HEADER HYDROLASE/SUBSTRATE 20-MAR-13 4JQG
TITLE CRYSTAL STRUCTURE OF AN INACTIVE MUTANT OF MMP-9 CATALYTIC DOMAIN IN
TITLE 2 COMPLEX WITH A FLUOROGENIC SYNTHETIC PEPTIDIC SUBSTRATE WITH A
TITLE 3 FLUORINE ATOM.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FLUOROGENIC PEPTIDIC SUBSTRATE (8MC)PLG(PFF)(DNW)AR(NH2);
COMPND 3 CHAIN: P, Q;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: MATRIX METALLOPROTEINASE-9;
COMPND 7 CHAIN: A, B;
COMPND 8 SYNONYM: MMP-9, 92 KDA GELATINASE, 92 KDA TYPE IV COLLAGENASE,
COMPND 9 GELATINASE B, GELB, 67 KDA MATRIX METALLOPROTEINASE-9, 82 KDA MATRIX
COMPND 10 METALLOPROTEINASE-9;
COMPND 11 EC: 3.4.24.35;
COMPND 12 ENGINEERED: YES;
COMPND 13 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: FLUOROGENIC SYNTHETIC L-PEPTIDE SUBSTRATE WITH LOWER
SOURCE 4 CATALYTIC EFFICIENCY WITH MMP-9 THAN THE IODINE CONTAINING SUBSTRATE
SOURCE 5 PDB CODE 4JIJ.;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 8 ORGANISM_COMMON: HUMAN;
SOURCE 9 ORGANISM_TAXID: 9606;
SOURCE 10 GENE: CLG4B, MMP9;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 13 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3 STAR);
SOURCE 14 EXPRESSION_SYSTEM_VECTOR_TYPE: PT7 PROMOTER;
SOURCE 15 EXPRESSION_SYSTEM_PLASMID: PET-14B
KEYWDS HALOGEN-WATER-HYDROGEN BRIDGE, ZINCIN-LIKE, GELATINASE, COLLAGENASE,
KEYWDS 2 CATALYTIC DOMAIN, HYDROLASE-SUBSTRATE COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR E.A.STURA,L.VERA,E.CASSAR-LAJEUNESSE,I.TRANCHANT,M.AMOURA,V.DIVE
REVDAT 5 06-DEC-23 4JQG 1 REMARK
REVDAT 4 20-SEP-23 4JQG 1 REMARK SEQADV LINK
REVDAT 3 16-AUG-17 4JQG 1 SOURCE REMARK
REVDAT 2 16-APR-14 4JQG 1 JRNL
REVDAT 1 12-MAR-14 4JQG 0
JRNL AUTH I.TRANCHANT,L.VERA,B.CZARNY,M.AMOURA,E.CASSAR,F.BEAU,
JRNL AUTH 2 E.A.STURA,V.DIVE
JRNL TITL HALOGEN BONDING CONTROLS SELECTIVITY OF FRET SUBSTRATE
JRNL TITL 2 PROBES FOR MMP-9.
JRNL REF CHEM.BIOL. V. 21 408 2014
JRNL REFN ISSN 1074-5521
JRNL PMID 24583051
JRNL DOI 10.1016/J.CHEMBIOL.2014.01.008
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8_1069)
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) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.52
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.990
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 29655
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.196
REMARK 3 R VALUE (WORKING SET) : 0.193
REMARK 3 FREE R VALUE : 0.242
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 1481
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 40.5335 - 4.1103 1.00 2777 146 0.1811 0.1972
REMARK 3 2 4.1103 - 3.2629 1.00 2648 139 0.1407 0.1770
REMARK 3 3 3.2629 - 2.8506 0.99 2550 134 0.1738 0.2462
REMARK 3 4 2.8506 - 2.5900 1.00 2580 134 0.1843 0.2724
REMARK 3 5 2.5900 - 2.4044 0.99 2537 134 0.2028 0.2805
REMARK 3 6 2.4044 - 2.2626 0.99 2546 133 0.2128 0.2565
REMARK 3 7 2.2626 - 2.1493 0.99 2514 131 0.2112 0.2773
REMARK 3 8 2.1493 - 2.0558 0.99 2534 133 0.2249 0.2878
REMARK 3 9 2.0558 - 1.9766 0.99 2512 133 0.2540 0.2915
REMARK 3 10 1.9766 - 1.9084 0.98 2478 129 0.2665 0.3285
REMARK 3 11 1.9084 - 1.8488 0.98 2498 135 0.3028 0.3348
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) : 0.220
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.080
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.05
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.05
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 2978
REMARK 3 ANGLE : 1.115 4053
REMARK 3 CHIRALITY : 0.079 389
REMARK 3 PLANARITY : 0.005 539
REMARK 3 DIHEDRAL : 16.629 1013
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 4JQG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-MAY-13.
REMARK 100 THE DEPOSITION ID IS D_1000078374.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-MAR-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.972981
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 : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29657
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.849
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 8.460
REMARK 200 R MERGE (I) : 0.34300
REMARK 200 R SYM (I) : 0.32500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.2900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.96
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.4
REMARK 200 DATA REDUNDANCY IN SHELL : 8.35
REMARK 200 R MERGE FOR SHELL (I) : 1.04500
REMARK 200 R SYM FOR SHELL (I) : 0.97900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.230
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: 4JIJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.18
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN: HMMP9 E402A AT 420 MICROM +
REMARK 280 AHA 120MM 0.12 M ACETOHYDROXAMIC ACID AND 0.5 MICROL IT34-F AT
REMARK 280 10 MILLI-M. RESERVOIR: 10% PEG 20K, 0.1 M MMT (L-MALIC ACID, MES,
REMARK 280 TRIS) 75% ACID/25% BASIC, 0.5 M NACL, 0.02 SRCL2, 10% GLYCEROL.
REMARK 280 CRYOPROTECTANT: 10% DI-ETHYLENE GLYCOL, 5% GLYCEROL, 10%
REMARK 280 PROPANEDIOL, 5% DIOXANE, .8 M LI FORMATE, 9% PEG 10,000 0.1M
REMARK 280 (MMT 75/25), PH 6.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 17.07000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 85.71000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 28.74000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 85.71000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 17.07000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 28.74000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3470 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 8460 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -92.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: P, 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3490 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 8680 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -140.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: Q, 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: 8450 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15770 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -250.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: P, A, Q, 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 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 -128.28 55.54
REMARK 500 ALA A 173 -131.45 55.54
REMARK 500 ASP A 185 -158.84 62.47
REMARK 500 LYS A 214 -11.01 71.45
REMARK 500 ALA B 173 -131.93 50.95
REMARK 500 ASP B 185 -163.95 64.16
REMARK 500 LEU B 212 -41.95 -133.17
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 301 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 AZI P 600 N3
REMARK 620 2 HIS A 226 NE2 100.3
REMARK 620 3 HIS A 230 NE2 99.4 103.5
REMARK 620 4 HIS A 236 NE2 136.1 111.9 101.1
REMARK 620 N 1 2 3
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 131 OD2
REMARK 620 2 ASP A 206 O 149.1
REMARK 620 3 GLU A 208 O 77.6 90.9
REMARK 620 4 PGO A 312 O1 69.9 139.9 91.7
REMARK 620 5 HOH A 577 O 86.2 72.1 113.6 140.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SR A 304 SR
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 165 O
REMARK 620 2 GLY A 197 O 166.7
REMARK 620 3 GLN A 199 O 85.8 82.8
REMARK 620 4 ASP A 201 OD1 83.8 102.5 88.9
REMARK 620 5 HOH A 562 O 82.7 87.7 73.5 158.5
REMARK 620 6 HOH A 581 O 101.6 83.1 139.5 131.2 68.2
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 175 NE2
REMARK 620 2 ASP A 177 OD1 110.7
REMARK 620 3 HIS A 190 NE2 106.8 116.3
REMARK 620 4 HIS A 203 ND1 112.6 94.2 116.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 303 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 182 OD1
REMARK 620 2 GLY A 183 O 84.9
REMARK 620 3 ASP A 185 O 86.9 87.4
REMARK 620 4 LEU A 187 O 89.6 174.3 93.9
REMARK 620 5 ASP A 205 OD2 91.2 85.0 172.4 93.5
REMARK 620 6 GLU A 208 OE2 173.7 95.7 86.8 89.9 95.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 309 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 432 O
REMARK 620 2 HOH B 402 O 89.1
REMARK 620 3 HOH B 464 O 125.9 133.1
REMARK 620 4 HOH B 593 O 125.2 128.1 59.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 301 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 AZI Q 600 N1
REMARK 620 2 HIS B 226 NE2 106.5
REMARK 620 3 HIS B 230 NE2 102.8 102.8
REMARK 620 4 HIS B 236 NE2 133.0 109.9 97.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SR B 305 SR
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 131 OD2
REMARK 620 2 ASP B 131 OD1 48.5
REMARK 620 3 ASP B 206 O 148.1 138.1
REMARK 620 4 ASP B 206 OD1 94.8 82.9 62.1
REMARK 620 5 GLU B 208 O 74.6 123.0 91.7 109.3
REMARK 620 6 PGO B 306 O1 77.4 68.0 134.0 147.3 99.3
REMARK 620 7 PGO B 306 O2 131.2 133.3 71.1 132.6 78.4 67.8
REMARK 620 8 HOH B 420 O 126.9 79.2 76.2 86.1 153.5 74.4 75.4
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SR B 304 SR
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 165 O
REMARK 620 2 GLY B 197 O 162.9
REMARK 620 3 GLN B 199 O 81.9 81.0
REMARK 620 4 ASP B 201 OD1 88.8 91.0 90.2
REMARK 620 5 HOH B 448 O 85.2 90.6 74.8 164.5
REMARK 620 6 HOH B 451 O 126.3 70.7 151.3 95.0 100.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 302 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 175 NE2
REMARK 620 2 ASP B 177 OD1 113.6
REMARK 620 3 HIS B 190 NE2 112.9 111.1
REMARK 620 4 HIS B 203 ND1 109.9 94.7 113.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 303 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 182 OD1
REMARK 620 2 GLY B 183 O 88.2
REMARK 620 3 ASP B 185 O 86.4 89.8
REMARK 620 4 LEU B 187 O 90.7 175.4 94.6
REMARK 620 5 ASP B 205 OD2 93.5 82.7 172.5 92.9
REMARK 620 6 GLU B 208 OE2 167.8 89.7 81.6 92.2 98.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 310 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 433 O
REMARK 620 2 HOH B 434 O 129.4
REMARK 620 3 HOH B 435 O 91.6 59.3
REMARK 620 4 HOH B 510 O 161.1 52.7 73.7
REMARK 620 5 HOH B 584 O 137.8 86.6 129.3 55.6
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 AZI P 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SR A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 308
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 309
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 310
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 311
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGO A 312
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AZI Q 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SR B 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SR B 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGO B 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 308
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 309
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 310
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 311
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4JIJ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF AN INACTIVE MUTANT OF MMP-9 CATALYTIC DOMAIN
REMARK 900 IN COMPLEX WITH A FLUOROGENIC SYNTHETIC PEPTIDIC SUBSTRATE
REMARK 900 RELATED ID: 4H3X RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF AN MMP BROAD SPECTRUM HYDROXAMATE BASED
REMARK 900 INHIBITOR CC27 IN COMPLEX WITH THE MMP-9 CATALYTIC DOMAIN
REMARK 900 RELATED ID: 4H1Q RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF AN MMP TWIN INHIBITOR COMPLEXING TWO MMP-9
REMARK 900 CATALYTIC DOMAINS STRUCTURE OF AN MMP TWIN INHIBITOR COMPLEXING TWO
REMARK 900 MMP-9 CATALYTIC DOMAINS
REMARK 900 RELATED ID: 4H2E RELATED DB: PDB
REMARK 900 CRYSTALCRYSTAL STRUCTURE OF AN MMP TWIN INHIBITOR COMPLEXING TWO
REMARK 900 MMP-9 CATALYTIC DOMAINS STRUCTURE OF AN MMP TWIN INHIBITOR
REMARK 900 COMPLEXING TWO MMP-9 CATALYTIC DOMAINS
REMARK 900 RELATED ID: 4HMA RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF AN MMP TWIN CARBOXYLATE BASED INHIBITOR LC20
REMARK 900 IN COMPLEX WITH THE MMP-9 CATALYTIC DOMAIN
REMARK 900 RELATED ID: 4H82 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MUTANT MMP-9 CATALYTIC DOMAIN IN COMPLEX WITH
REMARK 900 A TWIN INHIBITOR.
REMARK 900 RELATED ID: 2OW0 RELATED DB: PDB
REMARK 900 MMP-9 ACTIVE SITE MUTANT WITH IODINE-LABELED CARBOXYLATE INHIBITOR
REMARK 900 RELATED ID: 2OW1 RELATED DB: PDB
REMARK 900 MMP-9 ACTIVE SITE MUTANT WITH TRIFLUOROMETHYL HYDROXAMATE INHIBITOR
REMARK 900 RELATED ID: 4JXA RELATED DB: PDB
DBREF 4JQG A 107 216 UNP P14780 MMP9_HUMAN 107 216
DBREF 4JQG A 217 269 UNP P14780 MMP9_HUMAN 392 444
DBREF 4JQG B 107 216 UNP P14780 MMP9_HUMAN 107 216
DBREF 4JQG B 217 269 UNP P14780 MMP9_HUMAN 392 444
DBREF 4JQG P 1 9 PDB 4JQG 4JQG 1 9
DBREF 4JQG Q 1 9 PDB 4JQG 4JQG 1 9
SEQADV 4JQG ALA A 227 UNP P14780 GLU 402 ENGINEERED MUTATION
SEQADV 4JQG ALA B 227 UNP P14780 GLU 402 ENGINEERED MUTATION
SEQRES 1 P 9 8MC PRO LEU GLY PFF DNW ALA ARG NH2
SEQRES 1 A 164 GLY PHE GLN THR PHE GLU GLY ASP LEU LYS TRP HIS HIS
SEQRES 2 A 164 HIS ASN ILE THR TYR TRP ILE GLN ASN TYR SER GLU ASP
SEQRES 3 A 164 LEU PRO ARG ALA VAL ILE ASP ASP ALA PHE ALA ARG ALA
SEQRES 4 A 164 PHE ALA LEU TRP SER ALA VAL THR PRO LEU THR PHE THR
SEQRES 5 A 164 ARG VAL TYR SER ARG ASP ALA ASP ILE VAL ILE GLN PHE
SEQRES 6 A 164 GLY VAL ALA GLU HIS GLY ASP GLY TYR PRO PHE ASP GLY
SEQRES 7 A 164 LYS ASP GLY LEU LEU ALA HIS ALA PHE PRO PRO GLY PRO
SEQRES 8 A 164 GLY ILE GLN GLY ASP ALA HIS PHE ASP ASP ASP GLU LEU
SEQRES 9 A 164 TRP SER LEU GLY LYS GLY VAL GLY TYR SER LEU PHE LEU
SEQRES 10 A 164 VAL ALA ALA HIS ALA PHE GLY HIS ALA LEU GLY LEU ASP
SEQRES 11 A 164 HIS SER SER VAL PRO GLU ALA LEU MET TYR PRO MET TYR
SEQRES 12 A 164 ARG PHE THR GLU GLY PRO PRO LEU HIS LYS ASP ASP VAL
SEQRES 13 A 164 ASN GLY ILE ARG HIS LEU TYR GLY
SEQRES 1 Q 9 8MC PRO LEU GLY PFF DNW ALA ARG NH2
SEQRES 1 B 164 GLY PHE GLN THR PHE GLU GLY ASP LEU LYS TRP HIS HIS
SEQRES 2 B 164 HIS ASN ILE THR TYR TRP ILE GLN ASN TYR SER GLU ASP
SEQRES 3 B 164 LEU PRO ARG ALA VAL ILE ASP ASP ALA PHE ALA ARG ALA
SEQRES 4 B 164 PHE ALA LEU TRP SER ALA VAL THR PRO LEU THR PHE THR
SEQRES 5 B 164 ARG VAL TYR SER ARG ASP ALA ASP ILE VAL ILE GLN PHE
SEQRES 6 B 164 GLY VAL ALA GLU HIS GLY ASP GLY TYR PRO PHE ASP GLY
SEQRES 7 B 164 LYS ASP GLY LEU LEU ALA HIS ALA PHE PRO PRO GLY PRO
SEQRES 8 B 164 GLY ILE GLN GLY ASP ALA HIS PHE ASP ASP ASP GLU LEU
SEQRES 9 B 164 TRP SER LEU GLY LYS GLY VAL GLY TYR SER LEU PHE LEU
SEQRES 10 B 164 VAL ALA ALA HIS ALA PHE GLY HIS ALA LEU GLY LEU ASP
SEQRES 11 B 164 HIS SER SER VAL PRO GLU ALA LEU MET TYR PRO MET TYR
SEQRES 12 B 164 ARG PHE THR GLU GLY PRO PRO LEU HIS LYS ASP ASP VAL
SEQRES 13 B 164 ASN GLY ILE ARG HIS LEU TYR GLY
MODRES 4JQG PFF P 5 PHE 4-FLUORO-L-PHENYLALANINE
MODRES 4JQG DNW P 6 ALA 3-[(2,4-DINITROPHENYL)AMINO]-L-ALANINE
MODRES 4JQG PFF Q 5 PHE 4-FLUORO-L-PHENYLALANINE
MODRES 4JQG DNW Q 6 ALA 3-[(2,4-DINITROPHENYL)AMINO]-L-ALANINE
HET 8MC P 1 16
HET PFF P 5 12
HET DNW P 6 18
HET NH2 P 9 1
HET 8MC Q 1 16
HET PFF Q 5 12
HET DNW Q 6 18
HET NH2 Q 9 1
HET AZI P 600 3
HET ZN A 301 1
HET ZN A 302 1
HET CA A 303 1
HET SR A 304 1
HET CA A 305 1
HET EDO A 306 4
HET GOL A 307 6
HET EDO A 308 4
HET EDO A 309 4
HET EDO A 310 4
HET EDO A 311 4
HET PGO A 312 5
HET AZI Q 600 3
HET ZN B 301 1
HET ZN B 302 1
HET CA B 303 1
HET SR B 304 1
HET SR B 305 1
HET PGO B 306 5
HET EDO B 307 4
HET EDO B 308 4
HET NA B 309 1
HET NA B 310 1
HET NA B 311 1
HETNAM 8MC (7-METHOXY-2-OXO-2H-CHROMEN-4-YL)ACETIC ACID
HETNAM PFF 4-FLUORO-L-PHENYLALANINE
HETNAM DNW 3-[(2,4-DINITROPHENYL)AMINO]-L-ALANINE
HETNAM NH2 AMINO GROUP
HETNAM AZI AZIDE ION
HETNAM ZN ZINC ION
HETNAM CA CALCIUM ION
HETNAM SR STRONTIUM ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM GOL GLYCEROL
HETNAM PGO S-1,2-PROPANEDIOL
HETNAM NA SODIUM ION
HETSYN EDO ETHYLENE GLYCOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 8MC 2(C12 H10 O5)
FORMUL 1 PFF 2(C9 H10 F N O2)
FORMUL 1 DNW 2(C9 H10 N4 O6)
FORMUL 1 NH2 2(H2 N)
FORMUL 5 AZI 2(N3 1-)
FORMUL 6 ZN 4(ZN 2+)
FORMUL 8 CA 3(CA 2+)
FORMUL 9 SR 3(SR 2+)
FORMUL 11 EDO 7(C2 H6 O2)
FORMUL 12 GOL C3 H8 O3
FORMUL 17 PGO 2(C3 H8 O2)
FORMUL 27 NA 3(NA 1+)
FORMUL 30 HOH *428(H2 O)
HELIX 1 1 PRO A 133 VAL A 151 1 19
HELIX 2 2 LEU A 220 LEU A 232 1 13
HELIX 3 3 HIS A 257 GLY A 269 1 13
HELIX 4 4 PRO B 133 VAL B 151 1 19
HELIX 5 5 LEU B 220 GLY B 233 1 14
HELIX 6 6 HIS B 257 GLY B 269 1 13
SHEET 1 A 6 LEU P 3 DNW P 6 0
SHEET 2 A 6 LEU A 187 ALA A 191 -1 O LEU A 188 N PFF P 5
SHEET 3 A 6 ALA A 202 ASP A 205 -1 O HIS A 203 N HIS A 190
SHEET 4 A 6 ILE A 166 GLY A 171 1 N GLY A 171 O PHE A 204
SHEET 5 A 6 ASN A 120 ILE A 125 1 N TRP A 124 O ILE A 168
SHEET 6 A 6 THR A 155 ARG A 158 1 O THR A 157 N ILE A 121
SHEET 1 B 2 TRP A 210 SER A 211 0
SHEET 2 B 2 TYR A 218 SER A 219 1 O TYR A 218 N SER A 211
SHEET 1 C 6 LEU Q 3 DNW Q 6 0
SHEET 2 C 6 LEU B 187 ALA B 191 -1 O LEU B 188 N PFF Q 5
SHEET 3 C 6 ALA B 202 ASP B 205 -1 O HIS B 203 N HIS B 190
SHEET 4 C 6 ILE B 166 GLY B 171 1 N VAL B 167 O ALA B 202
SHEET 5 C 6 ASN B 120 ILE B 125 1 N TRP B 124 O ILE B 168
SHEET 6 C 6 THR B 155 ARG B 158 1 O THR B 155 N ILE B 121
SHEET 1 D 2 TRP B 210 SER B 211 0
SHEET 2 D 2 TYR B 218 SER B 219 1 O TYR B 218 N SER B 211
LINK C 8MC P 1 N PRO P 2 1555 1555 1.34
LINK C GLY P 4 N PFF P 5 1555 1555 1.33
LINK C PFF P 5 N DNW P 6 1555 1555 1.33
LINK C DNW P 6 N ALA P 7 1555 1555 1.33
LINK C ARG P 8 N NH2 P 9 1555 1555 1.33
LINK C 8MC Q 1 N PRO Q 2 1555 1555 1.34
LINK C GLY Q 4 N PFF Q 5 1555 1555 1.33
LINK C PFF Q 5 N DNW Q 6 1555 1555 1.33
LINK C DNW Q 6 N ALA Q 7 1555 1555 1.33
LINK C ARG Q 8 N NH2 Q 9 1555 1555 1.33
LINK N3 AZI P 600 ZN ZN A 301 1555 1555 2.05
LINK OD2 ASP A 131 CA CA A 305 1555 1555 2.52
LINK O ASP A 165 SR SR A 304 1555 1555 2.54
LINK NE2 HIS A 175 ZN ZN A 302 1555 1555 2.04
LINK OD1 ASP A 177 ZN ZN A 302 1555 1555 1.93
LINK OD1 ASP A 182 CA CA A 303 1555 1555 2.39
LINK O GLY A 183 CA CA A 303 1555 1555 2.26
LINK O ASP A 185 CA CA A 303 1555 1555 2.25
LINK O LEU A 187 CA CA A 303 1555 1555 2.35
LINK NE2 HIS A 190 ZN ZN A 302 1555 1555 2.00
LINK O GLY A 197 SR SR A 304 1555 1555 2.55
LINK O GLN A 199 SR SR A 304 1555 1555 2.61
LINK OD1 ASP A 201 SR SR A 304 1555 1555 2.62
LINK ND1 HIS A 203 ZN ZN A 302 1555 1555 2.04
LINK OD2 ASP A 205 CA CA A 303 1555 1555 2.33
LINK O ASP A 206 CA CA A 305 1555 1555 2.70
LINK OE2 GLU A 208 CA CA A 303 1555 1555 2.16
LINK O GLU A 208 CA CA A 305 1555 1555 2.26
LINK NE2 HIS A 226 ZN ZN A 301 1555 1555 2.00
LINK NE2 HIS A 230 ZN ZN A 301 1555 1555 2.13
LINK NE2 HIS A 236 ZN ZN A 301 1555 1555 2.00
LINK SR SR A 304 O HOH A 562 1555 1555 2.67
LINK SR SR A 304 O HOH A 581 1555 1555 2.62
LINK CA CA A 305 O1 PGO A 312 1555 1555 2.35
LINK CA CA A 305 O HOH A 577 1555 1555 2.14
LINK O HOH A 432 NA NA B 309 1555 1555 3.04
LINK N1 AZI Q 600 ZN ZN B 301 1555 1555 2.03
LINK OD2 ASP B 131 SR SR B 305 1555 1555 2.61
LINK OD1 ASP B 131 SR SR B 305 1555 1555 2.75
LINK O ASP B 165 SR SR B 304 1555 1555 2.57
LINK NE2 HIS B 175 ZN ZN B 302 1555 1555 2.07
LINK OD1 ASP B 177 ZN ZN B 302 1555 1555 1.89
LINK OD1 ASP B 182 CA CA B 303 1555 1555 2.36
LINK O GLY B 183 CA CA B 303 1555 1555 2.33
LINK O ASP B 185 CA CA B 303 1555 1555 2.32
LINK O LEU B 187 CA CA B 303 1555 1555 2.26
LINK NE2 HIS B 190 ZN ZN B 302 1555 1555 2.06
LINK O GLY B 197 SR SR B 304 1555 1555 2.46
LINK O GLN B 199 SR SR B 304 1555 1555 2.64
LINK OD1 ASP B 201 SR SR B 304 1555 1555 2.51
LINK ND1 HIS B 203 ZN ZN B 302 1555 1555 2.07
LINK OD2 ASP B 205 CA CA B 303 1555 1555 2.31
LINK O ASP B 206 SR SR B 305 1555 1555 2.58
LINK OD1 ASP B 206 SR SR B 305 1555 1555 2.73
LINK OE2 GLU B 208 CA CA B 303 1555 1555 2.24
LINK O GLU B 208 SR SR B 305 1555 1555 2.43
LINK NE2 HIS B 226 ZN ZN B 301 1555 1555 2.05
LINK NE2 HIS B 230 ZN ZN B 301 1555 1555 2.08
LINK NE2 HIS B 236 ZN ZN B 301 1555 1555 2.04
LINK SR SR B 304 O HOH B 448 1555 1555 2.49
LINK SR SR B 304 O HOH B 451 1555 1555 2.86
LINK SR SR B 305 O1 PGO B 306 1555 1555 2.62
LINK SR SR B 305 O2 PGO B 306 1555 1555 2.77
LINK SR SR B 305 O HOH B 420 1555 1555 2.59
LINK NA NA B 309 O HOH B 402 1555 1555 3.01
LINK NA NA B 309 O HOH B 464 1555 1555 2.30
LINK NA NA B 309 O HOH B 593 1555 1555 2.95
LINK NA NA B 310 O HOH B 433 1555 1555 2.78
LINK NA NA B 310 O HOH B 434 1555 1555 2.93
LINK NA NA B 310 O HOH B 435 1555 1555 2.67
LINK NA NA B 310 O HOH B 510 1555 1555 2.60
LINK NA NA B 310 O HOH B 584 1555 1555 2.31
SITE 1 AC1 9 ALA A 189 HIS A 190 HIS A 226 ALA A 227
SITE 2 AC1 9 HIS A 230 ZN A 301 LEU P 3 GLY P 4
SITE 3 AC1 9 PFF P 5
SITE 1 AC2 5 HIS A 226 HIS A 230 HIS A 236 GLY P 4
SITE 2 AC2 5 AZI P 600
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 7 ASP A 165 GLY A 197 GLN A 199 ASP A 201
SITE 2 AC5 7 HOH A 414 HOH A 562 HOH A 581
SITE 1 AC6 5 ASP A 131 ASP A 206 GLU A 208 PGO A 312
SITE 2 AC6 5 HOH A 577
SITE 1 AC7 5 LYS A 115 ARG A 265 LEU A 267 GLY A 269
SITE 2 AC7 5 PHE B 107
SITE 1 AC8 5 LEU A 114 GLY A 233 LEU A 234 ASP A 235
SITE 2 AC8 5 HOH A 425
SITE 1 AC9 4 LEU A 187 HIS A 190 HOH A 411 PRO P 2
SITE 1 BC1 7 ALA A 242 LEU A 243 ARG A 249 HOH A 446
SITE 2 BC1 7 HOH A 447 HOH A 557 PFF P 5
SITE 1 BC2 7 LYS A 115 TRP A 116 HIS A 117 HIS A 118
SITE 2 BC2 7 EDO A 311 HOH A 438 HOH A 589
SITE 1 BC3 4 GLY A 195 PRO A 196 EDO A 310 HOH A 448
SITE 1 BC4 9 ASP A 131 GLY A 197 ASP A 207 GLU A 208
SITE 2 BC4 9 LEU A 209 CA A 305 HOH A 450 HOH A 518
SITE 3 BC4 9 HOH A 576
SITE 1 BC5 9 ALA B 189 HIS B 190 HIS B 226 ALA B 227
SITE 2 BC5 9 HIS B 230 ZN B 301 LEU Q 3 GLY Q 4
SITE 3 BC5 9 PFF Q 5
SITE 1 BC6 5 HIS B 226 HIS B 230 HIS B 236 GLY Q 4
SITE 2 BC6 5 AZI Q 600
SITE 1 BC7 4 HIS B 175 ASP B 177 HIS B 190 HIS B 203
SITE 1 BC8 6 ASP B 182 GLY B 183 ASP B 185 LEU B 187
SITE 2 BC8 6 ASP B 205 GLU B 208
SITE 1 BC9 7 ALA B 164 ASP B 165 GLY B 197 GLN B 199
SITE 2 BC9 7 ASP B 201 HOH B 448 HOH B 451
SITE 1 CC1 5 ASP B 131 ASP B 206 GLU B 208 PGO B 306
SITE 2 CC1 5 HOH B 420
SITE 1 CC2 9 ASP B 131 LYS B 184 ASP B 206 ASP B 207
SITE 2 CC2 9 GLU B 208 LEU B 209 SR B 305 HOH B 500
SITE 3 CC2 9 HOH B 574
SITE 1 CC3 4 TYR B 179 HIS B 190 HOH B 491 PRO Q 2
SITE 1 CC4 1 HIS B 119
SITE 1 CC5 6 PRO A 255 HOH A 432 PRO B 255 HOH B 402
SITE 2 CC5 6 HOH B 464 HOH B 593
SITE 1 CC6 5 HOH B 433 HOH B 434 HOH B 435 HOH B 510
SITE 2 CC6 5 HOH B 584
SITE 1 CC7 2 HIS B 117 HIS B 118
CRYST1 34.140 57.480 171.420 90.00 90.00 90.00 P 21 21 21 8
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 0.029291 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017397 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005834 0.00000
HETATM 1 C 8MC P 1 -8.704 7.027 -34.933 1.00 15.16 C
HETATM 2 O 8MC P 1 -8.651 6.932 -33.694 1.00 14.16 O
HETATM 3 CA 8MC P 1 -8.092 8.244 -35.619 1.00 17.22 C
HETATM 4 C9 8MC P 1 -8.479 9.515 -34.874 1.00 10.34 C
HETATM 5 C10 8MC P 1 -7.701 10.025 -33.837 1.00 18.07 C
HETATM 6 C1 8MC P 1 -8.134 11.203 -33.213 1.00 16.91 C
HETATM 7 O2 8MC P 1 -7.479 11.693 -32.274 1.00 15.75 O
HETATM 8 C8 8MC P 1 -9.626 10.228 -35.205 1.00 12.85 C
HETATM 9 C7 8MC P 1 -10.449 9.788 -36.231 1.00 11.45 C
HETATM 10 C6 8MC P 1 -11.604 10.494 -36.542 1.00 15.34 C
HETATM 11 C5 8MC P 1 -11.932 11.658 -35.836 1.00 13.61 C
HETATM 12 O4 8MC P 1 -13.070 12.343 -36.181 1.00 17.40 O
HETATM 13 C11 8MC P 1 -13.714 13.250 -35.295 1.00 13.58 C
HETATM 14 C4 8MC P 1 -11.099 12.106 -34.811 1.00 15.34 C
HETATM 15 C2 8MC P 1 -9.940 11.386 -34.494 1.00 17.87 C
HETATM 16 O3 8MC P 1 -9.187 11.799 -33.561 1.00 17.42 O
(ATOM LINES ARE NOT SHOWN.)
END
