HEADER HYDROLASE 28-APR-99 1CK7
TITLE GELATINASE A (FULL-LENGTH)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (GELATINASE A);
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: FULL-LENGTH;
COMPND 5 SYNONYM: MMP-2,72KD TYPE IV COLLAGENASE;
COMPND 6 EC: 3.4.24.24;
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 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HIGH 5;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: VIRUS;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: BACULOVIRUS;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PVL1393;
SOURCE 12 EXPRESSION_SYSTEM_GENE: CLG4
KEYWDS HYDROLASE (METALLOPROTEASE), FULL-LENGTH, METALLOPROTEINASE,
KEYWDS 2 GELATINASE A, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.MORGUNOVA,A.TUUTTILA,U.BERGMANN,M.ISUPOV,Y.LINDQVIST,G.SCHNEIDER,
AUTHOR 2 K.TRYGGVASON
REVDAT 6 09-AUG-23 1CK7 1 REMARK
REVDAT 5 03-NOV-21 1CK7 1 REMARK SEQADV LINK
REVDAT 4 11-APR-18 1CK7 1 REMARK
REVDAT 3 04-APR-18 1CK7 1 REMARK
REVDAT 2 24-FEB-09 1CK7 1 VERSN
REVDAT 1 25-AUG-99 1CK7 0
JRNL AUTH E.MORGUNOVA,A.TUUTTILA,U.BERGMANN,M.ISUPOV,Y.LINDQVIST,
JRNL AUTH 2 G.SCHNEIDER,K.TRYGGVASON
JRNL TITL STRUCTURE OF HUMAN PRO-MATRIX METALLOPROTEINASE-2:
JRNL TITL 2 ACTIVATION MECHANISM REVEALED.
JRNL REF SCIENCE V. 284 1667 1999
JRNL REFN ISSN 0036-8075
JRNL PMID 10356396
JRNL DOI 10.1126/SCIENCE.284.5420.1667
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 30959
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 + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.286
REMARK 3 FREE R VALUE : 0.327
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1660
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4930
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 17
REMARK 3 SOLVENT ATOMS : 104
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 105.0
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 63.50
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.012 ; NULL
REMARK 3 ANGLE DISTANCE (A) : 0.024 ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.700 ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 NO ELECTRON DENSITY WAS OBSERVED FOR THE N-TERMINAL RESIDUE
REMARK 3 ALA 30 AND FOR RESIDUES ASP 450 - THR 460. PRESUMABLY THEY
REMARK 3 ARE DISORDERED. THESE RESIDUES ARE PART OF A FLEXIBLE
REMARK 3 LINKAGE BETWEEN CATALYTIC CORE AND C-TERMINAL HEMOPEXIN
REMARK 3 PARTS OF MMP-2.
REMARK 3
REMARK 3 RESIDUES 108 - 116 WERE MODELED INTO POOR ELECTRON DENSITY.
REMARK 3 THE SIDE CHAIN ORIENTATIONS WERE TAKEN FROM THE ROTAMER
REMARK 3 LIBRARY. THESE RESIDUES ARE IN THE LOOP WHICH CONECTS
REMARK 3 PROPEPTIDE AND CATALYTIC DOMAIN.
REMARK 3
REMARK 3 THE ELECTRON DENSITY FOR THE SURFACE LOOP 649 - 652 IS
REMARK 3 WEAK, AND THE INDIVIDUAL B-FACTORS ARE RATHER HIGH.
REMARK 4
REMARK 4 1CK7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-MAY-99.
REMARK 100 THE DEPOSITION ID IS D_1000000963.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : OCT-97
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.8
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM02
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97984
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS, SCALA, CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32057
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 34.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 10.20
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.11700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.98
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.4
REMARK 200 DATA REDUNDANCY IN SHELL : 10.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.40300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1GEN, PDB ENTRY 1FBL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 72.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.49
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.8
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 3555 -Y,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X,Z+3/4
REMARK 290 5555 -X+1/2,Y,-Z+3/4
REMARK 290 6555 X,-Y+1/2,-Z+1/4
REMARK 290 7555 Y+1/2,X+1/2,-Z+1/2
REMARK 290 8555 -Y,-X,-Z
REMARK 290 9555 X+1/2,Y+1/2,Z+1/2
REMARK 290 10555 -X,-Y,Z
REMARK 290 11555 -Y+1/2,X,Z+3/4
REMARK 290 12555 Y,-X+1/2,Z+1/4
REMARK 290 13555 -X,Y+1/2,-Z+1/4
REMARK 290 14555 X+1/2,-Y,-Z+3/4
REMARK 290 15555 Y,X,-Z
REMARK 290 16555 -Y+1/2,-X+1/2,-Z+1/2
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 60.66000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 60.66000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 172.55500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 60.66000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 86.27750
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 60.66000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 258.83250
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 60.66000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 258.83250
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 60.66000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 86.27750
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 60.66000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 60.66000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 172.55500
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 60.66000
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 60.66000
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 172.55500
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 60.66000
REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 258.83250
REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 60.66000
REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 86.27750
REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 60.66000
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 86.27750
REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 60.66000
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 258.83250
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 60.66000
REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 60.66000
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 172.55500
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 30
REMARK 465 ASP A 450
REMARK 465 ILE A 451
REMARK 465 ASP A 452
REMARK 465 LEU A 453
REMARK 465 GLY A 454
REMARK 465 THR A 455
REMARK 465 GLY A 456
REMARK 465 PRO A 457
REMARK 465 THR A 458
REMARK 465 PRO A 459
REMARK 465 THR A 460
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OH TYR A 591 O HOH A 1016 1.99
REMARK 500 O ALA A 635 O HOH A 1094 2.06
REMARK 500 NE2 GLN A 149 O HOH A 1014 2.14
REMARK 500 NZ LYS A 531 OE2 GLU A 549 2.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 ND2 ASN A 240 ND2 ASN A 240 10675 1.61
REMARK 500
REMARK 500 REMARK: NULL
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 CYS A 660 C CYS A 660 OXT 1.565
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 CYS A 60 CB - CA - C ANGL. DEV. = 9.7 DEGREES
REMARK 500 CYS A 60 CA - CB - SG ANGL. DEV. = 15.2 DEGREES
REMARK 500 ASP A 134 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ARG A 175 NE - CZ - NH2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 TYR A 182 N - CA - CB ANGL. DEV. = -11.9 DEGREES
REMARK 500 PHE A 184 CB - CG - CD2 ANGL. DEV. = 4.4 DEGREES
REMARK 500 ASP A 185 CB - CG - OD1 ANGL. DEV. = 6.5 DEGREES
REMARK 500 GLY A 186 O - C - N ANGL. DEV. = -10.7 DEGREES
REMARK 500 HIS A 193 CA - CB - CG ANGL. DEV. = 10.8 DEGREES
REMARK 500 ARG A 222 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 ARG A 222 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ASP A 229 O - C - N ANGL. DEV. = -11.3 DEGREES
REMARK 500 CYS A 233 CA - CB - SG ANGL. DEV. = 8.6 DEGREES
REMARK 500 GLY A 241 C - N - CA ANGL. DEV. = -12.8 DEGREES
REMARK 500 CYS A 247 CA - CB - SG ANGL. DEV. = 6.6 DEGREES
REMARK 500 ARG A 252 NH1 - CZ - NH2 ANGL. DEV. = 6.7 DEGREES
REMARK 500 ARG A 252 NE - CZ - NH2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 GLN A 298 C - N - CA ANGL. DEV. = -16.4 DEGREES
REMARK 500 ARG A 315 CA - CB - CG ANGL. DEV. = 13.4 DEGREES
REMARK 500 ASP A 383 CB - CG - OD2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 ARG A 385 CD - NE - CZ ANGL. DEV. = 10.7 DEGREES
REMARK 500 TYR A 524 CA - CB - CG ANGL. DEV. = 19.1 DEGREES
REMARK 500 TRP A 589 CA - CB - CG ANGL. DEV. = 12.3 DEGREES
REMARK 500 GLU A 641 N - CA - CB ANGL. DEV. = 15.1 DEGREES
REMARK 500 CYS A 660 C - N - CA ANGL. DEV. = 26.6 DEGREES
REMARK 500 CYS A 660 CA - CB - SG ANGL. DEV. = 12.9 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 SER A 32 99.28 174.02
REMARK 500 GLN A 91 -28.01 -38.99
REMARK 500 ALA A 108 98.30 69.91
REMARK 500 TYR A 110 49.97 -144.34
REMARK 500 ASN A 111 61.08 -119.74
REMARK 500 LYS A 118 113.78 -166.66
REMARK 500 TRP A 119 131.03 -32.91
REMARK 500 ARG A 175 -162.08 -111.34
REMARK 500 TRP A 176 -76.63 -39.99
REMARK 500 ASP A 188 -160.45 61.75
REMARK 500 PHE A 297 -67.50 -102.58
REMARK 500 GLN A 298 -55.67 -130.55
REMARK 500 ASP A 392 -165.48 -105.85
REMARK 500 LYS A 439 -71.64 -47.47
REMARK 500 TYR A 445 -169.75 -129.80
REMARK 500 SER A 448 150.35 155.99
REMARK 500 ILE A 481 -120.83 -115.53
REMARK 500 LYS A 489 -141.71 -145.62
REMARK 500 ASP A 490 -96.82 -62.66
REMARK 500 SER A 546 -2.49 82.57
REMARK 500 PHE A 572 159.56 161.25
REMARK 500 LYS A 639 -167.82 -102.94
REMARK 500 LEU A 640 140.04 -173.53
REMARK 500 SER A 647 103.14 -52.81
REMARK 500 LYS A 649 133.14 -175.37
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 ASP A 185 10.60
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 990 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 102 SG
REMARK 620 2 HIS A 403 NE2 104.3
REMARK 620 3 HIS A 407 NE2 114.1 106.5
REMARK 620 4 HIS A 413 NE2 109.4 112.4 110.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 993 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 166 OE1
REMARK 620 2 ALA A 167 O 60.4
REMARK 620 3 ASP A 168 O 129.4 69.2
REMARK 620 4 GLY A 200 O 96.9 157.3 133.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 991 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 178 NE2
REMARK 620 2 ASP A 180 OD2 118.0
REMARK 620 3 HIS A 193 NE2 80.9 127.2
REMARK 620 4 HIS A 206 ND1 104.3 89.6 135.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 992 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 185 O
REMARK 620 2 GLY A 186 O 55.5
REMARK 620 3 ASP A 188 O 95.0 82.4
REMARK 620 4 LEU A 190 O 128.7 171.7 89.9
REMARK 620 5 ASP A 208 OD2 85.3 89.5 169.9 97.8
REMARK 620 6 GLU A 211 OE2 135.3 81.8 63.9 92.1 109.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 994 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 476 O
REMARK 620 2 ASP A 521 O 81.7
REMARK 620 3 ASP A 569 O 147.8 82.9
REMARK 620 4 ASP A 618 O 105.9 124.4 61.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 996 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ILE A 478 O
REMARK 620 2 VAL A 523 O 128.4
REMARK 620 3 ALA A 571 O 141.2 85.2
REMARK 620 4 VAL A 620 O 77.4 154.2 71.1
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: ZNA
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: ZN 990 ACTIVE SITE
REMARK 800
REMARK 800 SITE_IDENTIFIER: ZNS
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: ZN 991 STRUCTURAL SITE
REMARK 800
REMARK 800 SITE_IDENTIFIER: CAA
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: CA 992 CATALYTIC DOMAIN
REMARK 800
REMARK 800 SITE_IDENTIFIER: CAB
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: CA 993 CATALYTIC DOMAIN
REMARK 800
REMARK 800 SITE_IDENTIFIER: CAH
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: CA 994 HEMOPEXIN DOMAIN
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 990
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 991
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 992
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 993
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 994
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 995
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 996
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 777
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 778
DBREF 1CK7 A 30 660 UNP P08253 MMP2_HUMAN 30 660
SEQADV 1CK7 ALA A 404 UNP P08253 GLU 404 ENGINEERED MUTATION
SEQRES 1 A 631 ALA PRO SER PRO ILE ILE LYS PHE PRO GLY ASP VAL ALA
SEQRES 2 A 631 PRO LYS THR ASP LYS GLU LEU ALA VAL GLN TYR LEU ASN
SEQRES 3 A 631 THR PHE TYR GLY CYS PRO LYS GLU SER CYS ASN LEU PHE
SEQRES 4 A 631 VAL LEU LYS ASP THR LEU LYS LYS MET GLN LYS PHE PHE
SEQRES 5 A 631 GLY LEU PRO GLN THR GLY ASP LEU ASP GLN ASN THR ILE
SEQRES 6 A 631 GLU THR MET ARG LYS PRO ARG CYS GLY ASN PRO ASP VAL
SEQRES 7 A 631 ALA ASN TYR ASN PHE PHE PRO ARG LYS PRO LYS TRP ASP
SEQRES 8 A 631 LYS ASN GLN ILE THR TYR ARG ILE ILE GLY TYR THR PRO
SEQRES 9 A 631 ASP LEU ASP PRO GLU THR VAL ASP ASP ALA PHE ALA ARG
SEQRES 10 A 631 ALA PHE GLN VAL TRP SER ASP VAL THR PRO LEU ARG PHE
SEQRES 11 A 631 SER ARG ILE HIS ASP GLY GLU ALA ASP ILE MET ILE ASN
SEQRES 12 A 631 PHE GLY ARG TRP GLU HIS GLY ASP GLY TYR PRO PHE ASP
SEQRES 13 A 631 GLY LYS ASP GLY LEU LEU ALA HIS ALA PHE ALA PRO GLY
SEQRES 14 A 631 THR GLY VAL GLY GLY ASP SER HIS PHE ASP ASP ASP GLU
SEQRES 15 A 631 LEU TRP THR LEU GLY GLU GLY GLN VAL VAL ARG VAL LYS
SEQRES 16 A 631 TYR GLY ASN ALA ASP GLY GLU TYR CYS LYS PHE PRO PHE
SEQRES 17 A 631 LEU PHE ASN GLY LYS GLU TYR ASN SER CYS THR ASP THR
SEQRES 18 A 631 GLY ARG SER ASP GLY PHE LEU TRP CYS SER THR THR TYR
SEQRES 19 A 631 ASN PHE GLU LYS ASP GLY LYS TYR GLY PHE CYS PRO HIS
SEQRES 20 A 631 GLU ALA LEU PHE THR MET GLY GLY ASN ALA GLU GLY GLN
SEQRES 21 A 631 PRO CYS LYS PHE PRO PHE ARG PHE GLN GLY THR SER TYR
SEQRES 22 A 631 ASP SER CYS THR THR GLU GLY ARG THR ASP GLY TYR ARG
SEQRES 23 A 631 TRP CYS GLY THR THR GLU ASP TYR ASP ARG ASP LYS LYS
SEQRES 24 A 631 TYR GLY PHE CYS PRO GLU THR ALA MET SER THR VAL GLY
SEQRES 25 A 631 GLY ASN SER GLU GLY ALA PRO CYS VAL PHE PRO PHE THR
SEQRES 26 A 631 PHE LEU GLY ASN LYS TYR GLU SER CYS THR SER ALA GLY
SEQRES 27 A 631 ARG SER ASP GLY LYS MET TRP CYS ALA THR THR ALA ASN
SEQRES 28 A 631 TYR ASP ASP ASP ARG LYS TRP GLY PHE CYS PRO ASP GLN
SEQRES 29 A 631 GLY TYR SER LEU PHE LEU VAL ALA ALA HIS ALA PHE GLY
SEQRES 30 A 631 HIS ALA MET GLY LEU GLU HIS SER GLN ASP PRO GLY ALA
SEQRES 31 A 631 LEU MET ALA PRO ILE TYR THR TYR THR LYS ASN PHE ARG
SEQRES 32 A 631 LEU SER GLN ASP ASP ILE LYS GLY ILE GLN GLU LEU TYR
SEQRES 33 A 631 GLY ALA SER PRO ASP ILE ASP LEU GLY THR GLY PRO THR
SEQRES 34 A 631 PRO THR LEU GLY PRO VAL THR PRO GLU ILE CYS LYS GLN
SEQRES 35 A 631 ASP ILE VAL PHE ASP GLY ILE ALA GLN ILE ARG GLY GLU
SEQRES 36 A 631 ILE PHE PHE PHE LYS ASP ARG PHE ILE TRP ARG THR VAL
SEQRES 37 A 631 THR PRO ARG ASP LYS PRO MET GLY PRO LEU LEU VAL ALA
SEQRES 38 A 631 THR PHE TRP PRO GLU LEU PRO GLU LYS ILE ASP ALA VAL
SEQRES 39 A 631 TYR GLU ALA PRO GLN GLU GLU LYS ALA VAL PHE PHE ALA
SEQRES 40 A 631 GLY ASN GLU TYR TRP ILE TYR SER ALA SER THR LEU GLU
SEQRES 41 A 631 ARG GLY TYR PRO LYS PRO LEU THR SER LEU GLY LEU PRO
SEQRES 42 A 631 PRO ASP VAL GLN ARG VAL ASP ALA ALA PHE ASN TRP SER
SEQRES 43 A 631 LYS ASN LYS LYS THR TYR ILE PHE ALA GLY ASP LYS PHE
SEQRES 44 A 631 TRP ARG TYR ASN GLU VAL LYS LYS LYS MET ASP PRO GLY
SEQRES 45 A 631 PHE PRO LYS LEU ILE ALA ASP ALA TRP ASN ALA ILE PRO
SEQRES 46 A 631 ASP ASN LEU ASP ALA VAL VAL ASP LEU GLN GLY GLY GLY
SEQRES 47 A 631 HIS SER TYR PHE PHE LYS GLY ALA TYR TYR LEU LYS LEU
SEQRES 48 A 631 GLU ASN GLN SER LEU LYS SER VAL LYS PHE GLY SER ILE
SEQRES 49 A 631 LYS SER ASP TRP LEU GLY CYS
HET ZN A 990 1
HET ZN A 991 1
HET CA A 992 1
HET CA A 993 1
HET CA A 994 1
HET CL A 995 1
HET NA A 996 1
HET SO4 A 777 5
HET SO4 A 778 5
HETNAM ZN ZINC ION
HETNAM CA CALCIUM ION
HETNAM CL CHLORIDE ION
HETNAM NA SODIUM ION
HETNAM SO4 SULFATE ION
FORMUL 2 ZN 2(ZN 2+)
FORMUL 4 CA 3(CA 2+)
FORMUL 7 CL CL 1-
FORMUL 8 NA NA 1+
FORMUL 9 SO4 2(O4 S 2-)
FORMUL 11 HOH *104(H2 O)
HELIX 1 H1 THR A 45 TYR A 58 1 14
HELIX 2 H2 LEU A 67 PHE A 81 1 15
HELIX 3 H3 GLN A 91 THR A 96 1 6
HELIX 4 H4 PRO A 137 SER A 152 1 16
HELIX 5 H5 PHE A 265 ASP A 268 1 4
HELIX 6 H6 TYR A 323 ASP A 326 1 4
HELIX 7 H7 ASN A 380 ASP A 384 1 5
HELIX 8 H8 LEU A 397 MET A 409 1 13
HELIX 9 H10 ALA A 510 PHE A 512 5 3
HELIX 10 H11 THR A 557 LEU A 559 5 3
HELIX 11 H12 ILE A 653 ASP A 656 1 4
SHEET 1 S1 1 GLN A 123 ILE A 128 0
SHEET 1 S2 1 ARG A 158 ILE A 162 0
SHEET 1 S3 1 ILE A 169 GLY A 174 0
SHEET 1 S4 1 LEU A 191 PHE A 195 0
SHEET 1 S5 1 ASP A 204 ASP A 209 0
SHEET 1 S6 1 LEU A 212 THR A 214 0
SHEET 1 S7 1 PHE A 237 PHE A 239 0
SHEET 1 S8 1 LYS A 242 TYR A 244 0
SHEET 1 S9 1 LEU A 257 SER A 260 0
SHEET 1 S10 1 LYS A 270 CYS A 274 0
SHEET 1 S11 1 PHE A 295 PHE A 297 0
SHEET 1 S12 1 THR A 300 TYR A 302 0
SHEET 1 S13 1 ARG A 315 GLY A 318 0
SHEET 1 S14 1 LYS A 328 CYS A 332 0
SHEET 1 S15 1 PHE A 353 GLY A 357 0
SHEET 1 S16 1 ASN A 358 TYR A 360 0
SHEET 1 S17 1 MET A 373 ALA A 376 0
SHEET 1 S18 1 LYS A 386 CYS A 390 0
SHEET 1 S19 1 GLY A 477 ILE A 481 0
SHEET 1 S20 1 GLU A 484 LYS A 489 0
SHEET 1 S21 1 PHE A 492 THR A 496 0
SHEET 1 S22 1 MET A 504 VAL A 509 0
SHEET 1 S23 1 TYR A 524 ALA A 526 0
SHEET 1 S24 1 LYS A 531 ALA A 536 0
SHEET 1 S25 1 ASN A 538 SER A 544 0
SHEET 1 S26 1 THR A 547 GLU A 549 0
SHEET 1 S27 1 LYS A 554 PRO A 555 0
SHEET 1 S28 1 LYS A 578 ALA A 584 0
SHEET 1 S29 1 ASP A 586 GLU A 593 0
SHEET 1 S30 1 LYS A 597 ASP A 599 0
SHEET 1 S31 1 LYS A 604 LEU A 605 0
SHEET 1 S32 1 ALA A 619 VAL A 621 0
SHEET 1 S33 1 TYR A 630 LYS A 633 0
SHEET 1 S34 1 TYR A 636 LEU A 638 0
SSBOND 1 CYS A 60 CYS A 65 1555 1555 2.78
SSBOND 2 CYS A 291 CYS A 317 1555 1555 2.22
SSBOND 3 CYS A 305 CYS A 332 1555 1555 2.29
SSBOND 4 CYS A 349 CYS A 375 1555 1555 2.19
SSBOND 5 CYS A 363 CYS A 390 1555 1555 2.39
SSBOND 6 CYS A 469 CYS A 660 1555 1555 2.58
LINK SG CYS A 102 ZN ZN A 990 1555 1555 2.50
LINK OE1 GLU A 166 CA CA A 993 1555 1555 3.22
LINK O ALA A 167 CA CA A 993 1555 1555 2.89
LINK O ASP A 168 CA CA A 993 1555 1555 2.90
LINK NE2 HIS A 178 ZN ZN A 991 1555 1555 2.16
LINK OD2 ASP A 180 ZN ZN A 991 1555 1555 2.26
LINK O ASP A 185 CA CA A 992 1555 1555 2.85
LINK O GLY A 186 CA CA A 992 1555 1555 2.41
LINK O ASP A 188 CA CA A 992 1555 1555 2.58
LINK O LEU A 190 CA CA A 992 1555 1555 2.47
LINK NE2 HIS A 193 ZN ZN A 991 1555 1555 2.08
LINK O GLY A 200 CA CA A 993 1555 1555 2.69
LINK ND1 HIS A 206 ZN ZN A 991 1555 1555 2.06
LINK OD2 ASP A 208 CA CA A 992 1555 1555 2.58
LINK OE2 GLU A 211 CA CA A 992 1555 1555 2.75
LINK NE2 HIS A 403 ZN ZN A 990 1555 1555 2.25
LINK NE2 HIS A 407 ZN ZN A 990 1555 1555 2.24
LINK NE2 HIS A 413 ZN ZN A 990 1555 1555 2.49
LINK O ASP A 476 CA CA A 994 1555 1555 2.54
LINK O ILE A 478 NA NA A 996 1555 1555 2.71
LINK O ASP A 521 CA CA A 994 1555 1555 2.78
LINK O VAL A 523 NA NA A 996 1555 1555 2.90
LINK O ASP A 569 CA CA A 994 1555 1555 2.68
LINK O ALA A 571 NA NA A 996 1555 1555 2.79
LINK O ASP A 618 CA CA A 994 1555 1555 2.72
LINK O VAL A 620 NA NA A 996 1555 1555 2.92
CISPEP 1 PHE A 235 PRO A 236 0 -2.55
CISPEP 2 PHE A 293 PRO A 294 0 -15.46
CISPEP 3 PHE A 351 PRO A 352 0 -2.41
CISPEP 4 GLY A 505 PRO A 506 0 7.23
CISPEP 5 TYR A 552 PRO A 553 0 6.80
CISPEP 6 PHE A 602 PRO A 603 0 9.20
SITE 1 ZNA 4 CYS A 102 HIS A 403 HIS A 407 HIS A 413
SITE 1 ZNS 4 ASP A 180 HIS A 178 HIS A 193 HIS A 206
SITE 1 CAA 6 ASP A 185 GLY A 186 ASP A 188 LEU A 190
SITE 2 CAA 6 ASP A 208 GLU A 211
SITE 1 CAB 6 GLU A 166 ALA A 167 ASP A 168 GLY A 200
SITE 2 CAB 6 GLY A 202 ASP A 204
SITE 1 CAH 4 ASP A 476 ASP A 521 ASP A 569 ASP A 618
SITE 1 AC1 4 CYS A 102 HIS A 403 HIS A 407 HIS A 413
SITE 1 AC2 4 HIS A 178 ASP A 180 HIS A 193 HIS A 206
SITE 1 AC3 6 ASP A 185 GLY A 186 ASP A 188 LEU A 190
SITE 2 AC3 6 ASP A 208 GLU A 211
SITE 1 AC4 6 GLU A 166 ALA A 167 ASP A 168 GLY A 200
SITE 2 AC4 6 GLY A 202 ASP A 204
SITE 1 AC5 4 ASP A 476 ASP A 521 ASP A 569 ASP A 618
SITE 1 AC6 4 ALA A 522 VAL A 523 ALA A 571 NA A 996
SITE 1 AC7 6 ILE A 478 ALA A 479 VAL A 523 ALA A 571
SITE 2 AC7 6 VAL A 620 CL A 995
SITE 1 AC8 7 GLN A 52 TYR A 53 THR A 56 PHE A 57
SITE 2 AC8 7 ASP A 185 LEU A 190 HOH A1097
SITE 1 AC9 4 GLN A 298 GLY A 299 THR A 300 THR A 307
CRYST1 121.320 121.320 345.110 90.00 90.00 90.00 I 41 2 2 16
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 0.008243 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008243 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002898 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
