HEADER HYDROLASE 06-APR-99 1QF1
TITLE THERMOLYSIN (E.C.3.4.24.27) COMPLEXED WITH (2-SULPHANYLHEPTANOYL)-PHE-
TITLE 2 ALA. PARAMETERS FOR ZN-BIDENTATION OF MERCAPTOACYLDIPEPTIDES IN
TITLE 3 METALLOENDOPEPTIDASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (THERMOLYSIN);
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.4.24.27
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS THERMOPROTEOLYTICUS;
SOURCE 3 ORGANISM_TAXID: 1427
KEYWDS NEUTRAL ENDOPEPTIDASE, ZN METALLOPEPTIDASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.-F.GAUCHER,M.SELKTI,G.TIRABOSCHI,T.PRANGE,B.P.ROQUES,A.TOMAS,
AUTHOR 2 M.C.FOURNIE-ZALUSKI
REVDAT 6 16-AUG-23 1QF1 1 REMARK LINK
REVDAT 5 20-NOV-19 1QF1 1 JRNL
REVDAT 4 31-JAN-18 1QF1 1 JRNL
REVDAT 3 24-FEB-09 1QF1 1 VERSN
REVDAT 2 01-APR-03 1QF1 1 JRNL
REVDAT 1 29-DEC-99 1QF1 0
JRNL AUTH J.F.GAUCHER,M.SELKTI,G.TIRABOSCHI,T.PRANGE,B.P.ROQUES,
JRNL AUTH 2 A.TOMAS,M.C.FOURNIE-ZALUSKI
JRNL TITL CRYSTAL STRUCTURES OF ALPHA-MERCAPTOACYLDIPEPTIDES IN THE
JRNL TITL 2 THERMOLYSIN ACTIVE SITE: STRUCTURAL PARAMETERS FOR A ZN
JRNL TITL 3 MONODENTATION OR BIDENTATION IN METALLOENDOPEPTIDASES.
JRNL REF BIOCHEMISTRY V. 38 12569 1999
JRNL REFN ISSN 0006-2960
JRNL PMID 10504225
JRNL DOI 10.1021/BI991043Z
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.C.FOURNIE-ZALUSKI,P.CORIC,V.THERY,W.GONZALEZ,H.MEUDAL,
REMARK 1 AUTH 2 S.TURCAUD,J.B.MICHEL,B.P.ROQUES
REMARK 1 TITL DESIGN OF ORALLY ACTIVE DUAL INHIBITORS OF NEUTRAL
REMARK 1 TITL 2 ENDOPEPTIDASE AND ANGIOTENSIN-CONVERTING ENZYME WITH LONG
REMARK 1 TITL 3 DURATION OF ACTION.
REMARK 1 REF J.MED.CHEM. V. 39 2594 1996
REMARK 1 REFN ISSN 0022-2623
REMARK 1 PMID 8691458
REMARK 1 DOI 10.1021/JM950783C
REMARK 1 REFERENCE 2
REMARK 1 AUTH P.CORIC,S.TURCAUD,H.MEUDAL,B.P.ROQUES,M.C.FOURNIE-ZALUSKI
REMARK 1 TITL OPTIMAL RECOGNITION OF NEUTRAL ENDOPEPTIDASE AND
REMARK 1 TITL 2 ANGIOTENSIN-CONVERTING ENZYME ACTIVE SITES BY
REMARK 1 TITL 3 MERCAPTOACYLDIPEPTIDES AS A MEANS TO DESIGN POTENT DUAL
REMARK 1 TITL 4 INHIBITORS.
REMARK 1 REF J.MED.CHEM. V. 39 1210 1996
REMARK 1 REFN ISSN 0022-2623
REMARK 1 PMID 8632427
REMARK 1 DOI 10.1021/JM950590P
REMARK 1 REFERENCE 3
REMARK 1 AUTH D.R.HOLLAND,A.C.HAUSRATH,D.JUERS,B.W.MATTHEWS
REMARK 1 TITL STRUCTURAL ANALYSIS OF ZINC SUBSTITUTIONS IN THE ACTIVE SITE
REMARK 1 TITL 2 OF THERMOLYSIN.
REMARK 1 REF PROTEIN SCI. V. 4 1955 1995
REMARK 1 REFN ISSN 0961-8368
REMARK 1 PMID 8535232
REMARK 1 DOI 10.1002/PRO.5560041001
REMARK 1 REFERENCE 4
REMARK 1 AUTH B.W.MATTHEWS,J.N.JANSONIUS,P.M.COLMAN,B.P.SCHOENBORN,
REMARK 1 AUTH 2 D.DUPOURQUE
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 PMID 18663849
REMARK 1 DOI 10.1038/NEWBIO238037A0
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 100000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 96.3
REMARK 3 NUMBER OF REFLECTIONS : 22425
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.165
REMARK 3 FREE R VALUE : 0.224
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2323
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.09
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.40
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2687
REMARK 3 BIN R VALUE (WORKING SET) : 0.1990
REMARK 3 BIN FREE R VALUE : 0.2500
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 252
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.016
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 : 39
REMARK 3 SOLVENT ATOMS : 204
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 16.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 10.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : 0.16
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.380
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.74
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.145
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; 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 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PARHCSDX.PRO
REMARK 3 PARAMETER FILE 2 : PARAM19.ION
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE WHOLE SET OF DATA WAS USED FOR THE LAST STEPS OF REFINEMENT
REMARK 3 (ENERGY
REMARK 3 MINIMIZATION, B-REFINEMENT). CONSEQUENTLY FREE RVALUE WAS
REMARK 3 CALCULATED BEFORE
REMARK 3 THIS STEPS.
REMARK 4
REMARK 4 1QF1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-APR-99.
REMARK 100 THE DEPOSITION ID IS D_1000000791.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : JUN-97
REMARK 200 TEMPERATURE (KELVIN) : 278
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : LURE
REMARK 200 BEAMLINE : DW32
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97
REMARK 200 MONOCHROMATOR : MIRRORS
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23624
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 23.400
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.09300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.23
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.26000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: PDB ENTRY 1LNF
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 8.0
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 43.94000
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 87.88000
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 65.91000
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 109.85000
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 21.97000
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 43.94000
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 87.88000
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 109.85000
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 65.91000
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 21.97000
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 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 25 82.13 -167.65
REMARK 500 THR A 26 -55.18 78.37
REMARK 500 PHE A 62 67.74 -119.33
REMARK 500 SER A 92 -175.85 63.67
REMARK 500 SER A 107 -163.77 60.03
REMARK 500 ASN A 111 57.16 -90.71
REMARK 500 SER A 118 -33.38 -131.83
REMARK 500 THR A 152 -98.97 -119.46
REMARK 500 ASN A 159 -138.70 54.98
REMARK 500 THR A 194 79.40 36.57
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 CATALYTIC ZN
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 A 323 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 57 OD1
REMARK 620 2 ASP A 57 OD2 51.5
REMARK 620 3 ASP A 59 OD1 119.8 69.4
REMARK 620 4 GLN A 61 O 99.4 88.3 88.5
REMARK 620 5 HOH A 327 O 84.2 133.8 156.0 86.7
REMARK 620 6 HOH A 333 O 83.5 89.3 85.4 173.9 99.0
REMARK 620 7 HOH A 356 O 155.4 149.1 80.0 95.4 77.1 83.8
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 321 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 138 OD2
REMARK 620 2 GLU A 177 OE1 80.4
REMARK 620 3 GLU A 177 OE2 126.8 47.9
REMARK 620 4 ASP A 185 OD1 160.7 118.9 72.0
REMARK 620 5 GLU A 187 O 87.3 147.3 142.1 76.5
REMARK 620 6 GLU A 190 OE1 83.6 130.3 117.8 82.6 77.5
REMARK 620 7 GLU A 190 OE2 98.0 85.2 70.1 83.7 126.7 50.9
REMARK 620 8 HOH A 329 O 101.3 75.6 79.8 85.5 77.3 154.1 149.9
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 320 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 142 NE2
REMARK 620 2 HIS A 146 NE2 92.3
REMARK 620 3 GLU A 166 OE2 114.3 90.2
REMARK 620 4 TI1 A 317 SG 119.9 95.5 125.1
REMARK 620 5 TI1 A 317 O1 93.7 172.3 91.8 77.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 322 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 177 OE2
REMARK 620 2 ASN A 183 O 89.1
REMARK 620 3 ASP A 185 OD2 89.5 91.8
REMARK 620 4 GLU A 190 OE2 83.3 170.6 82.6
REMARK 620 5 HOH A 337 O 83.9 92.5 172.1 92.2
REMARK 620 6 HOH A 378 O 175.2 92.3 95.0 95.7 91.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 324 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR A 193 O
REMARK 620 2 THR A 194 O 74.9
REMARK 620 3 THR A 194 OG1 79.0 68.0
REMARK 620 4 ILE A 197 O 153.3 81.7 104.1
REMARK 620 5 ASP A 200 OD1 127.3 132.7 76.0 78.3
REMARK 620 6 HOH A 343 O 83.7 149.0 129.8 111.8 78.3
REMARK 620 7 HOH A 384 O 82.9 77.8 144.4 79.8 138.1 77.4
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: ZN
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: ZN BINDING SITE
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 320
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 321
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 322
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 323
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 324
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TI1 A 317
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 325
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 326
DBREF 1QF1 A 1 316 UNP P00800 THER_BACTH 1 316
SEQRES 1 A 316 ILE THR GLY THR SER THR VAL GLY VAL GLY ARG GLY VAL
SEQRES 2 A 316 LEU GLY ASP GLN LYS ASN ILE ASN THR THR TYR SER THR
SEQRES 3 A 316 TYR TYR TYR LEU GLN ASP ASN THR ARG GLY ASP GLY ILE
SEQRES 4 A 316 PHE THR TYR ASP ALA LYS TYR ARG THR THR LEU PRO GLY
SEQRES 5 A 316 SER LEU TRP ALA ASP ALA ASP ASN GLN PHE PHE ALA SER
SEQRES 6 A 316 TYR ASP ALA PRO ALA VAL ASP ALA HIS TYR TYR ALA GLY
SEQRES 7 A 316 VAL THR TYR ASP TYR TYR LYS ASN VAL HIS ASN ARG LEU
SEQRES 8 A 316 SER TYR ASP GLY ASN ASN ALA ALA ILE ARG SER SER VAL
SEQRES 9 A 316 HIS TYR SER GLN GLY TYR ASN ASN ALA PHE TRP ASN GLY
SEQRES 10 A 316 SER GLU MET VAL TYR GLY ASP GLY ASP GLY GLN THR PHE
SEQRES 11 A 316 ILE PRO LEU SER GLY GLY ILE ASP VAL VAL ALA HIS GLU
SEQRES 12 A 316 LEU THR HIS ALA VAL THR ASP TYR THR ALA GLY LEU ILE
SEQRES 13 A 316 TYR GLN ASN GLU SER GLY ALA ILE ASN GLU ALA ILE SER
SEQRES 14 A 316 ASP ILE PHE GLY THR LEU VAL GLU PHE TYR ALA ASN LYS
SEQRES 15 A 316 ASN PRO ASP TRP GLU ILE GLY GLU ASP VAL TYR THR PRO
SEQRES 16 A 316 GLY ILE SER GLY ASP SER LEU ARG SER MET SER ASP PRO
SEQRES 17 A 316 ALA LYS TYR GLY ASP PRO ASP HIS TYR SER LYS ARG TYR
SEQRES 18 A 316 THR GLY THR GLN ASP ASN GLY GLY VAL HIS ILE ASN SER
SEQRES 19 A 316 GLY ILE ILE ASN LYS ALA ALA TYR LEU ILE SER GLN GLY
SEQRES 20 A 316 GLY THR HIS TYR GLY VAL SER VAL VAL GLY ILE GLY ARG
SEQRES 21 A 316 ASP LYS LEU GLY LYS ILE PHE TYR ARG ALA LEU THR GLN
SEQRES 22 A 316 TYR LEU THR PRO THR SER ASN PHE SER GLN LEU ARG ALA
SEQRES 23 A 316 ALA ALA VAL GLN SER ALA THR ASP LEU TYR GLY SER THR
SEQRES 24 A 316 SER GLN GLU VAL ALA SER VAL LYS GLN ALA PHE ASP ALA
SEQRES 25 A 316 VAL GLY VAL LYS
HET ZN A 320 1
HET CA A 321 1
HET CA A 322 1
HET CA A 323 1
HET CA A 324 1
HET TI1 A 317 26
HET DMS A 325 4
HET DMS A 326 4
HETNAM ZN ZINC ION
HETNAM CA CALCIUM ION
HETNAM TI1 [2(R,S)-2-SULFANYLHEPTANOYL]-PHE-ALA
HETNAM DMS DIMETHYL SULFOXIDE
FORMUL 2 ZN ZN 2+
FORMUL 3 CA 4(CA 2+)
FORMUL 7 TI1 C19 H28 N2 O4 S
FORMUL 8 DMS 2(C2 H6 O S)
FORMUL 10 HOH *204(H2 O)
HELIX 1 1 SER A 65 HIS A 88 5 24
HELIX 2 2 LEU A 133 GLY A 135 5 3
HELIX 3 3 ILE A 137 TYR A 151 1 15
HELIX 4 4 ASN A 159 ALA A 180 1 22
HELIX 5 5 PRO A 208 TYR A 211 5 4
HELIX 6 6 TYR A 217 LYS A 219 5 3
HELIX 7 7 GLN A 225 GLY A 229 1 5
HELIX 8 8 ASN A 233 GLN A 246 5 14
HELIX 9 9 ARG A 260 GLN A 273 1 14
HELIX 10 10 PHE A 281 TYR A 296 1 16
HELIX 11 11 GLN A 301 ALA A 312 1 12
SHEET 1 A 3 THR A 4 ARG A 11 0
SHEET 2 A 3 GLN A 17 SER A 25 -1 N TYR A 24 O THR A 4
SHEET 3 A 3 TYR A 27 TYR A 29 -1 N TYR A 29 O THR A 23
SHEET 1 B 2 ILE A 39 ASP A 43 0
SHEET 2 B 2 ILE A 100 VAL A 104 1 N ILE A 100 O PHE A 40
SHEET 1 C 2 ALA A 113 TRP A 115 0
SHEET 2 C 2 MET A 120 TYR A 122 -1 N VAL A 121 O PHE A 114
SHEET 1 D 2 GLY A 248 HIS A 250 0
SHEET 2 D 2 VAL A 253 VAL A 255 -1 N VAL A 255 O GLY A 248
LINK OD1 ASP A 57 CA CA A 323 1555 1555 2.36
LINK OD2 ASP A 57 CA CA A 323 1555 1555 2.58
LINK OD1 ASP A 59 CA CA A 323 1555 1555 2.41
LINK O GLN A 61 CA CA A 323 1555 1555 2.27
LINK OD2 ASP A 138 CA CA A 321 1555 1555 2.41
LINK NE2 HIS A 142 ZN ZN A 320 1555 1555 2.06
LINK NE2 HIS A 146 ZN ZN A 320 1555 1555 2.19
LINK OE2 GLU A 166 ZN ZN A 320 1555 1555 1.96
LINK OE1 GLU A 177 CA CA A 321 1555 1555 2.41
LINK OE2 GLU A 177 CA CA A 321 1555 1555 2.85
LINK OE2 GLU A 177 CA CA A 322 1555 1555 2.34
LINK O ASN A 183 CA CA A 322 1555 1555 2.40
LINK OD1 ASP A 185 CA CA A 321 1555 1555 2.56
LINK OD2 ASP A 185 CA CA A 322 1555 1555 2.43
LINK O GLU A 187 CA CA A 321 1555 1555 2.28
LINK OE1 GLU A 190 CA CA A 321 1555 1555 2.53
LINK OE2 GLU A 190 CA CA A 321 1555 1555 2.51
LINK OE2 GLU A 190 CA CA A 322 1555 1555 2.31
LINK O TYR A 193 CA CA A 324 1555 1555 2.34
LINK O THR A 194 CA CA A 324 1555 1555 2.40
LINK OG1 THR A 194 CA CA A 324 1555 1555 2.34
LINK O ILE A 197 CA CA A 324 1555 1555 2.28
LINK OD1 ASP A 200 CA CA A 324 1555 1555 2.35
LINK SG TI1 A 317 ZN ZN A 320 1555 1555 2.29
LINK O1 TI1 A 317 ZN ZN A 320 1555 1555 2.41
LINK CA CA A 321 O HOH A 329 1555 1555 2.43
LINK CA CA A 322 O HOH A 337 1555 1555 2.41
LINK CA CA A 322 O HOH A 378 1555 1555 2.38
LINK CA CA A 323 O HOH A 327 1555 1555 2.40
LINK CA CA A 323 O HOH A 333 1555 1555 2.39
LINK CA CA A 323 O HOH A 356 1555 1555 2.42
LINK CA CA A 324 O HOH A 343 1555 1555 2.41
LINK CA CA A 324 O HOH A 384 1555 1555 2.42
CISPEP 1 LEU A 50 PRO A 51 0 -0.09
SITE 1 ZN 3 HIS A 146 HIS A 142 GLU A 166
SITE 1 AC1 4 HIS A 142 HIS A 146 GLU A 166 TI1 A 317
SITE 1 AC2 6 ASP A 138 GLU A 177 ASP A 185 GLU A 187
SITE 2 AC2 6 GLU A 190 HOH A 329
SITE 1 AC3 6 GLU A 177 ASN A 183 ASP A 185 GLU A 190
SITE 2 AC3 6 HOH A 337 HOH A 378
SITE 1 AC4 6 ASP A 57 ASP A 59 GLN A 61 HOH A 327
SITE 2 AC4 6 HOH A 333 HOH A 356
SITE 1 AC5 6 TYR A 193 THR A 194 ILE A 197 ASP A 200
SITE 2 AC5 6 HOH A 343 HOH A 384
SITE 1 AC6 18 TYR A 110 ASN A 112 ALA A 113 VAL A 139
SITE 2 AC6 18 HIS A 142 GLU A 143 HIS A 146 TYR A 157
SITE 3 AC6 18 GLU A 166 ILE A 188 GLY A 189 LEU A 202
SITE 4 AC6 18 ARG A 203 HIS A 231 ZN A 320 HOH A 413
SITE 5 AC6 18 HOH A 459 HOH A 478
SITE 1 AC7 2 TRP A 115 HIS A 146
SITE 1 AC8 2 SER A 218 TYR A 251
CRYST1 93.310 93.310 131.820 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 0.010717 0.006187 0.000000 0.00000
SCALE2 0.000000 0.012375 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007586 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
