HEADER HYDROLASE 11-MAR-02 1L6J
TITLE CRYSTAL STRUCTURE OF HUMAN MATRIX METALLOPROTEINASE MMP9 (GELATINASE
TITLE 2 B).
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MATRIX METALLOPROTEINASE-9;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PRO-FORM WITH C-TERMINAL DOMAIN TRUNCATED;
COMPND 5 SYNONYM: MMP9, GELATINASE B, GELB;
COMPND 6 EC: 3.4.24.35;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BLR (DE3)
KEYWDS TWISTED BETA SHEET FLANKED BY HELICES, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.A.ELKINS,Y.S.HO,W.W.SMITH,C.A.JANSON,K.J.D'ALESSIO,M.S.MCQUENEY,
AUTHOR 2 M.D.CUMMINGS,A.M.ROMANIC
REVDAT 5 16-AUG-23 1L6J 1 REMARK LINK
REVDAT 4 24-FEB-09 1L6J 1 VERSN
REVDAT 3 01-APR-03 1L6J 1 JRNL
REVDAT 2 17-JUL-02 1L6J 1 DBREF
REVDAT 1 03-JUL-02 1L6J 0
JRNL AUTH P.A.ELKINS,Y.S.HO,W.W.SMITH,C.A.JANSON,K.J.D'ALESSIO,
JRNL AUTH 2 M.S.MCQUENEY,M.D.CUMMINGS,A.M.ROMANIC
JRNL TITL STRUCTURE OF THE C-TERMINALLY TRUNCATED HUMAN PROMMP9, A
JRNL TITL 2 GELATIN-BINDING MATRIX METALLOPROTEINASE.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 58 1182 2002
JRNL REFN ISSN 0907-4449
JRNL PMID 12077439
JRNL DOI 10.1107/S0907444902007849
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.97
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 89.1
REMARK 3 NUMBER OF REFLECTIONS : 24477
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.187
REMARK 3 FREE R VALUE : 0.230
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1265
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.53
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 20219
REMARK 3 BIN R VALUE (WORKING SET) : 0.2720
REMARK 3 BIN FREE R VALUE : 0.3150
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 39
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3180
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 5
REMARK 3 SOLVENT ATOMS : 191
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.00
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.29
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 0.013 ; 0.011
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.840 ; 2.030
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : 0.76
REMARK 3 BSOL : 250.0
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 STRUCTURE FACTOR ANALYSIS FOR THIS REPORT WAS
REMARK 3 MADE BY SFCHECK V 5.3.4 USING ANISOTROPIC SCALING
REMARK 3 AND THE BABINET BULK SOLVENT CORRECTION.
REMARK 3 THE CORRELATION BETWEEN THE EXPERIMENTAL MAP AND
REMARK 3 THE MODEL WAS COMPUTED USING CCP4/SFALL, CCP4/FFT
REMARK 3 AND CCP4/OVERLAPMAP. THE DIFFERENCE BETWEEN THE
REMARK 3 EXPERIMENTAL PHASES AND THE MODEL PHASES WAS
REMARK 3 COMPUTED USING CCP4/SFALL AND CCP4/PHISTATS.
REMARK 4
REMARK 4 1L6J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-MAR-02.
REMARK 100 THE DEPOSITION ID IS D_1000015687.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 8.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X12C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.271632, 1.209997, 1.272917
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : BRANDEIS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34009
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 89.1
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.07700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 73.8
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.19400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: PDB ENTRY 1CK7
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 70.66
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CHLORIDE, TRIS, HEPES, PH 8.2,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65
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 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
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 59.95800
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 29.97900
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 44.96850
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 14.98950
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 74.94750
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 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ALA A 20
REMARK 465 PRO A 21
REMARK 465 ARG A 22
REMARK 465 GLN A 23
REMARK 465 ARG A 24
REMARK 465 GLN A 25
REMARK 465 SER A 26
REMARK 465 THR A 27
REMARK 465 LEU A 28
REMARK 465 ARG A 56
REMARK 465 VAL A 57
REMARK 465 ALA A 58
REMARK 465 GLU A 59
REMARK 465 MET A 60
REMARK 465 ARG A 61
REMARK 465 GLY A 62
REMARK 465 GLU A 63
REMARK 465 SER A 64
REMARK 465 LYS A 65
REMARK 465 SER A 66
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 GLU A 174 N - CA - C ANGL. DEV. = -16.2 DEGREES
REMARK 500 PRO A 430 C - N - CA ANGL. DEV. = -10.2 DEGREES
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 LEU A 39 152.67 -47.37
REMARK 500 ALA A 173 -81.72 -141.55
REMARK 500 ALA A 189 -177.04 -175.20
REMARK 500 SER A 211 -153.40 -156.08
REMARK 500 ASP A 226 17.60 58.32
REMARK 500 ARG A 239 146.30 -14.77
REMARK 500 ASP A 266 19.97 53.92
REMARK 500 ASP A 280 -137.29 58.34
REMARK 500 ASP A 309 35.17 -80.68
REMARK 500 ALA A 318 7.36 -65.40
REMARK 500 ASN A 319 105.76 -168.62
REMARK 500 SER A 342 29.89 -144.28
REMARK 500 ARG A 370 152.61 -49.91
REMARK 500 ASP A 390 -155.58 -97.17
REMARK 500 ASP A 410 -164.60 -116.23
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 500 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 99 SG
REMARK 620 2 HIS A 401 NE2 104.7
REMARK 620 3 HIS A 405 NE2 117.2 107.3
REMARK 620 4 HIS A 411 NE2 117.7 106.4 102.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 503 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 131 OD2
REMARK 620 2 ASP A 206 O 155.5
REMARK 620 3 ASP A 206 OD1 82.9 74.6
REMARK 620 4 GLU A 208 O 77.8 96.5 99.9
REMARK 620 5 HOH A1054 O 81.7 105.9 86.5 157.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 504 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 165 O
REMARK 620 2 GLY A 197 O 141.6
REMARK 620 3 GLN A 199 O 72.0 72.8
REMARK 620 4 ASP A 201 OD1 91.7 90.5 70.3
REMARK 620 5 HOH A1052 O 115.2 60.1 103.8 149.8
REMARK 620 6 HOH A1084 O 154.4 62.8 124.5 78.2 81.9
REMARK 620 7 HOH A1174 O 70.1 81.6 65.2 135.2 52.5 132.6
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 501 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 175 NE2
REMARK 620 2 ASP A 177 OD2 115.0
REMARK 620 3 HIS A 190 NE2 112.4 116.2
REMARK 620 4 HIS A 203 ND1 102.2 93.4 115.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 502 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 182 OD1
REMARK 620 2 GLY A 183 O 91.8
REMARK 620 3 GLY A 186 N 84.5 97.1
REMARK 620 4 LEU A 187 O 83.9 169.5 92.0
REMARK 620 5 ASP A 205 OD2 98.5 81.8 176.8 89.4
REMARK 620 6 GLU A 208 OE2 177.6 89.9 97.0 94.1 80.0
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 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 504
DBREF 1L6J A 20 444 UNP P14780 MMP9_HUMAN 20 444
SEQRES 1 A 425 ALA PRO ARG GLN ARG GLN SER THR LEU VAL LEU PHE PRO
SEQRES 2 A 425 GLY ASP LEU ARG THR ASN LEU THR ASP ARG GLN LEU ALA
SEQRES 3 A 425 GLU GLU TYR LEU TYR ARG TYR GLY TYR THR ARG VAL ALA
SEQRES 4 A 425 GLU MET ARG GLY GLU SER LYS SER LEU GLY PRO ALA LEU
SEQRES 5 A 425 LEU LEU LEU GLN LYS GLN LEU SER LEU PRO GLU THR GLY
SEQRES 6 A 425 GLU LEU ASP SER ALA THR LEU LYS ALA MET ARG THR PRO
SEQRES 7 A 425 ARG CYS GLY VAL PRO ASP LEU GLY ARG PHE GLN THR PHE
SEQRES 8 A 425 GLU GLY ASP LEU LYS TRP HIS HIS HIS ASN ILE THR TYR
SEQRES 9 A 425 TRP ILE GLN ASN TYR SER GLU ASP LEU PRO ARG ALA VAL
SEQRES 10 A 425 ILE ASP ASP ALA PHE ALA ARG ALA PHE ALA LEU TRP SER
SEQRES 11 A 425 ALA VAL THR PRO LEU THR PHE THR ARG VAL TYR SER ARG
SEQRES 12 A 425 ASP ALA ASP ILE VAL ILE GLN PHE GLY VAL ALA GLU HIS
SEQRES 13 A 425 GLY ASP GLY TYR PRO PHE ASP GLY LYS ASP GLY LEU LEU
SEQRES 14 A 425 ALA HIS ALA PHE PRO PRO GLY PRO GLY ILE GLN GLY ASP
SEQRES 15 A 425 ALA HIS PHE ASP ASP ASP GLU LEU TRP SER LEU GLY LYS
SEQRES 16 A 425 GLY VAL VAL VAL PRO THR ARG PHE GLY ASN ALA ASP GLY
SEQRES 17 A 425 ALA ALA CYS HIS PHE PRO PHE ILE PHE GLU GLY ARG SER
SEQRES 18 A 425 TYR SER ALA CYS THR THR ASP GLY ARG SER ASP GLY LEU
SEQRES 19 A 425 PRO TRP CYS SER THR THR ALA ASN TYR ASP THR ASP ASP
SEQRES 20 A 425 ARG PHE GLY PHE CYS PRO SER GLU ARG LEU TYR THR ARG
SEQRES 21 A 425 ASP GLY ASN ALA ASP GLY LYS PRO CYS GLN PHE PRO PHE
SEQRES 22 A 425 ILE PHE GLN GLY GLN SER TYR SER ALA CYS THR THR ASP
SEQRES 23 A 425 GLY ARG SER ASP GLY TYR ARG TRP CYS ALA THR THR ALA
SEQRES 24 A 425 ASN TYR ASP ARG ASP LYS LEU PHE GLY PHE CYS PRO THR
SEQRES 25 A 425 ARG ALA ASP SER THR VAL MET GLY GLY ASN SER ALA GLY
SEQRES 26 A 425 GLU LEU CYS VAL PHE PRO PHE THR PHE LEU GLY LYS GLU
SEQRES 27 A 425 TYR SER THR CYS THR SER GLU GLY ARG GLY ASP GLY ARG
SEQRES 28 A 425 LEU TRP CYS ALA THR THR SER ASN PHE ASP SER ASP LYS
SEQRES 29 A 425 LYS TRP GLY PHE CYS PRO ASP GLN GLY TYR SER LEU PHE
SEQRES 30 A 425 LEU VAL ALA ALA HIS GLU PHE GLY HIS ALA LEU GLY LEU
SEQRES 31 A 425 ASP HIS SER SER VAL PRO GLU ALA LEU MET TYR PRO MET
SEQRES 32 A 425 TYR ARG PHE THR GLU GLY PRO PRO LEU HIS LYS ASP ASP
SEQRES 33 A 425 VAL ASN GLY ILE ARG HIS LEU TYR GLY
HET ZN A 500 1
HET ZN A 501 1
HET CA A 502 1
HET CA A 503 1
HET CA A 504 1
HETNAM ZN ZINC ION
HETNAM CA CALCIUM ION
FORMUL 2 ZN 2(ZN 2+)
FORMUL 4 CA 3(CA 2+)
FORMUL 7 HOH *191(H2 O)
HELIX 1 1 THR A 40 TYR A 52 1 13
HELIX 2 2 LEU A 67 SER A 79 1 13
HELIX 3 3 ASP A 87 ARG A 95 1 9
HELIX 4 4 PRO A 133 VAL A 151 1 19
HELIX 5 5 ASN A 261 ASP A 266 1 6
HELIX 6 6 ASN A 319 LYS A 324 1 6
HELIX 7 7 ARG A 332 THR A 336 5 5
HELIX 8 8 ASN A 378 LYS A 383 1 6
HELIX 9 9 LEU A 395 LEU A 407 1 13
HELIX 10 10 HIS A 432 TYR A 443 1 12
SHEET 1 A 5 THR A 155 VAL A 159 0
SHEET 2 A 5 ASN A 120 ILE A 125 1 N TYR A 123 O VAL A 159
SHEET 3 A 5 ILE A 166 GLY A 171 1 O ILE A 168 N TRP A 124
SHEET 4 A 5 ALA A 202 ASP A 205 1 O PHE A 204 N GLN A 169
SHEET 5 A 5 ALA A 189 ALA A 191 -1 N HIS A 190 O HIS A 203
SHEET 1 B 2 TRP A 210 SER A 211 0
SHEET 2 B 2 TYR A 393 SER A 394 1 O TYR A 393 N SER A 211
SHEET 1 C 2 PHE A 234 ILE A 235 0
SHEET 2 C 2 SER A 240 TYR A 241 -1 O TYR A 241 N PHE A 234
SHEET 1 D 2 TRP A 255 SER A 257 0
SHEET 2 D 2 PHE A 268 PHE A 270 -1 O GLY A 269 N CYS A 256
SHEET 1 E 2 PHE A 292 PHE A 294 0
SHEET 2 E 2 GLN A 297 TYR A 299 -1 O GLN A 297 N PHE A 294
SHEET 1 F 2 TRP A 313 ALA A 315 0
SHEET 2 F 2 PHE A 326 PHE A 328 -1 O GLY A 327 N CYS A 314
SHEET 1 G 2 PHE A 351 PHE A 353 0
SHEET 2 G 2 LYS A 356 TYR A 358 -1 O TYR A 358 N PHE A 351
SHEET 1 H 2 TRP A 372 ALA A 374 0
SHEET 2 H 2 TRP A 385 PHE A 387 -1 O GLY A 386 N CYS A 373
SSBOND 1 CYS A 230 CYS A 256 1555 1555 2.03
SSBOND 2 CYS A 244 CYS A 271 1555 1555 2.03
SSBOND 3 CYS A 288 CYS A 314 1555 1555 2.01
SSBOND 4 CYS A 302 CYS A 329 1555 1555 2.04
SSBOND 5 CYS A 347 CYS A 373 1555 1555 2.02
SSBOND 6 CYS A 361 CYS A 388 1555 1555 2.03
LINK SG CYS A 99 ZN ZN A 500 1555 1555 2.32
LINK OD2 ASP A 131 CA CA A 503 1555 1555 2.76
LINK O ASP A 165 CA CA A 504 1555 1555 2.75
LINK NE2 HIS A 175 ZN ZN A 501 1555 1555 2.19
LINK OD2 ASP A 177 ZN ZN A 501 1555 1555 2.17
LINK OD1 ASP A 182 CA CA A 502 1555 1555 2.61
LINK O GLY A 183 CA CA A 502 1555 1555 2.44
LINK N GLY A 186 CA CA A 502 1555 1555 2.86
LINK O LEU A 187 CA CA A 502 1555 1555 2.50
LINK NE2 HIS A 190 ZN ZN A 501 1555 1555 2.24
LINK O GLY A 197 CA CA A 504 1555 1555 2.85
LINK O GLN A 199 CA CA A 504 1555 1555 3.03
LINK OD1 ASP A 201 CA CA A 504 1555 1555 2.66
LINK ND1 HIS A 203 ZN ZN A 501 1555 1555 2.13
LINK OD2 ASP A 205 CA CA A 502 1555 1555 2.46
LINK O ASP A 206 CA CA A 503 1555 1555 2.52
LINK OD1 ASP A 206 CA CA A 503 1555 1555 2.72
LINK OE2 GLU A 208 CA CA A 502 1555 1555 2.46
LINK O GLU A 208 CA CA A 503 1555 1555 2.65
LINK NE2 HIS A 401 ZN ZN A 500 1555 1555 2.26
LINK NE2 HIS A 405 ZN ZN A 500 1555 1555 2.05
LINK NE2 HIS A 411 ZN ZN A 500 1555 1555 2.21
LINK CA CA A 503 O HOH A1054 1555 1555 2.78
LINK CA CA A 504 O HOH A1052 1555 1555 3.04
LINK CA CA A 504 O HOH A1084 1555 1555 3.34
LINK CA CA A 504 O HOH A1174 1555 1555 2.96
CISPEP 1 PHE A 232 PRO A 233 0 -0.27
CISPEP 2 PHE A 290 PRO A 291 0 0.27
CISPEP 3 PHE A 349 PRO A 350 0 -0.06
SITE 1 AC1 4 CYS A 99 HIS A 401 HIS A 405 HIS A 411
SITE 1 AC2 4 HIS A 175 ASP A 177 HIS A 190 HIS A 203
SITE 1 AC3 6 ASP A 182 GLY A 183 GLY A 186 LEU A 187
SITE 2 AC3 6 ASP A 205 GLU A 208
SITE 1 AC4 4 ASP A 131 ASP A 206 GLU A 208 HOH A1054
SITE 1 AC5 7 ALA A 164 ASP A 165 GLY A 197 GLN A 199
SITE 2 AC5 7 ASP A 201 HOH A1052 HOH A1174
CRYST1 123.685 123.685 89.937 90.00 90.00 120.00 P 65 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 0.008085 0.004668 0.000000 0.00000
SCALE2 0.000000 0.009336 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011119 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
