HEADER HYDROLASE 28-JAN-99 2TLX
TITLE THERMOLYSIN (NATIVE)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THERMOLYSIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: HYDROLASE (METALLOPROTEASE);
COMPND 5 EC: 3.4.24.27
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS THERMOPROTEOLYTICUS;
SOURCE 3 ORGANISM_TAXID: 1427
KEYWDS HYDROLASE, METALLOPROTEINASE, ORGANIC SOLVENT
EXPDTA X-RAY DIFFRACTION
AUTHOR A.C.ENGLISH,S.H.DONE,C.R.GROOM,R.E.HUBBARD
REVDAT 4 30-AUG-23 2TLX 1 REMARK LINK
REVDAT 3 24-FEB-09 2TLX 1 VERSN
REVDAT 2 01-APR-03 2TLX 1 JRNL
REVDAT 1 13-MAR-00 2TLX 0
JRNL AUTH A.C.ENGLISH,S.H.DONE,L.S.CAVES,C.R.GROOM,R.E.HUBBARD
JRNL TITL LOCATING INTERACTION SITES ON PROTEINS: THE CRYSTAL
JRNL TITL 2 STRUCTURE OF THERMOLYSIN SOAKED IN 2% TO 100% ISOPROPANOL.
JRNL REF PROTEINS V. 37 628 1999
JRNL REFN ISSN 0887-3585
JRNL PMID 10651278
JRNL DOI 10.1002/(SICI)1097-0134(19991201)37:4<628::AID-PROT13>3.3.CO
JRNL DOI 2 ;2-7
REMARK 1
REMARK 1 REFERENCE 1
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 REFERENCE 2
REMARK 1 AUTH M.A.HOLMES,B.W.MATTHEWS
REMARK 1 TITL STRUCTURE OF THERMOLYSIN REFINED AT 1.6 ANGSTROM RESOLUTION
REMARK 1 REF J.MOL.BIOL. V. 4 623 1982
REMARK 1 REFN ISSN 0022-2836
REMARK 2
REMARK 2 RESOLUTION. 1.65 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) : 1.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 39760
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.163
REMARK 3 FREE R VALUE : 0.187
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 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 : 207
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.10
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): 0.080
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.080
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.050
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.500
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.016 ; 0.020
REMARK 3 ANGLE DISTANCE (A) : 0.030 ; 0.040
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.036 ; 0.050
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) : 0.141 ; 0.150
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : 0.173 ; 0.300
REMARK 3 MULTIPLE TORSION (A) : 0.358 ; 0.300
REMARK 3 H-BOND (X...Y) (A) : 0.102 ; 0.300
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : 0.000 ; 15.000
REMARK 3 PLANAR (DEGREES) : 4.300 ; 7.000
REMARK 3 STAGGERED (DEGREES) : 15.300; 15.000
REMARK 3 TRANSVERSE (DEGREES) : 22.400; 20.000
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 2.162 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.723 ; 5.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 4.430 ; 5.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 6.149 ; 10.000
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THIS ENTRY FORMS PART OF A SERIES OF STRUCTURES GENERATED
REMARK 3 FROM SOAKING CRYSTALS OF THERMOLYSIN IN ORGANIC SOLVENTS/
REMARK 3 SOLUTES.
REMARK 3
REMARK 3 THE CONDITIONS USED TO CRYSTALLIZE THERMOLYSIN WERE
REMARK 3 DIFFERENT TO THOSE OF HOLMES AND MATTHEWS (1982), HENCE IT
REMARK 3 WAS NECESSARY TO RE-REFINE THE NATIVE STRUCTURE.
REMARK 4
REMARK 4 2TLX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-FEB-99.
REMARK 100 THE DEPOSITION ID IS D_1000000407.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JUL-98
REMARK 200 TEMPERATURE (KELVIN) : 293
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SRS
REMARK 200 BEAMLINE : PX9.6
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.87
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 : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41876
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.650
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 5.000
REMARK 200 R MERGE (I) : 0.07600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.10
REMARK 200 R MERGE FOR SHELL (I) : 0.35200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: ISOMORPHOUS REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: 1LNF
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.42
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.5
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 43.87200
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 87.74400
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 65.80800
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 109.68000
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 21.93600
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 43.87200
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 87.74400
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 109.68000
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 65.80800
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 21.93600
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 400
REMARK 400 COMPOUND
REMARK 400 THE ACTIVE SITE CLEFT OF THERMOLYSIN CONTAINS AT LEAST FOUR
REMARK 400 SUBSITES S1, S1(PRIME), S2, AND S2(PRIME).
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 157 OE2 GLU A 166 2.11
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 A 11 CD - NE - CZ ANGL. DEV. = 11.3 DEGREES
REMARK 500 TYR A 28 CB - CG - CD2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 ARG A 47 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ASP A 59 CB - CG - OD2 ANGL. DEV. = 12.3 DEGREES
REMARK 500 ASP A 67 CB - CG - OD1 ANGL. DEV. = 7.5 DEGREES
REMARK 500 ASP A 72 CB - CG - OD2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 ARG A 101 NE - CZ - NH1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 ASP A 138 CB - CG - OD1 ANGL. DEV. = 9.2 DEGREES
REMARK 500 HIS A 142 CE1 - NE2 - CD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 HIS A 146 ND1 - CE1 - NE2 ANGL. DEV. = -6.7 DEGREES
REMARK 500 HIS A 146 CE1 - NE2 - CD2 ANGL. DEV. = 7.7 DEGREES
REMARK 500 TYR A 151 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 GLU A 166 OE1 - CD - OE2 ANGL. DEV. = 12.5 DEGREES
REMARK 500 GLU A 177 OE1 - CD - OE2 ANGL. DEV. = -9.9 DEGREES
REMARK 500 GLU A 190 OE1 - CD - OE2 ANGL. DEV. = -7.5 DEGREES
REMARK 500 ILE A 197 O - C - N ANGL. DEV. = -10.2 DEGREES
REMARK 500 ASP A 200 CB - CG - OD2 ANGL. DEV. = 6.7 DEGREES
REMARK 500 ARG A 220 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 TYR A 251 CB - CG - CD2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 TYR A 251 CB - CG - CD1 ANGL. DEV. = 4.7 DEGREES
REMARK 500 ARG A 260 CD - NE - CZ ANGL. DEV. = 15.9 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 25 81.64 -159.95
REMARK 500 THR A 26 -63.45 78.74
REMARK 500 SER A 92 -176.13 64.29
REMARK 500 SER A 107 -160.01 57.34
REMARK 500 ASN A 111 49.83 -95.35
REMARK 500 THR A 152 -93.43 -122.10
REMARK 500 ASN A 159 -148.75 52.16
REMARK 500 THR A 194 75.54 34.02
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 RESIDUES 317 AND 318 FORM A DIPEPTIDE (VAL-LYS) BOUND IN THE ACTIVE
REMARK 600 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. THE NATIVE ENZYME HAS A
REMARK 600 VAL-LYS DIPEPTIDE BOUND IN THE ACTIVE SITE. IT IS PRESUMED THAT THE
REMARK 600 ORIGIN OF THIS DIPEPTIDE IS THE C-TERMINAL TWO RESIDUES OF THE
REMARK 600 PROTEIN. SINCE THE C-TERMINUS APPEARS AT FULL OCCUPANCY, MOLECULES
REMARK 600 NOT INCORPORATED 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 A 325 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 57 OD2
REMARK 620 2 ASP A 57 OD1 48.9
REMARK 620 3 ASP A 59 OD1 73.3 121.3
REMARK 620 4 GLN A 61 O 88.8 97.6 89.6
REMARK 620 5 HOH A 342 O 93.7 85.1 89.7 177.1
REMARK 620 6 HOH A 353 O 130.8 84.1 154.4 83.3 96.1
REMARK 620 7 HOH A 373 O 151.8 154.3 79.3 97.7 79.5 77.3
REMARK 620 N 1 2 3 4 5 6
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 138 OD2
REMARK 620 2 GLU A 177 OE1 78.9
REMARK 620 3 GLU A 177 OE2 125.4 46.7
REMARK 620 4 ASP A 185 OD1 160.8 120.2 73.8
REMARK 620 5 GLU A 187 O 84.9 145.3 141.7 77.8
REMARK 620 6 GLU A 190 OE1 85.0 131.7 124.1 82.9 76.3
REMARK 620 7 GLU A 190 OE2 96.5 88.9 80.0 86.4 123.5 47.9
REMARK 620 8 HOH A 340 O 100.1 78.6 77.2 83.3 74.3 149.6 156.8
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 322 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 142 NE2
REMARK 620 2 HIS A 146 NE2 104.8
REMARK 620 3 GLU A 166 OE1 87.6 118.6
REMARK 620 4 GLU A 166 OE2 137.6 89.5 51.3
REMARK 620 5 HOH A 327 O 113.9 133.5 88.6 79.2
REMARK 620 6 HOH A 328 O 101.9 96.2 140.4 116.2 52.2
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 GLU A 177 OE2
REMARK 620 2 ASN A 183 O 92.0
REMARK 620 3 ASP A 185 OD2 90.7 90.9
REMARK 620 4 GLU A 190 OE2 87.8 173.2 82.3
REMARK 620 5 HOH A 339 O 171.3 93.1 96.2 87.9
REMARK 620 6 HOH A 356 O 86.3 92.8 175.3 94.0 86.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 326 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR A 193 O
REMARK 620 2 THR A 194 OG1 73.6
REMARK 620 3 THR A 194 O 73.8 68.6
REMARK 620 4 ILE A 197 O 150.4 107.2 79.0
REMARK 620 5 ASP A 200 OD1 121.3 73.2 132.0 85.8
REMARK 620 6 HOH A 364 O 89.3 150.1 83.3 75.9 136.3
REMARK 620 7 HOH A 391 O 86.7 125.7 151.8 113.6 75.6 76.1
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 VAL A 317
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LYS A 318
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN 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 CA A 325
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 326
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 321
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1TLX RELATED DB: PDB
REMARK 900 RELATED ID: 1TLI RELATED DB: PDB
REMARK 900 RELATED ID: 2TLI RELATED DB: PDB
REMARK 900 RELATED ID: 3TLI RELATED DB: PDB
REMARK 900 RELATED ID: 4TLI RELATED DB: PDB
REMARK 900 RELATED ID: 5TLI RELATED DB: PDB
REMARK 900 RELATED ID: 6TLI RELATED DB: PDB
REMARK 900 RELATED ID: 7TLI RELATED DB: PDB
REMARK 900 RELATED ID: 8TLI RELATED DB: PDB
DBREF 2TLX 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 VAL A 317 7
HET LYS A 318 10
HET ZN A 322 1
HET CA A 323 1
HET CA A 324 1
HET CA A 325 1
HET CA A 326 1
HET DMS A 321 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 *207(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 VAL A 313 1 13
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 C VAL A 317 N LYS A 318 1555 1555 1.33
LINK OD2 ASP A 57 CA CA A 325 1555 1555 2.68
LINK OD1 ASP A 57 CA CA A 325 1555 1555 2.48
LINK OD1 ASP A 59 CA CA A 325 1555 1555 2.51
LINK O GLN A 61 CA CA A 325 1555 1555 2.43
LINK OD2 ASP A 138 CA CA A 323 1555 1555 2.49
LINK NE2 HIS A 142 ZN ZN A 322 1555 1555 2.22
LINK NE2 HIS A 146 ZN ZN A 322 1555 1555 2.18
LINK OE1 GLU A 166 ZN ZN A 322 1555 1555 2.68
LINK OE2 GLU A 166 ZN ZN A 322 1555 1555 2.65
LINK OE1 GLU A 177 CA CA A 323 1555 1555 2.53
LINK OE2 GLU A 177 CA CA A 323 1555 1555 2.82
LINK OE2 GLU A 177 CA CA A 324 1555 1555 2.52
LINK O ASN A 183 CA CA A 324 1555 1555 2.58
LINK OD1 ASP A 185 CA CA A 323 1555 1555 2.56
LINK OD2 ASP A 185 CA CA A 324 1555 1555 2.52
LINK O GLU A 187 CA CA A 323 1555 1555 2.52
LINK OE1 GLU A 190 CA CA A 323 1555 1555 2.60
LINK OE2 GLU A 190 CA CA A 323 1555 1555 2.61
LINK OE2 GLU A 190 CA CA A 324 1555 1555 2.52
LINK O TYR A 193 CA CA A 326 1555 1555 2.53
LINK OG1 THR A 194 CA CA A 326 1555 1555 2.65
LINK O THR A 194 CA CA A 326 1555 1555 2.61
LINK O ILE A 197 CA CA A 326 1555 1555 2.48
LINK OD1 ASP A 200 CA CA A 326 1555 1555 2.56
LINK ZN ZN A 322 O HOH A 327 1555 1555 2.41
LINK ZN ZN A 322 O HOH A 328 1555 1555 2.62
LINK CA CA A 323 O HOH A 340 1555 1555 2.52
LINK CA CA A 324 O HOH A 339 1555 1555 2.45
LINK CA CA A 324 O HOH A 356 1555 1555 2.36
LINK CA CA A 325 O HOH A 342 1555 1555 2.40
LINK CA CA A 325 O HOH A 353 1555 1555 2.41
LINK CA CA A 325 O HOH A 373 1555 1555 2.53
LINK CA CA A 326 O HOH A 364 1555 1555 2.40
LINK CA CA A 326 O HOH A 391 1555 1555 2.40
CISPEP 1 LEU A 50 PRO A 51 0 5.11
SITE 1 AC1 8 ASN A 112 ALA A 113 GLU A 143 ARG A 203
SITE 2 AC1 8 HIS A 231 LYS A 318 HOH A 328 HOH A 533
SITE 1 AC2 6 ASN A 111 ASN A 112 PHE A 130 HIS A 231
SITE 2 AC2 6 VAL A 317 HOH A 532
SITE 1 AC3 5 HIS A 142 HIS A 146 GLU A 166 HOH A 327
SITE 2 AC3 5 HOH A 328
SITE 1 AC4 6 ASP A 138 GLU A 177 ASP A 185 GLU A 187
SITE 2 AC4 6 GLU A 190 HOH A 340
SITE 1 AC5 6 GLU A 177 ASN A 183 ASP A 185 GLU A 190
SITE 2 AC5 6 HOH A 339 HOH A 356
SITE 1 AC6 6 ASP A 57 ASP A 59 GLN A 61 HOH A 342
SITE 2 AC6 6 HOH A 353 HOH A 373
SITE 1 AC7 6 TYR A 193 THR A 194 ILE A 197 ASP A 200
SITE 2 AC7 6 HOH A 364 HOH A 391
SITE 1 AC8 2 HIS A 216 SER A 218
CRYST1 94.145 94.145 131.616 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 0.010622 0.006133 0.000000 0.00000
SCALE2 0.000000 0.012265 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007598 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
