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Database: PDB
Entry: 5UE5
LinkDB: 5UE5
Original site: 5UE5 
HEADER    HYDROLASE                               29-DEC-16   5UE5              
TITLE     PROMMP-7 WITH HEPARIN OCTASACCHARIDE BOUND TO THE CATALYTIC DOMAIN    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MATRILYSIN;                                                
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: MATRIN,MATRIX METALLOPROTEINASE-7,MMP-7,PUMP-1 PROTEASE,    
COMPND   5 UTERINE METALLOPROTEINASE;                                           
COMPND   6 EC: 3.4.24.23;                                                       
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 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: MMP7, MPSL1, PUMP1;                                            
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    GLYCAN COMPLEX WITH PROTEIN, ENZYME COMPLEX WITH HEPARIN              
KEYWDS   2 OLIGOSACCHARIDE, ZYMOGEN, ALLOSTERIC EFFECTOR SITE, HYDROLASE        
EXPDTA    SOLUTION NMR                                                          
NUMMDL    16                                                                    
AUTHOR    Y.G.FULCHER,S.H.PRIOR,R.J.LINHARDT,S.R.VAN DOREN                      
REVDAT   2   27-SEP-17 5UE5    1       REMARK                                   
REVDAT   1   19-JUL-17 5UE5    0                                                
JRNL        AUTH   Y.G.FULCHER,S.H.PRIOR,S.MASUKO,L.LI,D.PU,F.ZHANG,            
JRNL        AUTH 2 R.J.LINHARDT,S.R.VAN DOREN                                   
JRNL        TITL   GLYCAN ACTIVATION OF A SHEDDASE: ELECTROSTATIC RECOGNITION   
JRNL        TITL 2 BETWEEN HEPARIN AND PROMMP-7.                                
JRNL        REF    STRUCTURE                     V.  25  1100 2017              
JRNL        REFN                   ISSN 1878-4186                               
JRNL        PMID   28648610                                                     
JRNL        DOI    10.1016/J.STR.2017.05.019                                    
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   S.H.PRIOR,Y.G.FULCHER,R.K.KOPPISETTI,A.JURKEVICH,            
REMARK   1  AUTH 2 S.R.VAN DOREN                                                
REMARK   1  TITL   CHARGE-TRIGGERED MEMBRANE INSERTION OF MATRIX                
REMARK   1  TITL 2 METALLOPROTEINASE-7, SUPPORTER OF INNATE IMMUNITY AND        
REMARK   1  TITL 3 TUMORS.                                                      
REMARK   1  REF    STRUCTURE                     V.  23  2099 2015              
REMARK   1  REFN                   ISSN 1878-4186                               
REMARK   1  PMID   26439767                                                     
REMARK   1  DOI    10.1016/J.STR.2015.08.013                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION. NOT APPLICABLE.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : SYBYL X 2.1.1                                        
REMARK   3   AUTHORS     : TRIPOS / CERTARA                                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS:                                           
REMARK   3  15000 STEPS OF REFINEMENT. EXPLICIT DISTANCE RESTRAINTS TO THE      
REMARK   3  TEMPO SPIN-LABELED REDUCING END OF HEPARIN DP8 WERE OBTAINED FROM   
REMARK   3  THE PRES (T2) USING AN EQUATION FROM BATTISTE AND WAGNER (2000,     
REMARK   3  BIOCHEMISTRY) SIMPLIFIED BY WHTC GREATER THAN1 TO THE FORM R EQUAL  
REMARK   3  TO 4KTC/T2  GIVEN BY KOPPISETTI ET AL. (2014, NATURE COMMS.). THE   
REMARK   3  ROTATIONAL CORRELATION TIME TC OF THE PROTEIN-HEPARIN COMPLEXES     
REMARK   3  WAS OBTAINED FROM AMIDE 15N CROSS-CORRELATION RATES NXY (LIU AND    
REMARK   3  PRESTEGARD, 2008, J. MAGN. RESON.) INTERPRETED BY THE SPECTRAL      
REMARK   3  DENSITY EXPRESSION USED IN THE TRACT APPROACH (LEE ET AL., 2006.    
REMARK   3  J. MAGN. RESON.). UPPER BOUNDS WERE SET AT 15% ABOVE THE DISTANCE   
REMARK   3  ESTIMATE. AN INTERMOLECULAR NOE FROM AN ARGININE BACKBONE AMIDE     
REMARK   3  FROM 2H/15N-LABELED ENZYME TO THE ANOMERIC PROTON H1 OF GLCNS6S 5   
REMARK   3  OR 7 HAD AN UPPER BOUND OF 6 A. LOWER BOUNDS WERE IMPLICITLY AT     
REMARK   3  VAN DER WAALS DISTANCE.                                             
REMARK   3  AMBIGUOUS DISTANCE RESTRAINTS FROM ANY RESIDUE OF HEPARIN DP8 TO    
REMARK   3  EXPLICIT PROTEIN AMIDE GROUPS WERE APPLIED ON THE BASIS OF AMIDE    
REMARK   3  CHEMICAL SHIFT PERTURBATIONS FROM HEPARIN DP8 OR PROTECTION OF      
REMARK   3  AMIDES BY HEPARIN DP4 FROM LINE BROADENING BY GD.EDTA WITH DELTAT2  
REMARK   3  GREATER THAN 37/SEC. AMBIGUOUS DISTANCE RESTRAINTS FROM ANY         
REMARK   3  RESIDUE OF HEPARIN DP8 TO LYSINE AMINO OR ARGININE UREIDO GROUPS    
REMARK   3  WERE ALSO APPLIED ON THE BASIS OF MUTATIONS THAT IMPAIRED           
REMARK   3  ACTIVATION OF PROMMP-7 BY HEPARIN DP16. THE COMBINATION OF THE      
REMARK   3  INTERMOLECULAR DISTANCE RESTRAINTS FROM THE EXPLICIT PRE AND NOE    
REMARK   3  MEASUREMENTS AND THE AMBIGUOUS SOURCES WERE USED TO DOCK            
REMARK   3  COORDINATES OF HEPARIN DP8 WITH THE NMR SOLUTION STRUCTURE OF       
REMARK   3  HUMAN PROMMP-7 OF PRIOR ET AL. (2015, STRUCTURE). TO ENABLE         
REMARK   3  MOLECULAR FLEXIBILITY WIDELY THROUGH THE PROMMP-7 AND HEPARIN DP8   
REMARK   3  CHAINS WHILE MAINTAINING THE STRUCTURAL INTEGRITY OF THE PROMMP-7   
REMARK   3  DURING THE RESTRAINED DOCKING SIMULATIONS, CYANA 2.1 (GUNTERT AND   
REMARK   3  BUCHNER, 2015, J. BIOMOL. NMR) WAS UTILIZED IN CONCERT WITH THE     
REMARK   3  INTRAMOLECULAR PROMMP-7 NOE-DERIVED DISTANCE RESTRAINTS AND         
REMARK   3  CHEMICAL SHIFT-DERIVED DIHEDRAL RESTRAINTS OF THE NMR STRUCTURE     
REMARK   3  (PRIOR ET AL., 2015, STRUCTURE). CYANA TOPOLOGY FILES DESCRIBING    
REMARK   3  THE SUGAR MONOMERS WERE DERIVED FROM TOPOLOGY FILES CURATED BY THE  
REMARK   3  AUTOMATED TOPOLOGY BUILDER (MALDE ET AL., 2011, J. CHEM. THEORY     
REMARK   3  COMPUT.) AND BASED ON ACCESSION NUMBER 9804 FOR 2-O-SULFO-ALPHA-L-  
REMARK   3  IDOPYRANURONIC ACID (IDS OR IDOA2S) AND 9778 FOR N,O6-DISULFO-      
REMARK   3  GLUCOSAMINE (SGN OR GLCNS6S). THE GLOBALLY FLEXIBLE DOCKING         
REMARK   3  SIMULATIONS REQUIRED THE PROMMP-7 POLYPEPTIDE TO BE LINKED TO THE   
REMARK   3  CALCIUM AND ZINC IONS AND HEPARIN DP8 CHAINS VIA TETHERS OF NON-    
REMARK   3  INTERACTING PSEUDOATOMS. WITH THIS TETHERING AND FLEXIBLE           
REMARK   3  STRUCTURAL INTEGRITY ENFORCED, THE CARBOHYDRATE CHAINS WERE DOCKED  
REMARK   3  WITH THE INTERMOLECULAR DISTANCE RESTRAINTS                         
REMARK   4                                                                      
REMARK   4 5UE5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-JAN-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000225723.                                   
REMARK 210                                                                      
REMARK 210 EXPERIMENTAL DETAILS                                                 
REMARK 210  EXPERIMENT TYPE                : NMR                                
REMARK 210  TEMPERATURE           (KELVIN) : 310; 310; 310; 310                 
REMARK 210  PH                             : 6.6; 6.6; 6.6; 6.6                 
REMARK 210  IONIC STRENGTH                 : 180; 180; 180; 30                  
REMARK 210  PRESSURE                       : 1 ATM; 1 ATM; 1 ATM; 1 ATM         
REMARK 210  SAMPLE CONTENTS                : 300 UM [U-99% 15N] PROMMP-7, 450   
REMARK 210                                   UM HEPARIN DP8, 93% H2O/7% D2O;    
REMARK 210                                   300 UM [U-99% 2H/15N] PROMMP-7,    
REMARK 210                                   450 UM HEPARIN DP8-TEMPO, 93%      
REMARK 210                                   H2O/7% D2O; 300 UM [U-99% 2H/15N]  
REMARK 210                                   PROMMP-7, 450 UM HEPARIN DP8,      
REMARK 210                                   93% H2O/7% D2O; 300 UM [U-99% 2H/  
REMARK 210                                   15N] PROMMP-7, 450 UM HEPARIN      
REMARK 210                                   DP4, 93% H2O/7% D2O; 300 UM [U-    
REMARK 210                                   100% 13C; U-100% 15N; U-80% 2H]    
REMARK 210                                   PROMMP-7, 93% H2O/7% D2O           
REMARK 210                                                                      
REMARK 210  NMR EXPERIMENTS CONDUCTED      : 3D 1H-15N NOESY; TROSY-DETECTED    
REMARK 210                                   TITRATION; PRES BY PROJECT-CPMG    
REMARK 210                                   TROSY; SOLVENT PRES, 1H            
REMARK 210                                   RELAXATION DETECTED VIA TROSY;     
REMARK 210                                   3D HNCACB; 3D CBCA(CO)NH           
REMARK 210  SPECTROMETER FIELD STRENGTH    : 800 MHZ                            
REMARK 210  SPECTROMETER MODEL             : AVANCEIII                          
REMARK 210  SPECTROMETER MANUFACTURER      : BRUKER                             
REMARK 210                                                                      
REMARK 210  STRUCTURE DETERMINATION.                                            
REMARK 210   SOFTWARE USED                 : CYANA 2.1, SPARKY, ANALYSIS,       
REMARK 210                                   TOPSPIN                            
REMARK 210   METHOD USED                   : TORSION ANGLE DYNAMICS             
REMARK 210                                                                      
REMARK 210 CONFORMERS, NUMBER CALCULATED   : 200                                
REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 16                                 
REMARK 210 CONFORMERS, SELECTION CRITERIA  : STRUCTURES WITH THE LEAST          
REMARK 210                                   RESTRAINT VIOLATIONS               
REMARK 210                                                                      
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1                   
REMARK 210                                                                      
REMARK 210 REMARK: NULL                                                         
REMARK 215                                                                      
REMARK 215 NMR STUDY                                                            
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION           
REMARK 215 NMR DATA.  PROTEIN DATA BANK CONVENTIONS REQUIRE THAT                
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON              
REMARK 215 THESE RECORDS ARE MEANINGLESS.                                       
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 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500  4 HIS A 143   CE1   HIS A 143   NE2    -0.067                       
REMARK 500  6 HIS A 143   CE1   HIS A 143   NE2    -0.067                       
REMARK 500  8 HIS A 123   CE1   HIS A 123   NE2    -0.067                       
REMARK 500 13 HIS A 198   CE1   HIS A 198   NE2    -0.067                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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  1 TRP A  12   CE2 -  CD2 -  CG  ANGL. DEV. =  -4.8 DEGREES          
REMARK 500  1 ARG A  21   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500  1 TRP A  84   CE2 -  CD2 -  CG  ANGL. DEV. =  -4.9 DEGREES          
REMARK 500  1 ARG A  92   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500  1 ARG A  98   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500  1 ARG A 107   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500  1 TRP A 116   CE2 -  CD2 -  CG  ANGL. DEV. =  -4.8 DEGREES          
REMARK 500  1 ARG A 125   NE  -  CZ  -  NH1 ANGL. DEV. =   4.1 DEGREES          
REMARK 500  1 ARG A 177   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500  1 TRP A 178   CE2 -  CD2 -  CG  ANGL. DEV. =  -4.9 DEGREES          
REMARK 500  1 ARG A 241   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500  1 ARG A 245   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500  2 TRP A  12   CE2 -  CD2 -  CG  ANGL. DEV. =  -4.8 DEGREES          
REMARK 500  2 ARG A  92   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500  2 ARG A 107   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES          
REMARK 500  2 TRP A 116   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.2 DEGREES          
REMARK 500  2 ARG A 125   NE  -  CZ  -  NH1 ANGL. DEV. =   4.3 DEGREES          
REMARK 500  2 TRP A 129   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.0 DEGREES          
REMARK 500  2 TRP A 178   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.3 DEGREES          
REMARK 500  2 ARG A 245   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500  3 TRP A  12   CE2 -  CD2 -  CG  ANGL. DEV. =  -4.9 DEGREES          
REMARK 500  3 ARG A  21   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500  3 ARG A  57   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500  3 TRP A  84   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.0 DEGREES          
REMARK 500  3 TRP A 116   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.2 DEGREES          
REMARK 500  3 ARG A 125   NE  -  CZ  -  NH1 ANGL. DEV. =   4.2 DEGREES          
REMARK 500  3 TRP A 129   CE2 -  CD2 -  CG  ANGL. DEV. =  -4.8 DEGREES          
REMARK 500  3 TRP A 178   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.0 DEGREES          
REMARK 500  3 HIS A 198   CG  -  CD2 -  NE2 ANGL. DEV. =  -8.0 DEGREES          
REMARK 500  3 ARG A 241   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500  3 ARG A 245   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500  4 ARG A  21   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500  4 TRP A  84   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.2 DEGREES          
REMARK 500  4 ARG A  98   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500  4 ARG A 107   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500  4 TRP A 116   CE2 -  CD2 -  CG  ANGL. DEV. =  -4.8 DEGREES          
REMARK 500  4 ARG A 125   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500  4 ARG A 177   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500  4 TRP A 178   CE2 -  CD2 -  CG  ANGL. DEV. =  -4.8 DEGREES          
REMARK 500  4 ARG A 245   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500  5 ARG A  21   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500  5 TYR A  23   CB  -  CG  -  CD2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500  5 ARG A  57   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500  5 ARG A  66   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500  5 ARG A  92   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500  5 ARG A  98   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500  5 ARG A 125   NE  -  CZ  -  NH1 ANGL. DEV. =   4.3 DEGREES          
REMARK 500  5 TRP A 178   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.1 DEGREES          
REMARK 500  5 ARG A 245   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500  6 TRP A  12   CE2 -  CD2 -  CG  ANGL. DEV. =  -4.9 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     153 ANGLE DEVIATIONS.                             
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  1 LEU A  24      146.11     68.63                                   
REMARK 500  1 THR A  29       47.38   -104.46                                   
REMARK 500  1 LEU A  48      137.06    -34.66                                   
REMARK 500  1 ILE A  50       95.51    -68.16                                   
REMARK 500  1 LEU A  54       81.69   -151.48                                   
REMARK 500  1 ASN A  55      -50.68   -175.63                                   
REMARK 500  1 SER A  56     -103.42    -78.01                                   
REMARK 500  1 ARG A  66      -57.06   -165.46                                   
REMARK 500  1 GLU A  74       81.03   -161.60                                   
REMARK 500  1 SER A  81      152.08     63.98                                   
REMARK 500  1 TRP A  84      100.18    -54.99                                   
REMARK 500  1 ALA A 112      -60.63    -91.05                                   
REMARK 500  1 TRP A 129       97.97   -172.76                                   
REMARK 500  1 ALA A 142       20.11    -79.21                                   
REMARK 500  1 TYR A 147      127.32     82.31                                   
REMARK 500  1 ASP A 150      -57.21     77.43                                   
REMARK 500  1 ASN A 154      150.06    -29.37                                   
REMARK 500  1 THR A 155       98.14     70.69                                   
REMARK 500  1 PRO A 162       81.22    -69.71                                   
REMARK 500  1 THR A 164      171.83     61.11                                   
REMARK 500  1 ASP A 173      107.60    -57.76                                   
REMARK 500  1 LEU A 184      -63.29   -132.70                                   
REMARK 500  1 MET A 212       39.11    -99.47                                   
REMARK 500  1 ASN A 218     -176.17     57.62                                   
REMARK 500  1 PHE A 224      140.62     71.30                                   
REMARK 500  1 SER A 244      -77.07     57.06                                   
REMARK 500  1 ARG A 245       80.32     50.92                                   
REMARK 500  2 GLN A   2       36.94   -153.81                                   
REMARK 500  2 LEU A  24      159.10     66.14                                   
REMARK 500  2 THR A  29       42.30   -100.82                                   
REMARK 500  2 ASN A  55      -54.46    166.35                                   
REMARK 500  2 SER A  56      -94.03    -85.48                                   
REMARK 500  2 ARG A  66      -58.40   -163.70                                   
REMARK 500  2 TYR A  75      170.41     60.04                                   
REMARK 500  2 SER A  76      130.57     70.90                                   
REMARK 500  2 SER A  81      151.01     61.80                                   
REMARK 500  2 GLU A 119       33.12    -93.90                                   
REMARK 500  2 LEU A 122      161.44    -47.52                                   
REMARK 500  2 TRP A 129       97.56   -165.62                                   
REMARK 500  2 ALA A 142       34.07    -80.46                                   
REMARK 500  2 TYR A 147      126.10     77.03                                   
REMARK 500  2 ASP A 150        5.04     52.01                                   
REMARK 500  2 ASN A 154      139.69    -27.20                                   
REMARK 500  2 THR A 155      120.85     75.52                                   
REMARK 500  2 PRO A 162       74.03    -67.50                                   
REMARK 500  2 ASP A 173      105.72    -57.73                                   
REMARK 500  2 ASP A 180      -63.67   -131.81                                   
REMARK 500  2 MET A 212       49.04   -100.63                                   
REMARK 500  2 THR A 215       41.56    -89.05                                   
REMARK 500  2 PHE A 224      130.90    -33.11                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     433 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500  1 TYR A 216         0.08    SIDE CHAIN                              
REMARK 500  2 TYR A  23         0.10    SIDE CHAIN                              
REMARK 500  3 TYR A 147         0.11    SIDE CHAIN                              
REMARK 500  4 PHE A 160         0.11    SIDE CHAIN                              
REMARK 500  4 TYR A 213         0.13    SIDE CHAIN                              
REMARK 500  4 TYR A 216         0.08    SIDE CHAIN                              
REMARK 500  5 TYR A  91         0.11    SIDE CHAIN                              
REMARK 500  5 TYR A 216         0.16    SIDE CHAIN                              
REMARK 500  6 TYR A 213         0.10    SIDE CHAIN                              
REMARK 500  6 TYR A 216         0.20    SIDE CHAIN                              
REMARK 500  7 TYR A 216         0.06    SIDE CHAIN                              
REMARK 500  8 TYR A 213         0.12    SIDE CHAIN                              
REMARK 500  9 TYR A  23         0.14    SIDE CHAIN                              
REMARK 500 12 TYR A  18         0.13    SIDE CHAIN                              
REMARK 500 12 TYR A  23         0.09    SIDE CHAIN                              
REMARK 500 12 TYR A 213         0.09    SIDE CHAIN                              
REMARK 500 12 TYR A 216         0.09    SIDE CHAIN                              
REMARK 500 14 TYR A 213         0.10    SIDE CHAIN                              
REMARK 500 16 TYR A 216         0.07    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610   1 SGN A  305                                                       
REMARK 610   2 SGN A  305                                                       
REMARK 610   3 SGN A  305                                                       
REMARK 610   4 SGN A  305                                                       
REMARK 610   5 SGN A  305                                                       
REMARK 610   6 SGN A  305                                                       
REMARK 610   7 SGN A  305                                                       
REMARK 610   8 SGN A  305                                                       
REMARK 610   9 SGN A  305                                                       
REMARK 610  10 SGN A  305                                                       
REMARK 610  11 SGN A  305                                                       
REMARK 610  12 SGN A  305                                                       
REMARK 610  13 SGN A  305                                                       
REMARK 610  14 SGN A  305                                                       
REMARK 610  15 SGN A  305                                                       
REMARK 610  16 SGN A  305                                                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 304  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  67   SG                                                     
REMARK 620 2 HIS A 194   NE2  79.1                                              
REMARK 620 3 HIS A 198   NE2  98.4  83.9                                        
REMARK 620 4 HIS A 204   NE2 154.3  98.3 106.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 301  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 133   O                                                      
REMARK 620 2 GLY A 165   O   104.1                                              
REMARK 620 3 LEU A 166   O   159.1  85.0                                        
REMARK 620 4 GLY A 167   O   130.3  78.6  69.5                                  
REMARK 620 5 ASP A 169   OD1  77.1 146.3  84.9 126.9                            
REMARK 620 N                    1     2     3     4                             
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 143   NE2                                                    
REMARK 620 2 ASP A 145   OD2  74.2                                              
REMARK 620 3 HIS A 158   NE2 145.3 120.2                                        
REMARK 620 4 HIS A 171   ND1  98.3 172.1  67.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 302  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 150   OD1                                                    
REMARK 620 2 ASP A 150   OD2  49.2                                              
REMARK 620 3 GLY A 151   O    59.7  73.8                                        
REMARK 620 4 GLY A 153   O    83.2 120.6 115.1                                  
REMARK 620 5 ASN A 154   O    51.5  72.6 109.9  48.6                            
REMARK 620 6 THR A 155   O    95.8  73.4 147.1  80.0  56.8                      
REMARK 620 7 ASP A 173   OD2 104.8  64.9  71.8 171.6 135.2  96.6                
REMARK 620 8 GLU A 176   OE2 127.9 175.8 102.2  59.7 108.2 110.5 115.3          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA 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 ZN A 304                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues SGN A    
REMARK 800  305 through IDS A 312                                               
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2MZE   RELATED DB: PDB                                   
REMARK 900 THE FREE STATE OF THIS ZYMOGEN PROTEASE                              
REMARK 900 RELATED ID: 5UE2   RELATED DB: PDB                                   
REMARK 900 ANOTHER COMPLEX THAT THE HEPARIN OCTASACCHARIDE FORMS WITH THIS      
REMARK 900 ZYMOGEN                                                              
REMARK 900 RELATED ID: 25485   RELATED DB: BMRB                                 
DBREF  5UE5 A    1   247  UNP    P09237   MMP7_HUMAN      21    267             
SEQADV 5UE5 ALA A  195  UNP  P09237    GLU   215 CONFLICT                       
SEQRES   1 A  247  PRO GLN GLU ALA GLY GLY MET SER GLU LEU GLN TRP GLU          
SEQRES   2 A  247  GLN ALA GLN ASP TYR LEU LYS ARG PHE TYR LEU TYR ASP          
SEQRES   3 A  247  SER GLU THR LYS ASN ALA ASN SER LEU GLU ALA LYS LEU          
SEQRES   4 A  247  LYS GLU MET GLN LYS PHE PHE GLY LEU PRO ILE THR GLY          
SEQRES   5 A  247  MET LEU ASN SER ARG VAL ILE GLU ILE MET GLN LYS PRO          
SEQRES   6 A  247  ARG CYS GLY VAL PRO ASP VAL ALA GLU TYR SER LEU PHE          
SEQRES   7 A  247  PRO ASN SER PRO LYS TRP THR SER LYS VAL VAL THR TYR          
SEQRES   8 A  247  ARG ILE VAL SER TYR THR ARG ASP LEU PRO HIS ILE THR          
SEQRES   9 A  247  VAL ASP ARG LEU VAL SER LYS ALA LEU ASN MET TRP GLY          
SEQRES  10 A  247  LYS GLU ILE PRO LEU HIS PHE ARG LYS VAL VAL TRP GLY          
SEQRES  11 A  247  THR ALA ASP ILE MET ILE GLY PHE ALA ARG GLY ALA HIS          
SEQRES  12 A  247  GLY ASP SER TYR PRO PHE ASP GLY PRO GLY ASN THR LEU          
SEQRES  13 A  247  ALA HIS ALA PHE ALA PRO GLY THR GLY LEU GLY GLY ASP          
SEQRES  14 A  247  ALA HIS PHE ASP GLU ASP GLU ARG TRP THR ASP GLY SER          
SEQRES  15 A  247  SER LEU GLY ILE ASN PHE LEU TYR ALA ALA THR HIS ALA          
SEQRES  16 A  247  LEU GLY HIS SER LEU GLY MET GLY HIS SER SER ASP PRO          
SEQRES  17 A  247  ASN ALA VAL MET TYR PRO THR TYR GLY ASN GLY ASP PRO          
SEQRES  18 A  247  GLN ASN PHE LYS LEU SER GLN ASP ASP ILE LYS GLY ILE          
SEQRES  19 A  247  GLN LYS LEU TYR GLY LYS ARG SER ASN SER ARG LYS LYS          
HET     CA  A 301       1                                                       
HET     CA  A 302       1                                                       
HET     ZN  A 303       1                                                       
HET     ZN  A 304       1                                                       
HET    SGN  A 305      28                                                       
HET    IDS  A 306      22                                                       
HET    SGN  A 307      28                                                       
HET    IDS  A 308      22                                                       
HET    SGN  A 309      28                                                       
HET    IDS  A 310      22                                                       
HET    SGN  A 311      28                                                       
HET    IDS  A 312      22                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM      ZN ZINC ION                                                         
HETNAM     SGN N,O6-DISULFO-GLUCOSAMINE                                         
HETNAM     IDS 2-O-SULFO-ALPHA-L-IDOPYRANURONIC ACID                            
HETSYN     IDS O2-SULFO-GLUCURONIC ACID                                         
FORMUL   2   CA    2(CA 2+)                                                     
FORMUL   4   ZN    2(ZN 2+)                                                     
FORMUL   6  SGN    4(C6 H13 N O11 S2)                                           
FORMUL   6  IDS    4(C6 H10 O10 S)                                              
HELIX    1 AA1 GLU A    3  MET A    7  5                                   5    
HELIX    2 AA2 SER A    8  TYR A   23  1                                  16    
HELIX    3 AA3 ASP A   26  LYS A   30  5                                   5    
HELIX    4 AA4 ASN A   33  GLY A   47  1                                  15    
HELIX    5 AA5 SER A   56  LYS A   64  1                                   9    
HELIX    6 AA6 PRO A  101  GLU A  119  1                                  19    
HELIX    7 AA7 ARG A  140  GLY A  144  5                                   5    
HELIX    8 AA8 PHE A  188  LEU A  200  1                                  13    
HELIX    9 AA9 SER A  227  GLY A  239  1                                  13    
SHEET    1 AA1 2 VAL A  88  VAL A  89  0                                        
SHEET    2 AA1 2 HIS A 123  PHE A 124  1  O  HIS A 123   N  VAL A  89           
SHEET    1 AA2 3 TYR A  91  ILE A  93  0                                        
SHEET    2 AA2 3 ILE A 134  ALA A 139  1  O  ILE A 136   N  ARG A  92           
SHEET    3 AA2 3 ALA A 170  ASP A 173  1  O  ALA A 170   N  MET A 135           
SHEET    1 AA3 2 TRP A 178  THR A 179  0                                        
SHEET    2 AA3 2 ILE A 186  ASN A 187  1  O  ILE A 186   N  THR A 179           
LINK         SG  CYS A  67                ZN    ZN A 304     1555   1555  2.50  
LINK         O   ASP A 133                CA    CA A 301     1555   1555  2.40  
LINK         NE2 HIS A 143                ZN    ZN A 303     1555   1555  2.26  
LINK         OD2 ASP A 145                ZN    ZN A 303     1555   1555  2.26  
LINK         OD1 ASP A 150                CA    CA A 302     1555   1555  2.70  
LINK         OD2 ASP A 150                CA    CA A 302     1555   1555  2.62  
LINK         O   GLY A 151                CA    CA A 302     1555   1555  2.42  
LINK         O   GLY A 153                CA    CA A 302     1555   1555  2.72  
LINK         O   ASN A 154                CA    CA A 302     1555   1555  3.17  
LINK         O   THR A 155                CA    CA A 302     1555   1555  2.42  
LINK         NE2 HIS A 158                ZN    ZN A 303     1555   1555  2.26  
LINK         O   GLY A 165                CA    CA A 301     1555   1555  2.41  
LINK         O   LEU A 166                CA    CA A 301     1555   1555  2.41  
LINK         O   GLY A 167                CA    CA A 301     1555   1555  2.59  
LINK         OD1 ASP A 169                CA    CA A 301     1555   1555  2.41  
LINK         ND1 HIS A 171                ZN    ZN A 303     1555   1555  2.46  
LINK         OD2 ASP A 173                CA    CA A 302     1555   1555  2.44  
LINK         OE2 GLU A 176                CA    CA A 302     1555   1555  2.42  
LINK         NE2 HIS A 194                ZN    ZN A 304     1555   1555  2.28  
LINK         NE2 HIS A 198                ZN    ZN A 304     1555   1555  2.24  
LINK         NE2 HIS A 204                ZN    ZN A 304     1555   1555  2.28  
LINK         O4  SGN A 305                 C1  IDS A 306     1555   1555  1.46  
LINK         O4  IDS A 306                 C1  SGN A 307     1555   1555  1.46  
LINK         O4  SGN A 307                 C1  IDS A 308     1555   1555  1.46  
LINK         O4  IDS A 308                 C1  SGN A 309     1555   1555  1.45  
LINK         O4  SGN A 309                 C1  IDS A 310     1555   1555  1.46  
LINK         O4  IDS A 310                 C1  SGN A 311     1555   1555  1.45  
LINK         O4  SGN A 311                 C1  IDS A 312     1555   1555  1.45  
SITE     1 AC1  5 ASP A 133  GLY A 165  LEU A 166  GLY A 167                    
SITE     2 AC1  5 ASP A 169                                                     
SITE     1 AC2  8 ASP A 150  GLY A 151  PRO A 152  GLY A 153                    
SITE     2 AC2  8 ASN A 154  THR A 155  ASP A 173  GLU A 176                    
SITE     1 AC3  4 HIS A 143  ASP A 145  HIS A 158  HIS A 171                    
SITE     1 AC4  4 CYS A  67  HIS A 194  HIS A 198  HIS A 204                    
SITE     1 AC5 13 TYR A  91  TYR A  96  ARG A  98  PRO A 101                    
SITE     2 AC5 13 HIS A 102  ILE A 103  ASP A 106  ARG A 107                    
SITE     3 AC5 13 SER A 110  ASN A 114  PHE A 124  ARG A 125                    
SITE     4 AC5 13 LYS A 126                                                     
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           1          
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      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
MODEL        1                                                                  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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