FORMUL 8 DMS 2(C2 H6 O S)
FORMUL 10 EDO 4(C2 H6 O2)
FORMUL 14 GOL C3 H8 O3
FORMUL 15 PGO 2(C3 H8 O2)
FORMUL 17 BUD C4 H10 O2
FORMUL 18 HOH *230(H2 O)
HELIX 1 AA1 PRO A 133 ALA A 150 1 18
HELIX 2 AA2 LEU A 220 LEU A 232 1 13
HELIX 3 AA3 HIS A 257 GLY A 269 1 13
SHEET 1 AA1 5 THR A 155 ARG A 158 0
SHEET 2 AA1 5 ASN A 120 ILE A 125 1 N ILE A 121 O THR A 157
SHEET 3 AA1 5 ILE A 166 GLY A 171 1 O ILE A 168 N TRP A 124
SHEET 4 AA1 5 ALA A 202 ASP A 205 1 O PHE A 204 N GLN A 169
SHEET 5 AA1 5 ALA A 189 ALA A 191 -1 N HIS A 190 O HIS A 203
SHEET 1 AA2 2 TRP A 210 SER A 211 0
SHEET 2 AA2 2 TYR A 218 SER A 219 1 O TYR A 218 N SER A 211
LINK OD1 ASP A 131 CA CA A 306 1555 1555 2.62
LINK OD2 ASP A 131 CA CA A 306 1555 1555 2.37
LINK O ASP A 165 CA CA A 305 1555 1555 2.34
LINK NE2 HIS A 175 ZN ZN A 303 1555 1555 1.97
LINK OD2 ASP A 177 ZN ZN A 303 1555 1555 1.99
LINK OD1 ASP A 182 CA CA A 304 1555 1555 2.43
LINK O GLY A 183 CA CA A 304 1555 1555 2.28
LINK O ASP A 185 CA CA A 304 1555 1555 2.33
LINK O LEU A 187 CA CA A 304 1555 1555 2.27
LINK NE2 HIS A 190 ZN ZN A 303 1555 1555 2.06
LINK O GLY A 197 CA CA A 305 1555 1555 2.31
LINK O GLN A 199 CA CA A 305 1555 1555 2.26
LINK OD1 ASP A 201 CA CA A 305 1555 1555 2.34
LINK ND1 HIS A 203 ZN ZN A 303 1555 1555 2.06
LINK OD2 ASP A 205 CA CA A 304 1555 1555 2.31
LINK O ASP A 206 CA CA A 306 1555 1555 2.41
LINK OD1 ASP A 206 CA CA A 306 1555 1555 2.42
LINK OE2 GLU A 208 CA CA A 304 1555 1555 2.34
LINK O GLU A 208 CA CA A 306 1555 1555 2.38
LINK NE2 HIS A 226 ZN ZN A 302 1555 1555 2.06
LINK NE2 HIS A 230 ZN ZN A 302 1555 1555 2.11
LINK NE2 HIS A 236 ZN ZN A 302 1555 1555 2.08
LINK O8 N73 A 301 ZN ZN A 302 1555 1555 2.16
LINK OA8 N73 A 301 ZN ZN A 302 1555 1555 2.31
LINK CA CA A 305 O HOH A 415 1555 1555 2.29
LINK CA CA A 305 O HOH A 452 1555 1555 2.31
LINK CA CA A 306 O HOH A 512 1555 1555 2.35
LINK CA CA A 306 O HOH A 515 1555 1555 2.42
SITE 1 AC1 16 LEU A 187 LEU A 188 ALA A 189 LEU A 222
SITE 2 AC1 16 HIS A 226 GLU A 227 HIS A 230 HIS A 236
SITE 3 AC1 16 LEU A 243 TYR A 245 PRO A 246 MET A 247
SITE 4 AC1 16 TYR A 248 ZN A 302 PGO A 315 HOH A 501
SITE 1 AC2 4 HIS A 226 HIS A 230 HIS A 236 N73 A 301
SITE 1 AC3 4 HIS A 175 ASP A 177 HIS A 190 HIS A 203
SITE 1 AC4 6 ASP A 182 GLY A 183 ASP A 185 LEU A 187
SITE 2 AC4 6 ASP A 205 GLU A 208
SITE 1 AC5 6 ASP A 165 GLY A 197 GLN A 199 ASP A 201
SITE 2 AC5 6 HOH A 415 HOH A 452
SITE 1 AC6 5 ASP A 131 ASP A 206 GLU A 208 HOH A 512
SITE 2 AC6 5 HOH A 515
SITE 1 AC7 3 HIS A 190 ALA A 191 PHE A 192
SITE 1 AC8 2 THR A 157 ASP A 182
SITE 1 AC9 6 ILE A 125 GLN A 126 TYR A 128 ALA A 173
SITE 2 AC9 6 GLU A 174 HOH A 460
SITE 1 AD1 6 SER A 211 LEU A 212 GLY A 215 VAL A 216
SITE 2 AD1 6 HIS A 266 HOH A 495
SITE 1 AD2 4 HIS A 118 HIS A 119 ASN A 120 HOH A 407
SITE 1 AD3 2 LEU A 187 ASN A 262
SITE 1 AD4 8 ASP A 113 LYS A 115 TRP A 116 HIS A 117
SITE 2 AD4 8 HIS A 118 GLY A 195 HOH A 406 HOH A 436
SITE 1 AD5 5 ARG A 162 GLY A 183 LYS A 184 ASP A 207
SITE 2 AD5 5 HOH A 537
SITE 1 AD6 5 PRO A 240 ALA A 242 ARG A 249 N73 A 301
SITE 2 AD6 5 HOH A 429
SITE 1 AD7 4 HIS A 117 GLU A 130 LEU A 132 PRO A 133
CRYST1 39.600 39.600 163.960 90.00 90.00 120.00 P 32 2 1 6
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 0.025253 0.014580 0.000000 0.00000
SCALE2 0.000000 0.029159 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006099 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
