HEADER HYDROLASE 28-OCT-98 2TLI
TITLE THERMOLYSIN (5% ISOPROPANOL SOAKED CRYSTALS)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 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 HYDROLASE, METALLOPROTEINASE, ORGANIC SOLVENT
EXPDTA X-RAY DIFFRACTION
AUTHOR A.C.ENGLISH,S.H.DONE,C.R.GROOM,R.E.HUBBARD
REVDAT 5 21-FEB-24 2TLI 1 REMARK LINK
REVDAT 4 24-FEB-09 2TLI 1 VERSN
REVDAT 3 01-APR-03 2TLI 1 JRNL
REVDAT 2 13-MAR-00 2TLI 3 ATOM
REVDAT 1 18-FEB-00 2TLI 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 2
REMARK 2 RESOLUTION. 1.95 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) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.0
REMARK 3 NUMBER OF REFLECTIONS : 22727
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) : 0.166
REMARK 3 FREE R VALUE : 0.211
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 : 13
REMARK 3 SOLVENT ATOMS : 153
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.90
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) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.160
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.150
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.080
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.810
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.014 ; 0.020
REMARK 3 ANGLE DISTANCE (A) : 0.032 ; 0.040
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.038 ; 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) : 0.138 ; 0.150
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : 0.181 ; 0.300
REMARK 3 MULTIPLE TORSION (A) : 0.354 ; 0.300
REMARK 3 H-BOND (X...Y) (A) : 0.135 ; 0.300
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : 4.500 ; 7.000
REMARK 3 STAGGERED (DEGREES) : 16.700; 15.000
REMARK 3 TRANSVERSE (DEGREES) : 22.900; 20.000
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 2.517 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.809 ; 5.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 5.099 ; 5.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 6.569 ; 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 ISOPROPANOL. AT
REMARK 3 THIS CONCENTRATION (5% ISOPROPANOL) A SINGLE MOLECULE OF
REMARK 3 ISOPROPANOL IS BOUND IN THE S1(PRIME) SUBSITE.
REMARK 4
REMARK 4 2TLI 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_1000178680.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : SEP-97
REMARK 200 TEMPERATURE (KELVIN) : 293.0
REMARK 200 PH : 7.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
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 RUH2R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : CCP4
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23955
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
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 (%) : 95.0
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : 0.07800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.08
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.80
REMARK 200 R MERGE FOR SHELL (I) : 0.23600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.200
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.33
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.50
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 43.62333
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 87.24667
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 65.43500
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 109.05833
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 21.81167
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 43.62333
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 87.24667
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 109.05833
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 65.43500
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 21.81167
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: DIMERIC
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 350 BIOMT1 2 0.500000 -0.866025 0.000000 46.99500
REMARK 350 BIOMT2 2 -0.866025 -0.500000 0.000000 81.39773
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -21.81167
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 O HOH A 1002 2.03
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 GLY A 95 C ASN A 96 N -0.192
REMARK 500 TYR A 157 CB TYR A 157 CG -0.162
REMARK 500 SER A 201 C LEU A 202 N -0.217
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 ASP A 32 CB - CG - OD1 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ARG A 47 CD - NE - CZ ANGL. DEV. = 19.2 DEGREES
REMARK 500 ARG A 47 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ASP A 57 CB - CG - OD2 ANGL. DEV. = 7.2 DEGREES
REMARK 500 ASP A 59 CB - CG - OD2 ANGL. DEV. = 10.1 DEGREES
REMARK 500 GLN A 61 O - C - N ANGL. DEV. = -13.9 DEGREES
REMARK 500 TYR A 106 CB - CG - CD2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 ASP A 138 CB - CG - OD1 ANGL. DEV. = 7.9 DEGREES
REMARK 500 TYR A 157 CB - CG - CD2 ANGL. DEV. = 5.1 DEGREES
REMARK 500 TYR A 157 CB - CG - CD1 ANGL. DEV. = -7.0 DEGREES
REMARK 500 ASN A 159 O - C - N ANGL. DEV. = -10.6 DEGREES
REMARK 500 GLU A 166 OE1 - CD - OE2 ANGL. DEV. = -23.6 DEGREES
REMARK 500 GLU A 166 CG - CD - OE2 ANGL. DEV. = 18.6 DEGREES
REMARK 500 LYS A 182 O - C - N ANGL. DEV. = -10.4 DEGREES
REMARK 500 GLU A 190 OE1 - CD - OE2 ANGL. DEV. = -10.6 DEGREES
REMARK 500 ILE A 197 CA - C - N ANGL. DEV. = 14.7 DEGREES
REMARK 500 ASP A 200 CB - CG - OD2 ANGL. DEV. = 13.6 DEGREES
REMARK 500 LEU A 202 C - N - CA ANGL. DEV. = 15.2 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 77.47 -162.80
REMARK 500 THR A 26 -62.62 85.79
REMARK 500 PHE A 62 73.74 -119.03
REMARK 500 SER A 92 -172.03 61.86
REMARK 500 SER A 107 -160.95 56.84
REMARK 500 THR A 152 -97.72 -116.78
REMARK 500 TYR A 157 55.56 -92.29
REMARK 500 ASN A 159 -141.95 42.04
REMARK 500 THR A 194 78.08 36.54
REMARK 500 ASP A 207 80.71 -151.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 SER A 25 10.57
REMARK 500 ARG A 203 -10.71
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 320 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 57 OD1
REMARK 620 2 ASP A 57 OD2 48.8
REMARK 620 3 ASP A 59 OD1 120.2 72.3
REMARK 620 4 GLN A 61 O 98.0 91.8 92.4
REMARK 620 5 HOH A1017 O 85.1 93.2 89.5 174.9
REMARK 620 6 HOH A1028 O 83.5 130.8 156.3 82.5 93.9
REMARK 620 7 HOH A1048 O 155.4 150.6 79.1 96.0 79.8 78.4
REMARK 620 N 1 2 3 4 5 6
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 ASP A 138 OD2
REMARK 620 2 GLU A 177 OE1 79.0
REMARK 620 3 GLU A 177 OE2 124.4 45.6
REMARK 620 4 ASP A 185 OD1 159.5 121.5 76.0
REMARK 620 5 GLU A 187 O 84.1 146.1 142.6 78.1
REMARK 620 6 GLU A 190 OE2 94.9 87.1 81.2 86.6 123.7
REMARK 620 7 GLU A 190 OE1 83.3 128.4 124.7 83.0 77.7 46.6
REMARK 620 8 HOH A1015 O 101.7 76.9 73.1 84.7 78.1 154.1 154.6
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 317 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 OE1 91.3 121.4
REMARK 620 4 GLU A 166 OE2 139.1 89.9 49.7
REMARK 620 5 HOH A1003 O 102.6 113.3 117.3 106.1
REMARK 620 N 1 2 3 4
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 GLU A 177 OE2
REMARK 620 2 ASN A 183 O 90.8
REMARK 620 3 ASP A 185 OD2 92.8 92.4
REMARK 620 4 GLU A 190 OE2 91.6 176.1 84.5
REMARK 620 5 HOH A1014 O 168.8 93.5 97.2 84.6
REMARK 620 6 HOH A1031 O 85.7 92.3 175.1 90.9 83.9
REMARK 620 N 1 2 3 4 5
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 TYR A 193 O
REMARK 620 2 THR A 194 OG1 73.4
REMARK 620 3 THR A 194 O 76.1 70.5
REMARK 620 4 ILE A 197 O 155.8 107.5 81.5
REMARK 620 5 ASP A 200 OD1 119.8 75.4 135.7 82.8
REMARK 620 6 HOH A1039 O 83.9 144.7 78.2 82.8 139.9
REMARK 620 7 HOH A1066 O 86.3 126.7 150.8 110.0 73.4 76.9
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 ZN 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 CA A 321
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 1000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPA A 1001
DBREF 2TLI 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 317 1
HET CA A 318 1
HET CA A 319 1
HET CA A 320 1
HET CA A 321 1
HET DMS A1000 4
HET IPA A1001 4
HETNAM ZN ZINC ION
HETNAM CA CALCIUM ION
HETNAM DMS DIMETHYL SULFOXIDE
HETNAM IPA ISOPROPYL ALCOHOL
HETSYN IPA 2-PROPANOL
FORMUL 2 ZN ZN 2+
FORMUL 3 CA 4(CA 2+)
FORMUL 7 DMS C2 H6 O S
FORMUL 8 IPA C3 H8 O
FORMUL 9 HOH *153(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 TYR A 179 1 21
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 320 1555 1555 2.62
LINK OD2 ASP A 57 CA CA A 320 1555 1555 2.66
LINK OD1 ASP A 59 CA CA A 320 1555 1555 2.53
LINK O GLN A 61 CA CA A 320 1555 1555 2.60
LINK OD2 ASP A 138 CA CA A 318 1555 1555 2.57
LINK NE2 HIS A 142 ZN ZN A 317 1555 1555 2.03
LINK NE2 HIS A 146 ZN ZN A 317 1555 1555 2.03
LINK OE1 GLU A 166 ZN ZN A 317 1555 1555 2.23
LINK OE2 GLU A 166 ZN ZN A 317 1555 1555 2.29
LINK OE1 GLU A 177 CA CA A 318 1555 1555 2.64
LINK OE2 GLU A 177 CA CA A 318 1555 1555 2.89
LINK OE2 GLU A 177 CA CA A 319 1555 1555 2.55
LINK O ASN A 183 CA CA A 319 1555 1555 2.63
LINK OD1 ASP A 185 CA CA A 318 1555 1555 2.62
LINK OD2 ASP A 185 CA CA A 319 1555 1555 2.49
LINK O GLU A 187 CA CA A 318 1555 1555 2.55
LINK OE2 GLU A 190 CA CA A 318 1555 1555 2.66
LINK OE1 GLU A 190 CA CA A 318 1555 1555 2.62
LINK OE2 GLU A 190 CA CA A 319 1555 1555 2.49
LINK O TYR A 193 CA CA A 321 1555 1555 2.63
LINK OG1 THR A 194 CA CA A 321 1555 1555 2.66
LINK O THR A 194 CA CA A 321 1555 1555 2.64
LINK O ILE A 197 CA CA A 321 1555 1555 2.62
LINK OD1 ASP A 200 CA CA A 321 1555 1555 2.60
LINK ZN ZN A 317 O HOH A1003 1555 1555 2.08
LINK CA CA A 318 O HOH A1015 1555 1555 2.75
LINK CA CA A 319 O HOH A1014 1555 1555 2.55
LINK CA CA A 319 O HOH A1031 1555 1555 2.53
LINK CA CA A 320 O HOH A1017 1555 1555 2.27
LINK CA CA A 320 O HOH A1028 1555 1555 2.52
LINK CA CA A 320 O HOH A1048 1555 1555 2.68
LINK CA CA A 321 O HOH A1039 1555 1555 2.50
LINK CA CA A 321 O HOH A1066 1555 1555 2.60
CISPEP 1 LEU A 50 PRO A 51 0 6.85
SITE 1 AC1 4 HIS A 142 HIS A 146 GLU A 166 HOH A1003
SITE 1 AC2 6 ASP A 138 GLU A 177 ASP A 185 GLU A 187
SITE 2 AC2 6 GLU A 190 HOH A1015
SITE 1 AC3 6 GLU A 177 ASN A 183 ASP A 185 GLU A 190
SITE 2 AC3 6 HOH A1014 HOH A1031
SITE 1 AC4 6 ASP A 57 ASP A 59 GLN A 61 HOH A1017
SITE 2 AC4 6 HOH A1028 HOH A1048
SITE 1 AC5 6 TYR A 193 THR A 194 ILE A 197 ASP A 200
SITE 2 AC5 6 HOH A1039 HOH A1066
SITE 1 AC6 4 HIS A 216 SER A 218 TYR A 251 HOH A1117
SITE 1 AC7 4 GLU A 143 LEU A 202 ARG A 203 HOH A1068
CRYST1 93.990 93.990 130.870 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 0.010639 0.006143 0.000000 0.00000
SCALE2 0.000000 0.012285 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007641 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
