HEADER LYASE 18-DEC-03 1V7L
TITLE STRUCTURE OF 3-ISOPROPYLMALATE ISOMERASE SMALL SUBUNIT FROM PYROCOCCUS
TITLE 2 HORIKOSHII
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 3-ISOPROPYLMALATE DEHYDRATASE SMALL SUBUNIT;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: 3-ISOPROPYLMALATE ISOMERASE SMALL SUBUNIT, ISOPROPYLMALATE
COMPND 5 ISOMERASE, ALPHA-IPM ISOMERASE, IPMI;
COMPND 6 EC: 4.2.1.33;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PYROCOCCUS HORIKOSHII;
SOURCE 3 ORGANISM_TAXID: 70601;
SOURCE 4 STRAIN: OT3;
SOURCE 5 GENE: PH1724;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: B834(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-22B
KEYWDS BETA BARREL, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.YAO,T.KIRITA,N.SAKAI,I.TANAKA
REVDAT 4 27-DEC-23 1V7L 1 REMARK
REVDAT 3 13-JUL-11 1V7L 1 VERSN
REVDAT 2 24-FEB-09 1V7L 1 VERSN
REVDAT 1 16-NOV-04 1V7L 0
JRNL AUTH Y.YASUTAKE,M.YAO,N.SAKAI,T.KIRITA,I.TANAKA
JRNL TITL CRYSTAL STRUCTURE OF THE PYROCOCCUS HORIKOSHII
JRNL TITL 2 ISOPROPYLMALATE ISOMERASE SMALL SUBUNIT PROVIDES INSIGHT
JRNL TITL 3 INTO THE DUAL SUBSTRATE SPECIFICITY OF THE ENZYME
JRNL REF J.MOL.BIOL. V. 344 325 2004
JRNL REFN ISSN 0022-2836
JRNL PMID 15522288
JRNL DOI 10.1016/J.JMB.2004.09.035
REMARK 2
REMARK 2 RESOLUTION. 1.98 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.98
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 28757
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) : 0.206
REMARK 3 FREE R VALUE : 0.247
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2914
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 : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.98
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.10
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.62
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4221
REMARK 3 BIN R VALUE (WORKING SET) : 0.2352
REMARK 3 BIN FREE R VALUE : 0.2762
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.83
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 462
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 : 2528
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 294
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 35.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.34
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.90300
REMARK 3 B22 (A**2) : -2.90300
REMARK 3 B33 (A**2) : 5.80500
REMARK 3 B12 (A**2) : -2.55500
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.25
REMARK 3 ESD FROM SIGMAA (A) : 0.15
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) : 0.30
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.20
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.640
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.94
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.050
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.558 ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.405 ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.375 ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.695 ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : THROUGHOUT
REMARK 3 KSOL : 0.44
REMARK 3 BSOL : 55.98
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 : CNS_PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 1 : CNS_PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1V7L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-DEC-03.
REMARK 100 THE DEPOSITION ID IS D_1000006306.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-DEC-00
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.3
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL41XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.045
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA, CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29033
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.980
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 15.10
REMARK 200 R MERGE (I) : 0.08400
REMARK 200 R SYM (I) : 0.08200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.98
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.09
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 15.40
REMARK 200 R MERGE FOR SHELL (I) : 0.38900
REMARK 200 R SYM FOR SHELL (I) : 0.37700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE, SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.83
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES, 1.4M AMMONIUM SULFATE, PH
REMARK 280 7.3, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 62 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+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z
REMARK 290 5555 Y,-X+Y,Z+2/3
REMARK 290 6555 X-Y,X,Z+1/3
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+2/3
REMARK 290 11555 -X+Y,Y,-Z
REMARK 290 12555 X,X-Y,-Z+1/3
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 101.50533
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 50.75267
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 0.00000
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 101.50533
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 50.75267
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 101.50533
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 50.75267
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 101.50533
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 0.00000
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 50.75267
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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, B
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 18950 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 47870 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -74.0 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 -1.000000 0.000000 0.000000 -47.60400
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 82.45255
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 3 -0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 -1.000000 50.75267
REMARK 350 BIOMT1 4 0.500000 0.866025 0.000000 -47.60400
REMARK 350 BIOMT2 4 0.866025 -0.500000 0.000000 82.45255
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 50.75267
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 5 -0.500000 0.866025 0.000000 -47.60400
REMARK 350 BIOMT2 5 -0.866025 -0.500000 0.000000 82.45255
REMARK 350 BIOMT3 5 0.000000 0.000000 1.000000 50.75267
REMARK 350 BIOMT1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 6 0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 6 0.000000 0.000000 1.000000 50.75267
REMARK 350 BIOMT1 7 1.000000 0.000000 0.000000 -47.60400
REMARK 350 BIOMT2 7 0.000000 -1.000000 0.000000 82.45255
REMARK 350 BIOMT3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 8 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 8 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
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
REMARK 350 BIOMOLECULE: 4
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ARG A 163
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 O LEU B 26 N THR B 27 1.54
REMARK 500 O TYR B 24 N LEU B 26 1.97
REMARK 500 CD2 TYR B 24 OG SER B 69 2.14
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 ARG B 23 C TYR B 24 N 0.174
REMARK 500 LEU B 26 C THR B 27 N -0.438
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 B 23 CA - C - N ANGL. DEV. = -29.5 DEGREES
REMARK 500 ARG B 23 O - C - N ANGL. DEV. = 29.2 DEGREES
REMARK 500 ASN B 25 C - N - CA ANGL. DEV. = -15.8 DEGREES
REMARK 500 ASN B 25 CA - CB - CG ANGL. DEV. = -13.6 DEGREES
REMARK 500 LEU B 26 CA - C - N ANGL. DEV. = 28.4 DEGREES
REMARK 500 LEU B 26 O - C - N ANGL. DEV. = -30.9 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 LEU A 26 80.41 -63.37
REMARK 500 THR A 27 141.72 -173.18
REMARK 500 ARG A 42 80.04 -150.90
REMARK 500 ARG A 157 57.54 -111.86
REMARK 500 ASP A 159 18.55 46.84
REMARK 500 LEU A 160 44.30 -79.40
REMARK 500 PRO B 21 -80.89 -74.79
REMARK 500 ARG B 23 -46.20 167.24
REMARK 500 TYR B 24 -16.81 -49.03
REMARK 500 ASN B 25 97.75 -56.47
REMARK 500 LEU B 26 3.13 33.50
REMARK 500 THR B 27 79.31 -55.62
REMARK 500 LYS B 28 -24.55 -39.52
REMARK 500 ASP B 29 97.82 -38.68
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 LEU B 26 23.65
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1V7L A 1 163 UNP O59393 LEUD_PYRHO 1 163
DBREF 1V7L B 1 163 UNP O59393 LEUD_PYRHO 1 163
SEQRES 1 A 163 MET ILE THR THR GLY LYS VAL TRP LYS PHE GLY ASP ASP
SEQRES 2 A 163 ILE SER THR ASP GLU ILE THR PRO GLY ARG TYR ASN LEU
SEQRES 3 A 163 THR LYS ASP PRO LYS GLU LEU ALA LYS ILE ALA PHE ILE
SEQRES 4 A 163 GLU VAL ARG PRO ASP PHE ALA ARG ASN VAL ARG PRO GLY
SEQRES 5 A 163 ASP VAL VAL VAL ALA GLY LYS ASN PHE GLY ILE GLY SER
SEQRES 6 A 163 SER ARG GLU SER ALA ALA LEU ALA LEU LYS ALA LEU GLY
SEQRES 7 A 163 ILE ALA GLY VAL ILE ALA GLU SER PHE GLY ARG ILE PHE
SEQRES 8 A 163 TYR ARG ASN ALA ILE ASN ILE GLY ILE PRO LEU LEU LEU
SEQRES 9 A 163 GLY LYS THR GLU GLY LEU LYS ASP GLY ASP LEU VAL THR
SEQRES 10 A 163 VAL ASN TRP GLU THR GLY GLU VAL ARG LYS GLY ASP GLU
SEQRES 11 A 163 ILE LEU MET PHE GLU PRO LEU GLU ASP PHE LEU LEU GLU
SEQRES 12 A 163 ILE VAL ARG GLU GLY GLY ILE LEU GLU TYR ILE ARG ARG
SEQRES 13 A 163 ARG GLY ASP LEU CYS ILE ARG
SEQRES 1 B 163 MET ILE THR THR GLY LYS VAL TRP LYS PHE GLY ASP ASP
SEQRES 2 B 163 ILE SER THR ASP GLU ILE THR PRO GLY ARG TYR ASN LEU
SEQRES 3 B 163 THR LYS ASP PRO LYS GLU LEU ALA LYS ILE ALA PHE ILE
SEQRES 4 B 163 GLU VAL ARG PRO ASP PHE ALA ARG ASN VAL ARG PRO GLY
SEQRES 5 B 163 ASP VAL VAL VAL ALA GLY LYS ASN PHE GLY ILE GLY SER
SEQRES 6 B 163 SER ARG GLU SER ALA ALA LEU ALA LEU LYS ALA LEU GLY
SEQRES 7 B 163 ILE ALA GLY VAL ILE ALA GLU SER PHE GLY ARG ILE PHE
SEQRES 8 B 163 TYR ARG ASN ALA ILE ASN ILE GLY ILE PRO LEU LEU LEU
SEQRES 9 B 163 GLY LYS THR GLU GLY LEU LYS ASP GLY ASP LEU VAL THR
SEQRES 10 B 163 VAL ASN TRP GLU THR GLY GLU VAL ARG LYS GLY ASP GLU
SEQRES 11 B 163 ILE LEU MET PHE GLU PRO LEU GLU ASP PHE LEU LEU GLU
SEQRES 12 B 163 ILE VAL ARG GLU GLY GLY ILE LEU GLU TYR ILE ARG ARG
SEQRES 13 B 163 ARG GLY ASP LEU CYS ILE ARG
FORMUL 3 HOH *294(H2 O)
HELIX 1 1 SER A 15 THR A 20 1 6
HELIX 2 2 ASP A 29 ALA A 37 1 9
HELIX 3 3 ASP A 44 VAL A 49 1 6
HELIX 4 4 GLU A 68 GLY A 78 1 11
HELIX 5 5 GLY A 88 GLY A 99 1 12
HELIX 6 6 GLU A 138 GLU A 147 1 10
HELIX 7 7 GLY A 149 ARG A 157 1 9
HELIX 8 8 SER B 15 THR B 20 1 6
HELIX 9 9 ASP B 29 ALA B 37 1 9
HELIX 10 10 ASP B 44 VAL B 49 1 6
HELIX 11 11 GLU B 68 LEU B 77 1 10
HELIX 12 12 GLY B 88 GLY B 99 1 12
HELIX 13 13 GLU B 138 GLY B 148 1 11
HELIX 14 14 GLY B 149 GLY B 158 1 10
SHEET 1 A 8 GLU A 130 MET A 133 0
SHEET 2 A 8 GLU A 124 LYS A 127 -1 N VAL A 125 O LEU A 132
SHEET 3 A 8 LEU A 115 ASN A 119 -1 N THR A 117 O ARG A 126
SHEET 4 A 8 ILE A 2 LYS A 9 -1 N THR A 3 O VAL A 118
SHEET 5 A 8 VAL A 54 VAL A 56 1 O VAL A 56 N TRP A 8
SHEET 6 A 8 GLY A 81 ALA A 84 1 O ILE A 83 N VAL A 55
SHEET 7 A 8 LEU A 102 LEU A 104 1 O LEU A 103 N VAL A 82
SHEET 8 A 8 GLU A 135 PRO A 136 -1 O GLU A 135 N LEU A 104
SHEET 1 B 7 LEU B 102 LEU B 104 0
SHEET 2 B 7 GLY B 81 ALA B 84 1 N VAL B 82 O LEU B 103
SHEET 3 B 7 VAL B 54 VAL B 56 1 N VAL B 55 O ILE B 83
SHEET 4 B 7 ILE B 2 LYS B 9 1 N TRP B 8 O VAL B 56
SHEET 5 B 7 LEU B 115 ASN B 119 -1 O VAL B 118 N THR B 3
SHEET 6 B 7 GLU B 124 LYS B 127 -1 O ARG B 126 N THR B 117
SHEET 7 B 7 GLU B 130 MET B 133 -1 O LEU B 132 N VAL B 125
SSBOND 1 CYS A 161 CYS A 161 1555 12565 2.50
SSBOND 2 CYS B 161 CYS B 161 1555 10664 2.20
CRYST1 95.208 95.208 152.258 90.00 90.00 120.00 P 62 2 2 24
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 0.010503 0.006064 0.000000 0.00000
SCALE2 0.000000 0.012128 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006568 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
