HEADER HYDROLASE 05-DEC-08 3FGD
TITLE DRUGSCORE FP: THERMOYLSIN IN COMPLEX WITH FRAGMENT.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THERMOLYSIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 233-548;
COMPND 5 SYNONYM: THERMOSTABLE NEUTRAL PROTEINASE;
COMPND 6 EC: 3.4.24.27
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS THERMOPROTEOLYTICUS;
SOURCE 3 ORGANISM_TAXID: 1427
KEYWDS DRUGSCORE FP, PROTEIN FRAGMENT COMPLEX, HYDROLASE, METAL-BINDING,
KEYWDS 2 METALLOPROTEASE, PROTEASE, SECRETED, ZYMOGEN
EXPDTA X-RAY DIFFRACTION
AUTHOR L.ENGLERT,A.HEINE,G.KLEBE
REVDAT 4 06-SEP-23 3FGD 1 REMARK LINK
REVDAT 3 24-JUL-19 3FGD 1 REMARK
REVDAT 2 13-JUL-11 3FGD 1 VERSN
REVDAT 1 15-DEC-09 3FGD 0
JRNL AUTH P.PFEFFER,G.NEUDERT,L.ENGLERT,T.RITSCHEL,B.BAUM,G.KLEBE
JRNL TITL DRUGSCORE FP: PROFILING PROTEIN-LIGAND INTERACTIONS USING
JRNL TITL 2 FINGERPRINT SIMPLICITY PAIRED WITH KNOWLEDGE-BASED POTENTIAL
JRNL TITL 3 FIELDS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.33 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : SHELXL-97
REMARK 3 AUTHORS : G.M.SHELDRICK
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.33
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.5
REMARK 3 CROSS-VALIDATION METHOD : FREE R
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.148
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.148
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.217
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 3627
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 72226
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : 0.135
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : 0.135
REMARK 3 FREE R VALUE (F>4SIG(F)) : 0.171
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : 2984
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 60091
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2416
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 29
REMARK 3 SOLVENT ATOMS : 288
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 2731.6
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 0.00
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 8
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 25010
REMARK 3 NUMBER OF RESTRAINTS : 31371
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.012
REMARK 3 ANGLE DISTANCES (A) : 0.027
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.027
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.071
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.071
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.032
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.004
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.029
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.085
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: NULL
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: ANISOTROPIC SCALING APPLIED BY THE
REMARK 3 METHOD OF PARKIN, MOEZZI & HOPE, J.APPL.CRYST.28(1995)53-56
REMARK 3 ANISOTROPIC REFINEMENT REDUCED FREE R (NO CUTOFF). THERE ARE
REMARK 3 FIVE DIFFERENCE MAP BLOBS ABOVE 0.6 E/A^3 LEFT WHICH COULD NOT
REMARK 3 BE REFINED AS WATER, DMSO, GLYCEROLE OR ANY OTHER MOLECULE
REMARK 3 PRESENT DURING CRYSTALLISATION.
REMARK 4
REMARK 4 3FGD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-DEC-08.
REMARK 100 THE DEPOSITION ID IS D_1000050557.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-NOV-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91841
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR KMC
REMARK 200 -2
REMARK 200 OPTICS : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 72415
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.330
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 200 DATA REDUNDANCY : 5.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 26.2800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.33
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.35
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.41500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.320
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1TMN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.92
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.12
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50MM TRIS/HCL, 50% DMSO, 1.9M CSCL, PH
REMARK 280 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 288K
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 42.89100
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 85.78200
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 64.33650
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 107.22750
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 21.44550
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 42.89100
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 85.78200
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 107.22750
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 64.33650
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 21.44550
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: 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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLN A 128 CG CD OE1 NE2
REMARK 470 GLN A 158 CG CD OE1 NE2
REMARK 470 LYS A 182 CG CD CE NZ
REMARK 470 GLN A 225 CG CD OE1 NE2
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 ASP A 16 CB - CG - OD1 ANGL. DEV. = 7.5 DEGREES
REMARK 500 TYR A 46 CB - CG - CD1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 TYR A 81 CG - CD1 - CE1 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ARG A 101 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ARG A 260 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG A 260 NE - CZ - NH2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 ASP A 261 CB - CG - OD1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ARG A 269 NH1 - CZ - NH2 ANGL. DEV. = 8.0 DEGREES
REMARK 500 ARG A 269 NE - CZ - NH1 ANGL. DEV. = -3.8 DEGREES
REMARK 500 ARG A 269 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 TYR A 274 CB - CG - CD2 ANGL. DEV. = 3.7 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 THR A 26 -56.21 66.18
REMARK 500 SER A 92 -172.45 60.60
REMARK 500 SER A 107 -165.10 63.37
REMARK 500 THR A 152 -103.25 -118.55
REMARK 500 ASN A 159 -144.60 54.76
REMARK 500 THR A 194 76.35 38.74
REMARK 500 ILE A 232 -61.44 -105.94
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 CA A 319 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 57 OD1
REMARK 620 2 ASP A 57 OD2 52.1
REMARK 620 3 ASP A 59 OD1 70.1 122.0
REMARK 620 4 GLN A 61 O 88.5 93.5 89.2
REMARK 620 5 HOH A1436 O 146.5 158.6 77.0 96.9
REMARK 620 6 HOH A1603 O 88.4 86.3 87.6 176.2 84.5
REMARK 620 7 HOH A1604 O 134.2 83.7 153.5 82.1 79.3 101.6
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 317 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 138 OD2
REMARK 620 2 GLU A 177 OE1 78.1
REMARK 620 3 GLU A 177 OE2 128.3 50.3
REMARK 620 4 ASP A 185 OD1 160.1 121.8 71.5
REMARK 620 5 GLU A 187 O 83.2 147.7 142.1 79.8
REMARK 620 6 GLU A 190 OE1 84.2 126.3 121.3 81.9 76.9
REMARK 620 7 GLU A 190 OE2 99.3 81.8 73.5 83.1 127.5 51.6
REMARK 620 8 HOH A1470 O 98.1 80.7 78.6 87.9 76.1 152.5 152.2
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 321 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 142 NE2
REMARK 620 2 HIS A 146 NE2 104.9
REMARK 620 3 GLU A 166 OE2 121.9 95.5
REMARK 620 4 BYA A 322 O3 116.2 126.4 90.7
REMARK 620 5 BYA A 322 O1 89.8 96.3 141.6 53.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 318 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 177 OE2
REMARK 620 2 ASN A 183 O 91.7
REMARK 620 3 ASP A 185 OD2 86.4 89.8
REMARK 620 4 GLU A 190 OE2 83.6 170.5 81.7
REMARK 620 5 HOH A1673 O 88.6 86.4 173.7 101.7
REMARK 620 6 HOH A1675 O 177.6 90.1 95.2 94.8 89.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 320 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR A 193 O
REMARK 620 2 THR A 194 O 77.0
REMARK 620 3 THR A 194 OG1 76.2 68.4
REMARK 620 4 ILE A 197 O 156.7 81.6 104.5
REMARK 620 5 ASP A 200 OD1 121.0 130.3 72.1 80.2
REMARK 620 6 HOH A1517 O 87.5 83.8 150.2 81.0 137.3
REMARK 620 7 HOH A1606 O 82.5 153.4 122.9 114.5 75.2 78.4
REMARK 620 N 1 2 3 4 5 6
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 317
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 318
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 319
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 320
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 321
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BYA A 322
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 323
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 324
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3F28 RELATED DB: PDB
REMARK 900 THERMOLYSIN IN COMPLEX WITH 2-[(CYCLOPROPYLCARBONYL)OXY]-3-
REMARK 900 METHYLBENZOIC ACID
REMARK 900 RELATED ID: 8TLN RELATED DB: PDB
REMARK 900 THERMOLYSIN IN COMPLEX WITH VAL-LYS
DBREF 3FGD A 1 316 UNP P00800 THER_BACTH 233 548
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 ASN 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 GLN 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 CA A 317 1
HET CA A 318 1
HET CA A 319 1
HET CA A 320 1
HET ZN A 321 1
HET BYA A 322 14
HET DMS A 323 4
HET GOL A 324 6
HETNAM CA CALCIUM ION
HETNAM ZN ZINC ION
HETNAM BYA N-(PHENYLCARBONYL)-BETA-ALANINE
HETNAM DMS DIMETHYL SULFOXIDE
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 CA 4(CA 2+)
FORMUL 6 ZN ZN 2+
FORMUL 7 BYA C10 H11 N O3
FORMUL 8 DMS C2 H6 O S
FORMUL 9 GOL C3 H8 O3
FORMUL 10 HOH *288(H2 O)
HELIX 1 1 ALA A 64 TYR A 66 5 3
HELIX 2 2 ASP A 67 ASN A 89 1 23
HELIX 3 3 PRO A 132 GLY A 135 5 4
HELIX 4 4 GLY A 136 THR A 152 1 17
HELIX 5 5 GLN A 158 ASN A 181 1 24
HELIX 6 6 ASP A 207 GLY A 212 5 6
HELIX 7 7 HIS A 216 ARG A 220 5 5
HELIX 8 8 THR A 224 VAL A 230 1 7
HELIX 9 9 ASN A 233 GLY A 247 1 15
HELIX 10 10 GLY A 259 TYR A 274 1 16
HELIX 11 11 ASN A 280 GLY A 297 1 18
HELIX 12 12 SER A 300 VAL A 313 1 14
SHEET 1 A 5 ALA A 56 ASP A 57 0
SHEET 2 A 5 TYR A 28 TYR A 29 -1 N TYR A 28 O ASP A 57
SHEET 3 A 5 GLN A 17 TYR A 24 -1 N THR A 23 O TYR A 29
SHEET 4 A 5 THR A 4 ARG A 11 -1 N THR A 4 O TYR A 24
SHEET 5 A 5 GLN A 61 PHE A 62 1 O PHE A 62 N VAL A 9
SHEET 1 B 3 GLN A 31 ASP A 32 0
SHEET 2 B 3 ILE A 39 ASP A 43 -1 O ILE A 39 N ASP A 32
SHEET 3 B 3 SER A 53 LEU A 54 -1 O SER A 53 N ASP A 43
SHEET 1 C 5 GLN A 31 ASP A 32 0
SHEET 2 C 5 ILE A 39 ASP A 43 -1 O ILE A 39 N ASP A 32
SHEET 3 C 5 ILE A 100 TYR A 106 1 O ILE A 100 N PHE A 40
SHEET 4 C 5 MET A 120 GLY A 123 1 O MET A 120 N ARG A 101
SHEET 5 C 5 ALA A 113 TRP A 115 -1 N PHE A 114 O VAL A 121
SHEET 1 D 2 GLU A 187 ILE A 188 0
SHEET 2 D 2 ARG A 203 SER A 204 -1 O ARG A 203 N ILE A 188
SHEET 1 E 2 GLY A 248 HIS A 250 0
SHEET 2 E 2 VAL A 253 VAL A 255 -1 O VAL A 255 N GLY A 248
LINK OD1 ASP A 57 CA CA A 319 1555 1555 2.59
LINK OD2 ASP A 57 CA CA A 319 1555 1555 2.38
LINK OD1 ASP A 59 CA CA A 319 1555 1555 2.40
LINK O GLN A 61 CA CA A 319 1555 1555 2.31
LINK OD2 ASP A 138 CA CA A 317 1555 1555 2.39
LINK NE2 HIS A 142 ZN ZN A 321 1555 1555 1.99
LINK NE2 HIS A 146 ZN ZN A 321 1555 1555 2.00
LINK OE2 GLU A 166 ZN ZN A 321 1555 1555 1.98
LINK OE1 GLU A 177 CA CA A 317 1555 1555 2.46
LINK OE2 GLU A 177 CA CA A 317 1555 1555 2.79
LINK OE2 GLU A 177 CA CA A 318 1555 1555 2.47
LINK O ASN A 183 CA CA A 318 1555 1555 2.32
LINK OD1 ASP A 185 CA CA A 317 1555 1555 2.47
LINK OD2 ASP A 185 CA CA A 318 1555 1555 2.35
LINK O GLU A 187 CA CA A 317 1555 1555 2.32
LINK OE1 GLU A 190 CA CA A 317 1555 1555 2.51
LINK OE2 GLU A 190 CA CA A 317 1555 1555 2.48
LINK OE2 GLU A 190 CA CA A 318 1555 1555 2.27
LINK O TYR A 193 CA CA A 320 1555 1555 2.37
LINK O THR A 194 CA CA A 320 1555 1555 2.41
LINK OG1 THR A 194 CA CA A 320 1555 1555 2.38
LINK O ILE A 197 CA CA A 320 1555 1555 2.33
LINK OD1 ASP A 200 CA CA A 320 1555 1555 2.41
LINK CA CA A 317 O HOH A1470 1555 1555 2.43
LINK CA CA A 318 O HOH A1673 1555 1555 2.30
LINK CA CA A 318 O HOH A1675 1555 1555 2.28
LINK CA CA A 319 O HOH A1436 1555 1555 2.40
LINK CA CA A 319 O HOH A1603 1555 1555 2.28
LINK CA CA A 319 O HOH A1604 1555 1555 2.43
LINK CA CA A 320 O HOH A1517 1555 1555 2.33
LINK CA CA A 320 O HOH A1606 1555 1555 2.39
LINK ZN ZN A 321 O3 BYA A 322 1555 1555 1.97
LINK ZN ZN A 321 O1 BYA A 322 1555 1555 2.63
CISPEP 1 LEU A 50 PRO A 51 0 2.74
SITE 1 AC1 6 ASP A 138 GLU A 177 ASP A 185 GLU A 187
SITE 2 AC1 6 GLU A 190 HOH A1470
SITE 1 AC2 6 GLU A 177 ASN A 183 ASP A 185 GLU A 190
SITE 2 AC2 6 HOH A1673 HOH A1675
SITE 1 AC3 6 ASP A 57 ASP A 59 GLN A 61 HOH A1436
SITE 2 AC3 6 HOH A1603 HOH A1604
SITE 1 AC4 6 TYR A 193 THR A 194 ILE A 197 ASP A 200
SITE 2 AC4 6 HOH A1517 HOH A1606
SITE 1 AC5 4 HIS A 142 HIS A 146 GLU A 166 BYA A 322
SITE 1 AC6 15 ASN A 112 ALA A 113 PHE A 130 LEU A 133
SITE 2 AC6 15 VAL A 139 HIS A 142 GLU A 143 HIS A 146
SITE 3 AC6 15 TYR A 157 GLU A 166 LEU A 202 ARG A 203
SITE 4 AC6 15 HIS A 231 ZN A 321 HOH A1676
SITE 1 AC7 8 TRP A 115 HIS A 146 ASP A 150 TYR A 157
SITE 2 AC7 8 HOH A1676 HOH A1677 HOH A1680 HOH A1683
SITE 1 AC8 11 THR A 152 GLY A 247 GLY A 248 VAL A 255
SITE 2 AC8 11 GLN A 273 LEU A 275 HOH A1432 HOH A1434
SITE 3 AC8 11 HOH A1487 HOH A1507 HOH A1632
CRYST1 92.600 92.600 128.673 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 0.010799 0.006235 0.000000 0.00000
SCALE2 0.000000 0.012470 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007772 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
