HEADER GLUTATHIONE TRANSFERASE 01-DEC-94 1GTA
TITLE CRYSTAL STRUCTURES OF A SCHISTOSOMAL DRUG AND VACCINE TARGET:
TITLE 2 GLUTATHIONE S-TRANSFERASE FROM SCHISTOSOMA JAPONICA AND ITS COMPLEX
TITLE 3 WITH THE LEADING ANTISCHISTOSOMAL DRUG PRAZIQUANTEL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTATHIONE S-TRANSFERASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 2.5.1.18;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SCHISTOSOMA JAPONICUM;
SOURCE 3 ORGANISM_TAXID: 6182;
SOURCE 4 EXPRESSION_SYSTEM_PLASMID: PGEX-3X
KEYWDS GLUTATHIONE TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.A.MCTIGUE,J.A.TAINER
REVDAT 5 07-FEB-24 1GTA 1 REMARK
REVDAT 4 13-JUL-11 1GTA 1 VERSN
REVDAT 3 24-FEB-09 1GTA 1 VERSN
REVDAT 2 01-APR-03 1GTA 1 JRNL
REVDAT 1 07-FEB-95 1GTA 0
JRNL AUTH M.A.MCTIGUE,D.R.WILLIAMS,J.A.TAINER
JRNL TITL CRYSTAL STRUCTURES OF A SCHISTOSOMAL DRUG AND VACCINE
JRNL TITL 2 TARGET: GLUTATHIONE S-TRANSFERASE FROM SCHISTOSOMA JAPONICA
JRNL TITL 3 AND ITS COMPLEX WITH THE LEADING ANTISCHISTOSOMAL DRUG
JRNL TITL 4 PRAZIQUANTEL.
JRNL REF J.MOL.BIOL. V. 246 21 1995
JRNL REFN ISSN 0022-2836
JRNL PMID 7853399
JRNL DOI 10.1006/JMBI.1994.0061
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 7.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : NULL
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.197
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 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1786
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 114
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
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) : 0.024
REMARK 3 BOND ANGLES (DEGREES) : 4.100
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1GTA 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_1000173702.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 10832
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: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63 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
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/2
REMARK 290 6555 X-Y,X,Z+1/2
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z
REMARK 290 10555 -Y,-X,-Z+1/2
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/2
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 0.00000
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 0.00000
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 35.10000
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 35.10000
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 35.10000
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 0.00000
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 0.00000
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 35.10000
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 35.10000
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 35.10000
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 300 REMARK: THE SECOND SUBUNIT OF THE GST DIMER IS GENERATED BY THE
REMARK 300 SYMMETRY OPERATION Y, X, -Z.
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 3010 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19350 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL
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 0.00000
REMARK 350 BIOMT2 2 0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 70.20000
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 HIS A 215 CG ND1 CD2 CE1 NE2
REMARK 470 LYS A 218 CG CD CE NZ
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 HIS A 31 NE2 HIS A 31 CD2 -0.068
REMARK 500 HIS A 147 NE2 HIS A 147 CD2 -0.066
REMARK 500 HIS A 150 NE2 HIS A 150 CD2 -0.073
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 TRP A 8 CD1 - CG - CD2 ANGL. DEV. = 9.0 DEGREES
REMARK 500 TRP A 8 CG - CD1 - NE1 ANGL. DEV. = -6.7 DEGREES
REMARK 500 TRP A 8 CE2 - CD2 - CG ANGL. DEV. = -6.1 DEGREES
REMARK 500 VAL A 14 CG1 - CB - CG2 ANGL. DEV. = -10.4 DEGREES
REMARK 500 ARG A 18 NE - CZ - NH1 ANGL. DEV. = 11.8 DEGREES
REMARK 500 ARG A 18 NE - CZ - NH2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 TYR A 23 CD1 - CG - CD2 ANGL. DEV. = 6.8 DEGREES
REMARK 500 TYR A 23 CB - CG - CD1 ANGL. DEV. = -4.8 DEGREES
REMARK 500 GLU A 34 CA - CB - CG ANGL. DEV. = -14.2 DEGREES
REMARK 500 ARG A 35 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG A 35 NE - CZ - NH2 ANGL. DEV. = -4.9 DEGREES
REMARK 500 TRP A 41 CD1 - CG - CD2 ANGL. DEV. = 8.2 DEGREES
REMARK 500 TRP A 41 CB - CG - CD1 ANGL. DEV. = -8.7 DEGREES
REMARK 500 TRP A 41 CG - CD1 - NE1 ANGL. DEV. = -6.6 DEGREES
REMARK 500 TRP A 41 CE2 - CD2 - CG ANGL. DEV. = -6.8 DEGREES
REMARK 500 TRP A 41 CG - CD2 - CE3 ANGL. DEV. = 6.6 DEGREES
REMARK 500 ARG A 42 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG A 42 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 VAL A 63 N - CA - CB ANGL. DEV. = -14.6 DEGREES
REMARK 500 LEU A 65 CA - CB - CG ANGL. DEV. = 13.8 DEGREES
REMARK 500 THR A 66 N - CA - C ANGL. DEV. = 20.2 DEGREES
REMARK 500 MET A 69 CG - SD - CE ANGL. DEV. = -25.7 DEGREES
REMARK 500 ARG A 73 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 TYR A 74 CB - CG - CD1 ANGL. DEV. = -4.0 DEGREES
REMARK 500 GLY A 83 CA - C - N ANGL. DEV. = 18.9 DEGREES
REMARK 500 MET A 94 CG - SD - CE ANGL. DEV. = -26.2 DEGREES
REMARK 500 ARG A 103 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG A 108 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 TYR A 111 CB - CG - CD2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 PHE A 122 CB - CG - CD2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 ARG A 136 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 CYS A 138 CA - CB - SG ANGL. DEV. = -14.0 DEGREES
REMARK 500 VAL A 148 CG1 - CB - CG2 ANGL. DEV. = -15.8 DEGREES
REMARK 500 TYR A 156 CB - CG - CD2 ANGL. DEV. = -6.7 DEGREES
REMARK 500 MET A 165 CG - SD - CE ANGL. DEV. = -18.2 DEGREES
REMARK 500 ALA A 172 CB - CA - C ANGL. DEV. = -10.0 DEGREES
REMARK 500 ALA A 172 N - CA - CB ANGL. DEV. = 9.6 DEGREES
REMARK 500 TRP A 201 CD1 - CG - CD2 ANGL. DEV. = 6.4 DEGREES
REMARK 500 TRP A 201 CE2 - CD2 - CG ANGL. DEV. = -5.7 DEGREES
REMARK 500 TRP A 206 CD1 - CG - CD2 ANGL. DEV. = 5.1 DEGREES
REMARK 500 ASP A 214 CB - CG - OD1 ANGL. DEV. = 6.9 DEGREES
REMARK 500 HIS A 215 N - CA - C ANGL. DEV. = 17.0 DEGREES
REMARK 500 PRO A 216 C - N - CA ANGL. DEV. = 17.6 DEGREES
REMARK 500 PRO A 216 CA - N - CD ANGL. DEV. = -8.7 DEGREES
REMARK 500 PRO A 216 N - CA - C ANGL. DEV. = 28.6 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 TYR A 111 -18.37 60.96
REMARK 500 ALA A 172 -23.05 97.12
REMARK 500 HIS A 215 -169.77 -119.56
REMARK 500 PRO A 216 131.56 -23.48
REMARK 500 PRO A 217 170.53 -52.57
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 HIS A 215 PRO A 216 110.29
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 HIS A 215 10.82
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1GTA A 1 218 UNP P08515 GST26_SCHJA 1 218
SEQRES 1 A 218 MET SER PRO ILE LEU GLY TYR TRP LYS ILE LYS GLY LEU
SEQRES 2 A 218 VAL GLN PRO THR ARG LEU LEU LEU GLU TYR LEU GLU GLU
SEQRES 3 A 218 LYS TYR GLU GLU HIS LEU TYR GLU ARG ASP GLU GLY ASP
SEQRES 4 A 218 LYS TRP ARG ASN LYS LYS PHE GLU LEU GLY LEU GLU PHE
SEQRES 5 A 218 PRO ASN LEU PRO TYR TYR ILE ASP GLY ASP VAL LYS LEU
SEQRES 6 A 218 THR GLN SER MET ALA ILE ILE ARG TYR ILE ALA ASP LYS
SEQRES 7 A 218 HIS ASN MET LEU GLY GLY CYS PRO LYS GLU ARG ALA GLU
SEQRES 8 A 218 ILE SER MET LEU GLU GLY ALA VAL LEU ASP ILE ARG TYR
SEQRES 9 A 218 GLY VAL SER ARG ILE ALA TYR SER LYS ASP PHE GLU THR
SEQRES 10 A 218 LEU LYS VAL ASP PHE LEU SER LYS LEU PRO GLU MET LEU
SEQRES 11 A 218 LYS MET PHE GLU ASP ARG LEU CYS HIS LYS THR TYR LEU
SEQRES 12 A 218 ASN GLY ASP HIS VAL THR HIS PRO ASP PHE MET LEU TYR
SEQRES 13 A 218 ASP ALA LEU ASP VAL VAL LEU TYR MET ASP PRO MET CYS
SEQRES 14 A 218 LEU ASP ALA PHE PRO LYS LEU VAL CYS PHE LYS LYS ARG
SEQRES 15 A 218 ILE GLU ALA ILE PRO GLN ILE ASP LYS TYR LEU LYS SER
SEQRES 16 A 218 SER LYS TYR ILE ALA TRP PRO LEU GLN GLY TRP GLN ALA
SEQRES 17 A 218 THR PHE GLY GLY GLY ASP HIS PRO PRO LYS
FORMUL 2 HOH *114(H2 O)
HELIX 1 H1 GLN A 15 LEU A 24 1 10
HELIX 2 H2 GLY A 38 LYS A 44 1 7
HELIX 3 H3 GLN A 67 ALA A 76 1 10
HELIX 4 H4 GLU A 88 ILE A 109 1 22
HELIX 5 H5A PHE A 115 PHE A 122 1 8
HELIX 6 H5B LEU A 126 LEU A 137 1 12
HELIX 7 H6 ASP A 152 MET A 165 1 14
HELIX 8 H7 PRO A 174 GLU A 184 1 11
HELIX 9 H8 ILE A 189 LYS A 194 1 6
SHEET 1 S1 4 GLU A 29 TYR A 33 0
SHEET 2 S1 4 PRO A 3 TYR A 7 1 N LEU A 5 O GLU A 29
SHEET 3 S1 4 TYR A 57 ASP A 60 -1 N TYR A 57 O GLY A 6
SHEET 4 S1 4 VAL A 63 THR A 66 -1 O VAL A 63 N ASP A 60
CISPEP 1 LEU A 55 PRO A 56 0 4.02
CISPEP 2 TRP A 201 PRO A 202 0 -6.49
CRYST1 125.200 125.200 70.200 90.00 90.00 120.00 P 63 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 0.007987 0.004611 0.000000 0.00000
SCALE2 0.000000 0.009223 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014245 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
