HEADER HYDROLASE (METALLOPROTEASE) 13-MAY-94 1LNF
TITLE A STRUCTURAL ANALYSIS OF METAL SUBSTITUTIONS IN THERMOLYSIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THERMOLYSIN;
COMPND 3 CHAIN: E;
COMPND 4 EC: 3.4.24.27;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS THERMOPROTEOLYTICUS;
SOURCE 3 ORGANISM_TAXID: 1427
KEYWDS HYDROLASE (METALLOPROTEASE)
EXPDTA X-RAY DIFFRACTION
AUTHOR D.R.HOLLAND,B.W.MATTHEWS
REVDAT 9 14-FEB-24 1LNF 1 REMARK LINK
REVDAT 8 04-APR-18 1LNF 1 REMARK
REVDAT 7 29-NOV-17 1LNF 1 HELIX
REVDAT 6 18-JUL-12 1LNF 1 REMARK
REVDAT 5 13-JUN-12 1LNF 1 REMARK VERSN
REVDAT 4 25-AUG-09 1LNF 1 SOURCE
REVDAT 3 14-JUL-09 1LNF 1 REMARK
REVDAT 2 24-FEB-09 1LNF 1 VERSN
REVDAT 1 08-MAY-95 1LNF 0
JRNL AUTH D.R.HOLLAND,A.C.HAUSRATH,D.JUERS,B.W.MATTHEWS
JRNL TITL STRUCTURAL ANALYSIS OF ZINC SUBSTITUTIONS IN THE ACTIVE SITE
JRNL TITL 2 OF THERMOLYSIN.
JRNL REF PROTEIN SCI. V. 4 1955 1995
JRNL REFN ISSN 0961-8368
JRNL PMID 8535232
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH D.R.HOLLAND,D.E.TRONRUD,H.W.PLEY,K.M.FLAHERTY,W.STARK,
REMARK 1 AUTH 2 J.N.JANSONIUS,D.B.MCKAY,B.W.MATTHEWS
REMARK 1 TITL STRUCTURAL COMPARISON SUGGESTS THAT THERMOLYSIN AND RELATED
REMARK 1 TITL 2 NEUTRAL PROTEASES UNDERGO HINGE-BENDING MOTION DURING
REMARK 1 TITL 3 CATALYSIS
REMARK 1 REF BIOCHEMISTRY V. 31 11310 1992
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 2
REMARK 1 AUTH M.A.HOLMES,B.W.MATTHEWS
REMARK 1 TITL STRUCTURE OF THERMOLYSIN REFINED AT 1.6 ANGSTROMS RESOLUTION
REMARK 1 REF J.MOL.BIOL. V. 160 623 1982
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 3
REMARK 1 AUTH A.F.MONZINGO,B.W.MATTHEWS
REMARK 1 TITL STRUCTURE OF A MERCAPTAN-THERMOLYSIN COMPLEX ILLUSTRATES
REMARK 1 TITL 2 MODE OF INHIBITION OF ZINC PROTEASES BY SUBSTRATE-ANALOGUE
REMARK 1 TITL 3 MERCAPTANS
REMARK 1 REF BIOCHEMISTRY V. 21 3390 1982
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 4
REMARK 1 AUTH M.A.HOLMES,B.W.MATTHEWS
REMARK 1 TITL BINDING OF HYDROXAMIC ACID INHIBITORS TO CRYSTALLINE
REMARK 1 TITL 2 THERMOLYSIN SUGGESTS A PENTACOORDINATE ZINC INTERMEDIATE IN
REMARK 1 TITL 3 CATALYSIS
REMARK 1 REF BIOCHEMISTRY V. 20 6912 1981
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 5
REMARK 1 AUTH M.C.BOLOGNESI,B.W.MATTHEWS
REMARK 1 TITL BINDING OF THE BIPRODUCT ANALOG L-BENZYLSUCCINIC ACID TO
REMARK 1 TITL 2 THERMOLYSIN DETERMINED BY X-RAY CRYSTALLOGRAPHY
REMARK 1 REF J.BIOL.CHEM. V. 254 634 1979
REMARK 1 REFN ISSN 0021-9258
REMARK 1 REFERENCE 6
REMARK 1 AUTH W.R.KESTER,B.W.MATTHEWS
REMARK 1 TITL COMPARISON OF THE STRUCTURES OF CARBOXYPEPTIDASE A AND
REMARK 1 TITL 2 THERMOLYSIN
REMARK 1 REF J.BIOL.CHEM. V. 252 7704 1977
REMARK 1 REFN ISSN 0021-9258
REMARK 1 REFERENCE 7
REMARK 1 AUTH L.H.WEAVER,W.R.KESTER,B.W.MATTHEWS
REMARK 1 TITL A CRYSTALLOGRAPHIC STUDY OF THE COMPLEX OF PHOSPHORAMIDON
REMARK 1 TITL 2 WITH THERMOLYSIN. A MODEL FOR THE PRESUMED CATALYTIC
REMARK 1 TITL 3 TRANSITION STATE AND FOR THE BINDING OF EXTENDED SUBSTRATES
REMARK 1 REF J.MOL.BIOL. V. 114 119 1977
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 8
REMARK 1 AUTH W.R.KESTER,B.W.MATTHEWS
REMARK 1 TITL CRYSTALLOGRAPHIC STUDY OF THE BINDING OF DIPEPTIDE
REMARK 1 TITL 2 INHIBITORS TO THERMOLYSIN. IMPLICATIONS FOR THE MECHANISM OF
REMARK 1 TITL 3 CATALYSIS
REMARK 1 REF BIOCHEMISTRY V. 16 2506 1977
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 9
REMARK 1 AUTH F.W.DAHLQUIST,J.W.LONG,W.L.BIGBEE
REMARK 1 TITL ROLE OF CALCIUM IN THE THERMAL STABILITY OF THERMOLYSIN
REMARK 1 REF BIOCHEMISTRY V. 15 1103 1976
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 10
REMARK 1 EDIT M.O.DAYHOFF
REMARK 1 REF ATLAS OF PROTEIN SEQUENCE V. 5 98 1976
REMARK 1 REF 2 AND STRUCTURE (DATA SECTION)
REMARK 1 PUBL NATIONAL BIOMEDICAL RESEARCH FOUNDATION, SILVER SPRING,MD.
REMARK 1 REFN
REMARK 1 REFERENCE 11
REMARK 1 AUTH P.L.LEVY,M.K.PANGBURN,Y.BURSTEIN,L.H.ERICSSON,H.NEURATH,
REMARK 1 AUTH 2 K.A.WALSH
REMARK 1 TITL EVIDENCE OF HOMOLOGOUS RELATIONSHIP BETWEEN THERMOLYSIN AND
REMARK 1 TITL 2 NEUTRAL PROTEASE A OF BACILLUS SUBTILIS
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 72 4341 1975
REMARK 1 REFN ISSN 0027-8424
REMARK 1 REFERENCE 12
REMARK 1 AUTH B.W.MATTHEWS,L.H.WEAVER,W.R.KESTER
REMARK 1 TITL THE CONFORMATION OF THERMOLYSIN
REMARK 1 REF J.BIOL.CHEM. V. 249 8030 1974
REMARK 1 REFN ISSN 0021-9258
REMARK 1 REFERENCE 13
REMARK 1 AUTH B.W.MATTHEWS,L.H.WEAVER
REMARK 1 TITL BINDING OF LANTHANIDE IONS TO THERMOLYSIN
REMARK 1 REF BIOCHEMISTRY V. 13 1719 1974
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 14
REMARK 1 AUTH P.M.COLMAN,J.N.JANSONIUS,B.W.MATTHEWS
REMARK 1 TITL THE STRUCTURE OF THERMOLYSIN,AN ELECTRON DENSITY MAP AT 2.3
REMARK 1 TITL 2 ANGSTROMS RESOLUTION
REMARK 1 REF J.MOL.BIOL. V. 70 701 1972
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 15
REMARK 1 AUTH K.TITANI,M.A.HERMODSON,L.H.ERICSSON,K.A.WALSH,H.NEURATH
REMARK 1 TITL AMINO-ACID SEQUENCE OF THERMOLYSIN
REMARK 1 REF NATURE NEW BIOL. V. 238 35 1972
REMARK 1 REFN ISSN 0369-4887
REMARK 1 REFERENCE 16
REMARK 1 AUTH B.W.MATTHEWS,J.N.JANSONIUS,P.M.COLMAN,B.P.SCHOENBORN,
REMARK 1 AUTH 2 D.DUPORQUE
REMARK 1 TITL THREE DIMENSIONAL STRUCTURE OF THERMOLYSIN
REMARK 1 REF NATURE NEW BIOL. V. 238 37 1972
REMARK 1 REFN ISSN 0369-4887
REMARK 1 REFERENCE 17
REMARK 1 AUTH B.W.MATTHEWS,P.M.COLMAN,J.N.JANSONIUS,K.TITANI,K.A.WALSH,
REMARK 1 AUTH 2 H.NEURATH
REMARK 1 TITL STRUCTURE OF THERMOLYSIN
REMARK 1 REF NATURE NEW BIOL. V. 238 41 1972
REMARK 1 REFN ISSN 0369-4887
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : TNT
REMARK 3 AUTHORS : TRONRUD,TEN EYCK,MATTHEWS
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 36953
REMARK 3
REMARK 3 USING DATA ABOVE SIGMA CUTOFF.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : 0.152
REMARK 3 R VALUE (WORKING SET) : NULL
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 USING ALL DATA, NO SIGMA CUTOFF.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2432
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 26
REMARK 3 SOLVENT ATOMS : 159
REMARK 3
REMARK 3 WILSON B VALUE (FROM FCALC, A**2) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. RMS WEIGHT COUNT
REMARK 3 BOND LENGTHS (A) : 0.015 ; NULL ; NULL
REMARK 3 BOND ANGLES (DEGREES) : 2.000 ; NULL ; NULL
REMARK 3 TORSION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 TRIGONAL CARBON PLANES (A) : NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES (A) : NULL ; NULL ; NULL
REMARK 3 ISOTROPIC THERMAL FACTORS (A**2) : NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS (A) : NULL ; NULL ; NULL
REMARK 3
REMARK 3 INCORRECT CHIRAL-CENTERS (COUNT) : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 RESTRAINT LIBRARIES.
REMARK 3 STEREOCHEMISTRY : NULL
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1LNF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000174773.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 298.0
REMARK 200 PH : 7.2
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : MULTIWIRE AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : XUONG-HAMLIN
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XENGEN (HOWARD, NIELSEN, XUONG)
REMARK 200 DATA SCALING SOFTWARE : XENGEN (HOWARD, NIELSEN, XUONG)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE CRYSTAL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR SUBSTITUTION
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.02
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.2
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+5/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/6
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 43.80000
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 87.60000
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 65.70000
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 109.50000
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 21.90000
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 43.80000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 87.60000
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 109.50000
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 65.70000
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 21.90000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
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: 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 OE2 GLU E 143 O HOH E 906 1.99
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 GLU E 166 CD GLU E 166 OE2 -0.077
REMARK 500 GLU E 177 CD GLU E 177 OE2 0.081
REMARK 500 GLU E 187 CD GLU E 187 OE1 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 ARG E 11 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG E 11 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ASP E 16 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP E 16 CB - CG - OD2 ANGL. DEV. = -6.7 DEGREES
REMARK 500 ASP E 43 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 ASP E 59 CB - CG - OD1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ASP E 59 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 ASP E 82 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP E 82 CB - CG - OD2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 ASP E 150 CB - CG - OD2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 ASP E 185 CB - CG - OD1 ANGL. DEV. = -5.5 DEGREES
REMARK 500 ASP E 200 CB - CG - OD1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ASP E 200 CB - CG - OD2 ANGL. DEV. = -8.2 DEGREES
REMARK 500 ASP E 207 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 ASP E 215 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 ASP E 226 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ARG E 285 NE - CZ - NH1 ANGL. DEV. = 3.3 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 E 25 81.56 -159.18
REMARK 500 THR E 26 -62.37 78.24
REMARK 500 SER E 92 -171.10 61.00
REMARK 500 SER E 107 -163.05 63.00
REMARK 500 ASN E 111 53.51 -96.08
REMARK 500 THR E 152 -99.09 -114.48
REMARK 500 ASN E 159 -144.36 51.82
REMARK 500 THR E 194 73.52 37.71
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 RESIDUES 1321 AND 1322 FORM A DIPEPTIDE (VAL-LYS) BOUND IN THE
REMARK 600 ACTIVE SITE OF THE MOLECULE. IT IS PRESUMED THAT THE ORIGIN OF THIS
REMARK 600 DIPEPTIDE IS THE C-TERMINAL TWO RESIDUES OF THE PROTEIN. SINCE THE
REMARK 600 C-TERMINUS APPEARS AT FULL OCCUPANCY, MOLECULES NOT INCORPORATED
REMARK 600 INTO THE CRYSTAL MUST HAVE BEEN SACRIFICED.
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 903 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 57 OD1
REMARK 620 2 ASP E 57 OD2 52.4
REMARK 620 3 ASP E 59 OD1 118.4 66.4
REMARK 620 4 GLN E 61 O 95.9 90.8 90.9
REMARK 620 5 HOH E 910 O 155.4 149.8 83.7 94.2
REMARK 620 6 HOH E 911 O 83.6 84.0 83.9 173.8 88.6
REMARK 620 7 HOH E 966 O 81.4 132.8 160.0 84.0 77.4 102.0
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 901 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 138 OD2
REMARK 620 2 GLU E 177 OE1 74.6
REMARK 620 3 GLU E 177 OE2 123.4 49.5
REMARK 620 4 ASP E 185 OD1 159.9 125.4 76.6
REMARK 620 5 GLU E 187 O 84.5 145.3 146.9 77.1
REMARK 620 6 GLU E 190 OE1 84.3 127.6 120.1 83.3 76.0
REMARK 620 7 GLU E 190 OE2 100.3 83.4 68.7 84.9 128.2 53.6
REMARK 620 8 HOH E 925 O 100.0 79.4 80.3 84.1 77.3 152.4 148.7
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN E 800 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS E 142 NE2
REMARK 620 2 HIS E 146 NE2 105.2
REMARK 620 3 GLU E 166 OE2 138.4 85.6
REMARK 620 4 GLU E 166 OE1 85.9 120.7 55.3
REMARK 620 5 HOH E 906 O 97.6 95.4 121.7 141.6
REMARK 620 6 HOH E 907 O 125.1 123.2 74.3 90.0 56.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 902 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU E 177 OE2
REMARK 620 2 ASN E 183 O 90.0
REMARK 620 3 ASP E 185 OD2 90.5 92.9
REMARK 620 4 GLU E 190 OE2 84.1 172.5 82.5
REMARK 620 5 HOH E 905 O 84.8 91.3 173.7 92.7
REMARK 620 6 HOH E 908 O 165.7 93.8 103.1 93.1 81.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 904 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR E 193 O
REMARK 620 2 THR E 194 O 77.8
REMARK 620 3 THR E 194 OG1 79.0 68.8
REMARK 620 4 ILE E 197 O 154.1 80.6 106.3
REMARK 620 5 ASP E 200 OD1 127.5 134.7 79.5 78.3
REMARK 620 6 HOH E 909 O 82.6 78.2 144.8 79.1 134.8
REMARK 620 7 HOH E 932 O 83.7 151.4 128.7 110.0 73.8 78.0
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: ZN
REMARK 800 EVIDENCE_CODE: NULL
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VAL E 1321
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LYS E 1322
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E 903
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E 904
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS E 320
DBREF 1LNF E 1 316 UNP P00800 THER_BACTH 1 316
SEQRES 1 E 316 ILE THR GLY THR SER THR VAL GLY VAL GLY ARG GLY VAL
SEQRES 2 E 316 LEU GLY ASP GLN LYS ASN ILE ASN THR THR TYR SER THR
SEQRES 3 E 316 TYR TYR TYR LEU GLN ASP ASN THR ARG GLY ASP GLY ILE
SEQRES 4 E 316 PHE THR TYR ASP ALA LYS TYR ARG THR THR LEU PRO GLY
SEQRES 5 E 316 SER LEU TRP ALA ASP ALA ASP ASN GLN PHE PHE ALA SER
SEQRES 6 E 316 TYR ASP ALA PRO ALA VAL ASP ALA HIS TYR TYR ALA GLY
SEQRES 7 E 316 VAL THR TYR ASP TYR TYR LYS ASN VAL HIS ASN ARG LEU
SEQRES 8 E 316 SER TYR ASP GLY ASN ASN ALA ALA ILE ARG SER SER VAL
SEQRES 9 E 316 HIS TYR SER GLN GLY TYR ASN ASN ALA PHE TRP ASN GLY
SEQRES 10 E 316 SER GLU MET VAL TYR GLY ASP GLY ASP GLY GLN THR PHE
SEQRES 11 E 316 ILE PRO LEU SER GLY GLY ILE ASP VAL VAL ALA HIS GLU
SEQRES 12 E 316 LEU THR HIS ALA VAL THR ASP TYR THR ALA GLY LEU ILE
SEQRES 13 E 316 TYR GLN ASN GLU SER GLY ALA ILE ASN GLU ALA ILE SER
SEQRES 14 E 316 ASP ILE PHE GLY THR LEU VAL GLU PHE TYR ALA ASN LYS
SEQRES 15 E 316 ASN PRO ASP TRP GLU ILE GLY GLU ASP VAL TYR THR PRO
SEQRES 16 E 316 GLY ILE SER GLY ASP SER LEU ARG SER MET SER ASP PRO
SEQRES 17 E 316 ALA LYS TYR GLY ASP PRO ASP HIS TYR SER LYS ARG TYR
SEQRES 18 E 316 THR GLY THR GLN ASP ASN GLY GLY VAL HIS ILE ASN SER
SEQRES 19 E 316 GLY ILE ILE ASN LYS ALA ALA TYR LEU ILE SER GLN GLY
SEQRES 20 E 316 GLY THR HIS TYR GLY VAL SER VAL VAL GLY ILE GLY ARG
SEQRES 21 E 316 ASP LYS LEU GLY LYS ILE PHE TYR ARG ALA LEU THR GLN
SEQRES 22 E 316 TYR LEU THR PRO THR SER ASN PHE SER GLN LEU ARG ALA
SEQRES 23 E 316 ALA ALA VAL GLN SER ALA THR ASP LEU TYR GLY SER THR
SEQRES 24 E 316 SER GLN GLU VAL ALA SER VAL LYS GLN ALA PHE ASP ALA
SEQRES 25 E 316 VAL GLY VAL LYS
HET VAL E1321 7
HET LYS E1322 10
HET ZN E 800 1
HET CA E 901 1
HET CA E 902 1
HET CA E 903 1
HET CA E 904 1
HET DMS E 320 4
HETNAM VAL VALINE
HETNAM LYS LYSINE
HETNAM ZN ZINC ION
HETNAM CA CALCIUM ION
HETNAM DMS DIMETHYL SULFOXIDE
FORMUL 2 VAL C5 H11 N O2
FORMUL 3 LYS C6 H15 N2 O2 1+
FORMUL 4 ZN ZN 2+
FORMUL 5 CA 4(CA 2+)
FORMUL 9 DMS C2 H6 O S
FORMUL 10 HOH *159(H2 O)
HELIX 1 H1 SER E 65 VAL E 87 165,66 3/10 OR ALPHA-II CONFN 23
HELIX 2 H2 LEU E 133 GLY E 135 5 3
HELIX 3 H3 ILE E 137 ASP E 150 1151 IN ALPHA-II CONFORMATION 14
HELIX 4 H4 GLU E 160 ALA E 180 1180 IN 3/10 CONFORMATION 21
HELIX 5 H5 GLU E 190 VAL E 192 1192 IN 3/10 OR ALPHA-II CONFN 3
HELIX 6 H6 PRO E 208 TYR E 211 5 4
HELIX 7 H7 TYR E 217 LYS E 219 5 3
HELIX 8 H8 ASP E 226 GLY E 229 6LEFT-HAND ALPHA HELIX 4
HELIX 9 H9 ASN E 233 GLN E 246 1233,234 IN 3/10 CONFORMATION 14
HELIX 10 H10 ARG E 260 TYR E 274 1262 IN ALPHA-II CONFORMATION 15
HELIX 11 H11 PHE E 281 TYR E 296 1 16
HELIX 12 H12 GLN E 301 VAL E 313 1313 IN 3/10 CONFORMATION 13
SHEET 1 S1 5 GLN E 31 ASP E 32 0
SHEET 2 S1 5 ILE E 39 ASP E 43 -1 N ILE E 39 O ASP E 32
SHEET 3 S1 5 ILE E 100 TYR E 106 1 N SER E 102 O PHE E 40
SHEET 4 S1 5 GLU E 119 TYR E 122 1 N TYR E 122 O SER E 103
SHEET 5 S1 5 ASN E 112 TRP E 115 -1 N PHE E 114 O VAL E 121
SHEET 1 S2 5 GLY E 52 LEU E 54 0
SHEET 2 S2 5 ILE E 39 ASP E 43 -1 N ASP E 43 O SER E 53
SHEET 3 S2 5 ILE E 100 TYR E 106 1 N SER E 102 O PHE E 40
SHEET 4 S2 5 GLU E 119 TYR E 122 1 N TYR E 122 O SER E 103
SHEET 5 S2 5 ASN E 112 TRP E 115 -1 N PHE E 114 O VAL E 121
SHEET 1 S3 5 TRP E 55 ASP E 57 0
SHEET 2 S3 5 TYR E 27 TYR E 29 -1 O TYR E 28 N ASP E 57
SHEET 3 S3 5 ASP E 16 SER E 25 -1 O THR E 23 N TYR E 29
SHEET 4 S3 5 THR E 2 ARG E 11 -1 O THR E 6 N THR E 22
SHEET 5 S3 5 GLN E 61 PHE E 62 1 N PHE E 62 O VAL E 9
LINK C VAL E1321 N LYS E1322 1555 1555 1.34
LINK OD1 ASP E 57 CA CA E 903 1555 1555 2.38
LINK OD2 ASP E 57 CA CA E 903 1555 1555 2.60
LINK OD1 ASP E 59 CA CA E 903 1555 1555 2.32
LINK O GLN E 61 CA CA E 903 1555 1555 2.24
LINK OD2 ASP E 138 CA CA E 901 1555 1555 2.31
LINK NE2 HIS E 142 ZN ZN E 800 1555 1555 1.98
LINK NE2 HIS E 146 ZN ZN E 800 1555 1555 1.99
LINK OE2 GLU E 166 ZN ZN E 800 1555 1555 2.24
LINK OE1 GLU E 166 ZN ZN E 800 1555 1555 2.38
LINK OE1 GLU E 177 CA CA E 901 1555 1555 2.52
LINK OE2 GLU E 177 CA CA E 901 1555 1555 2.83
LINK OE2 GLU E 177 CA CA E 902 1555 1555 2.27
LINK O ASN E 183 CA CA E 902 1555 1555 2.42
LINK OD1 ASP E 185 CA CA E 901 1555 1555 2.41
LINK OD2 ASP E 185 CA CA E 902 1555 1555 2.23
LINK O GLU E 187 CA CA E 901 1555 1555 2.20
LINK OE1 GLU E 190 CA CA E 901 1555 1555 2.42
LINK OE2 GLU E 190 CA CA E 901 1555 1555 2.53
LINK OE2 GLU E 190 CA CA E 902 1555 1555 2.26
LINK O TYR E 193 CA CA E 904 1555 1555 2.41
LINK O THR E 194 CA CA E 904 1555 1555 2.34
LINK OG1 THR E 194 CA CA E 904 1555 1555 2.24
LINK O ILE E 197 CA CA E 904 1555 1555 2.24
LINK OD1 ASP E 200 CA CA E 904 1555 1555 2.22
LINK ZN ZN E 800 O HOH E 906 1555 1555 2.38
LINK ZN ZN E 800 O HOH E 907 1555 1555 2.28
LINK CA CA E 901 O HOH E 925 1555 1555 2.56
LINK CA CA E 902 O HOH E 905 1555 1555 2.35
LINK CA CA E 902 O HOH E 908 1555 1555 2.27
LINK CA CA E 903 O HOH E 910 1555 1555 2.35
LINK CA CA E 903 O HOH E 911 1555 1555 2.32
LINK CA CA E 903 O HOH E 966 1555 1555 2.48
LINK CA CA E 904 O HOH E 909 1555 1555 2.25
LINK CA CA E 904 O HOH E 932 1555 1555 2.43
CISPEP 1 LEU E 50 PRO E 51 0 4.21
SITE 1 ZN 5 HIS E 142 HIS E 146 GLU E 166 HOH E 906
SITE 2 ZN 5 HOH E 907
SITE 1 AC1 8 ASN E 112 ALA E 113 GLU E 143 ARG E 203
SITE 2 AC1 8 HIS E 231 HOH E 390 HOH E 906 LYS E1322
SITE 1 AC2 3 ASN E 111 ASN E 112 VAL E1321
SITE 1 AC3 6 HIS E 142 GLU E 143 HIS E 146 GLU E 166
SITE 2 AC3 6 HOH E 906 HOH E 907
SITE 1 AC4 6 ASP E 138 GLU E 177 ASP E 185 GLU E 187
SITE 2 AC4 6 GLU E 190 HOH E 925
SITE 1 AC5 6 GLU E 177 ASN E 183 ASP E 185 GLU E 190
SITE 2 AC5 6 HOH E 905 HOH E 908
SITE 1 AC6 6 ASP E 57 ASP E 59 GLN E 61 HOH E 910
SITE 2 AC6 6 HOH E 911 HOH E 966
SITE 1 AC7 6 TYR E 193 THR E 194 ILE E 197 ASP E 200
SITE 2 AC7 6 HOH E 909 HOH E 932
SITE 1 AC8 3 HIS E 216 SER E 218 TYR E 251
CRYST1 93.850 93.850 131.400 90.00 90.00 120.00 P 61 2 2 12
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 0.010655 0.006152 0.000000 0.00000
SCALE2 0.000000 0.012304 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007610 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
