HEADER HYDROLASE 27-MAY-14 4TKK
TITLE SULFOLOBUS SOLFATARICUS HJC MUTANTS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HOLLIDAY JUNCTION RESOLVASE HJC;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: HJC;
COMPND 5 EC: 3.1.22.4;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SULFOLOBUS SOLFATARICUS;
SOURCE 3 ORGANISM_TAXID: 273057;
SOURCE 4 STRAIN: ATCC 35092 / DSM 1617 / JCM 11322 / P2;
SOURCE 5 GENE: HJC, SSO0575, ORF-C21_024;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.S.BOND
REVDAT 2 27-DEC-23 4TKK 1 REMARK
REVDAT 1 12-AUG-15 4TKK 0
JRNL AUTH C.L.MIDDLETON,J.L.PARKER,G.J.KNOTT,M.F.WHITE,C.S.BOND
JRNL TITL CRYSTAL UNENGINEERING: REDUCING THE CRYSTALLISABILITY OF
JRNL TITL 2 SULFOLOBUS SOLFATARICUS HJC
JRNL REF AUST.J.CHEM. V. 67 1818 2014
JRNL REFN ISSN 0004-9425
JRNL DOI 10.1071/CH14342
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.0
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 16.23
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 3 NUMBER OF REFLECTIONS : 18062
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 + TEST SET) : 0.204
REMARK 3 R VALUE (WORKING SET) : 0.202
REMARK 3 FREE R VALUE : 0.248
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.110
REMARK 3 FREE R VALUE TEST SET COUNT : 923
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 : 9
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.54
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.34
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2929
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2678
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2773
REMARK 3 BIN R VALUE (WORKING SET) : 0.2649
REMARK 3 BIN FREE R VALUE : 0.3209
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.33
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 156
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 : 2000
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 167
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 54.91
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 52.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
REMARK 3 B12 (A**2) : 0.00000
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) : 0.328
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.241
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.208
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.234
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.207
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.946
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.915
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 2020 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 2704 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 768 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 48 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 288 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 2020 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 268 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 2548 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.19
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.14
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 20.10
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4TKK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-JUN-14.
REMARK 100 THE DEPOSITION ID IS D_1000201774.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-NOV-00
REMARK 200 TEMPERATURE (KELVIN) : 103.15
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
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) : 0.86
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18314
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
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 (%) : 99.4
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.7000
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: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
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 (%): 66.37
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.66
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: (26.6% V/V PEG 400, 5% GLYCEROL, 0.19M
REMARK 280 CALCIUM CHLORIDE AND 0.095M HEPES PH 7.4, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 Z,X,Y
REMARK 290 6555 Z,-X,-Y
REMARK 290 7555 -Z,-X,Y
REMARK 290 8555 -Z,X,-Y
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z,-X
REMARK 290 11555 Y,-Z,-X
REMARK 290 12555 -Y,-Z,X
REMARK 290 13555 X+1/2,Y+1/2,Z+1/2
REMARK 290 14555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 15555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 16555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 17555 Z+1/2,X+1/2,Y+1/2
REMARK 290 18555 Z+1/2,-X+1/2,-Y+1/2
REMARK 290 19555 -Z+1/2,-X+1/2,Y+1/2
REMARK 290 20555 -Z+1/2,X+1/2,-Y+1/2
REMARK 290 21555 Y+1/2,Z+1/2,X+1/2
REMARK 290 22555 -Y+1/2,Z+1/2,-X+1/2
REMARK 290 23555 Y+1/2,-Z+1/2,-X+1/2
REMARK 290 24555 -Y+1/2,-Z+1/2,X+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 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 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 0.00000
REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 70.58600
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 70.58600
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 70.58600
REMARK 290 SMTRY1 14 -1.000000 0.000000 0.000000 70.58600
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 70.58600
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 70.58600
REMARK 290 SMTRY1 15 -1.000000 0.000000 0.000000 70.58600
REMARK 290 SMTRY2 15 0.000000 1.000000 0.000000 70.58600
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 70.58600
REMARK 290 SMTRY1 16 1.000000 0.000000 0.000000 70.58600
REMARK 290 SMTRY2 16 0.000000 -1.000000 0.000000 70.58600
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 70.58600
REMARK 290 SMTRY1 17 0.000000 0.000000 1.000000 70.58600
REMARK 290 SMTRY2 17 1.000000 0.000000 0.000000 70.58600
REMARK 290 SMTRY3 17 0.000000 1.000000 0.000000 70.58600
REMARK 290 SMTRY1 18 0.000000 0.000000 1.000000 70.58600
REMARK 290 SMTRY2 18 -1.000000 0.000000 0.000000 70.58600
REMARK 290 SMTRY3 18 0.000000 -1.000000 0.000000 70.58600
REMARK 290 SMTRY1 19 0.000000 0.000000 -1.000000 70.58600
REMARK 290 SMTRY2 19 -1.000000 0.000000 0.000000 70.58600
REMARK 290 SMTRY3 19 0.000000 1.000000 0.000000 70.58600
REMARK 290 SMTRY1 20 0.000000 0.000000 -1.000000 70.58600
REMARK 290 SMTRY2 20 1.000000 0.000000 0.000000 70.58600
REMARK 290 SMTRY3 20 0.000000 -1.000000 0.000000 70.58600
REMARK 290 SMTRY1 21 0.000000 1.000000 0.000000 70.58600
REMARK 290 SMTRY2 21 0.000000 0.000000 1.000000 70.58600
REMARK 290 SMTRY3 21 1.000000 0.000000 0.000000 70.58600
REMARK 290 SMTRY1 22 0.000000 -1.000000 0.000000 70.58600
REMARK 290 SMTRY2 22 0.000000 0.000000 1.000000 70.58600
REMARK 290 SMTRY3 22 -1.000000 0.000000 0.000000 70.58600
REMARK 290 SMTRY1 23 0.000000 1.000000 0.000000 70.58600
REMARK 290 SMTRY2 23 0.000000 0.000000 -1.000000 70.58600
REMARK 290 SMTRY3 23 -1.000000 0.000000 0.000000 70.58600
REMARK 290 SMTRY1 24 0.000000 -1.000000 0.000000 70.58600
REMARK 290 SMTRY2 24 0.000000 0.000000 -1.000000 70.58600
REMARK 290 SMTRY3 24 1.000000 0.000000 0.000000 70.58600
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1530 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13710 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL
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 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 MET A 1
REMARK 465 ASN A 2
REMARK 465 ALA A 3
REMARK 465 LYS A 4
REMARK 465 LYS A 5
REMARK 465 ARG A 6
REMARK 465 LYS A 7
REMARK 465 GLY A 8
REMARK 465 ALA A 32
REMARK 465 GLY A 33
REMARK 465 SER A 34
REMARK 465 LYS A 35
REMARK 465 ARG A 36
REMARK 465 ASN A 141
REMARK 465 PHE A 142
REMARK 465 LEU A 143
REMARK 465 MET B 1
REMARK 465 ASN B 2
REMARK 465 ALA B 3
REMARK 465 LYS B 4
REMARK 465 LYS B 5
REMARK 465 ARG B 6
REMARK 465 LYS B 7
REMARK 465 GLY B 8
REMARK 465 ALA B 32
REMARK 465 GLY B 33
REMARK 465 SER B 34
REMARK 465 LYS B 35
REMARK 465 ARG B 36
REMARK 465 ASN B 141
REMARK 465 PHE B 142
REMARK 465 LEU B 143
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLU A 118 CG CD OE1 OE2
REMARK 480 GLU B 118 CG
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 ILE B 119 92.75 -64.46
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 249 DISTANCE = 9.57 ANGSTROMS
REMARK 525 HOH A 255 DISTANCE = 16.09 ANGSTROMS
REMARK 525 HOH A 267 DISTANCE = 7.71 ANGSTROMS
REMARK 525 HOH A 269 DISTANCE = 15.70 ANGSTROMS
REMARK 525 HOH A 270 DISTANCE = 7.53 ANGSTROMS
REMARK 525 HOH A 282 DISTANCE = 12.96 ANGSTROMS
REMARK 525 HOH B 270 DISTANCE = 11.76 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4TKD RELATED DB: PDB
DBREF 4TKK A 1 143 UNP Q7LXU0 HJC_SULSO 1 143
DBREF 4TKK B 1 143 UNP Q7LXU0 HJC_SULSO 1 143
SEQADV 4TKK ALA A 32 UNP Q7LXU0 SER 32 ENGINEERED MUTATION
SEQADV 4TKK ALA B 32 UNP Q7LXU0 SER 32 ENGINEERED MUTATION
SEQRES 1 A 143 MET ASN ALA LYS LYS ARG LYS GLY SER ALA VAL GLU ARG
SEQRES 2 A 143 ASN ILE VAL SER ARG LEU ARG ASP LYS GLY PHE ALA VAL
SEQRES 3 A 143 VAL ARG ALA PRO ALA ALA GLY SER LYS ARG LYS ASP PRO
SEQRES 4 A 143 ILE PRO ASP ILE ILE ALA LEU LYS ASN GLY VAL ILE ILE
SEQRES 5 A 143 LEU ILE GLU MET LYS SER ARG LYS ASP ILE GLU GLY LYS
SEQRES 6 A 143 ILE TYR VAL ARG ARG GLU GLN ALA GLU GLY ILE ILE GLU
SEQRES 7 A 143 PHE ALA ARG LYS SER GLY GLY SER LEU PHE LEU GLY VAL
SEQRES 8 A 143 LYS LYS PRO GLY VAL LEU LYS PHE ILE PRO PHE GLU LYS
SEQRES 9 A 143 LEU ARG ARG THR GLU THR GLY ASN TYR VAL ALA ASP SER
SEQRES 10 A 143 GLU ILE GLU GLY LEU ASP LEU GLU ASP LEU VAL ARG LEU
SEQRES 11 A 143 VAL GLU ALA LYS ILE SER ARG THR LEU ASP ASN PHE LEU
SEQRES 1 B 143 MET ASN ALA LYS LYS ARG LYS GLY SER ALA VAL GLU ARG
SEQRES 2 B 143 ASN ILE VAL SER ARG LEU ARG ASP LYS GLY PHE ALA VAL
SEQRES 3 B 143 VAL ARG ALA PRO ALA ALA GLY SER LYS ARG LYS ASP PRO
SEQRES 4 B 143 ILE PRO ASP ILE ILE ALA LEU LYS ASN GLY VAL ILE ILE
SEQRES 5 B 143 LEU ILE GLU MET LYS SER ARG LYS ASP ILE GLU GLY LYS
SEQRES 6 B 143 ILE TYR VAL ARG ARG GLU GLN ALA GLU GLY ILE ILE GLU
SEQRES 7 B 143 PHE ALA ARG LYS SER GLY GLY SER LEU PHE LEU GLY VAL
SEQRES 8 B 143 LYS LYS PRO GLY VAL LEU LYS PHE ILE PRO PHE GLU LYS
SEQRES 9 B 143 LEU ARG ARG THR GLU THR GLY ASN TYR VAL ALA ASP SER
SEQRES 10 B 143 GLU ILE GLU GLY LEU ASP LEU GLU ASP LEU VAL ARG LEU
SEQRES 11 B 143 VAL GLU ALA LYS ILE SER ARG THR LEU ASP ASN PHE LEU
FORMUL 3 HOH *167(H2 O)
HELIX 1 AA1 SER A 9 LYS A 22 1 14
HELIX 2 AA2 ARG A 69 GLY A 84 1 16
HELIX 3 AA3 GLU A 103 LEU A 105 5 3
HELIX 4 AA4 ASP A 123 ASP A 140 1 18
HELIX 5 AA5 ALA B 10 LYS B 22 1 13
HELIX 6 AA6 ARG B 69 GLY B 84 1 16
HELIX 7 AA7 GLU B 103 LEU B 105 5 3
HELIX 8 AA8 ASP B 123 ASP B 140 1 18
SHEET 1 AA1 5 ALA A 25 ARG A 28 0
SHEET 2 AA1 5 ILE A 43 LYS A 47 -1 O LEU A 46 N ALA A 25
SHEET 3 AA1 5 VAL A 50 GLU A 55 -1 O ILE A 52 N ALA A 45
SHEET 4 AA1 5 SER A 86 LYS A 93 1 O GLY A 90 N GLU A 55
SHEET 5 AA1 5 VAL A 96 PRO A 101 -1 O LYS A 98 N VAL A 91
SHEET 1 AA2 4 ARG A 59 LYS A 60 0
SHEET 2 AA2 4 ILE A 66 VAL A 68 -1 O TYR A 67 N ARG A 59
SHEET 3 AA2 4 TYR A 113 ALA A 115 -1 O ALA A 115 N ILE A 66
SHEET 4 AA2 4 ARG A 106 ARG A 107 -1 N ARG A 106 O VAL A 114
SHEET 1 AA3 5 ALA B 25 ARG B 28 0
SHEET 2 AA3 5 ILE B 43 LYS B 47 -1 O LEU B 46 N ALA B 25
SHEET 3 AA3 5 VAL B 50 GLU B 55 -1 O ILE B 52 N ALA B 45
SHEET 4 AA3 5 SER B 86 LYS B 93 1 O GLY B 90 N GLU B 55
SHEET 5 AA3 5 VAL B 96 PRO B 101 -1 O LYS B 98 N VAL B 91
SHEET 1 AA4 4 ARG B 59 LYS B 60 0
SHEET 2 AA4 4 ILE B 66 VAL B 68 -1 O TYR B 67 N ARG B 59
SHEET 3 AA4 4 TYR B 113 VAL B 114 -1 O TYR B 113 N VAL B 68
SHEET 4 AA4 4 ARG B 106 ARG B 107 -1 N ARG B 106 O VAL B 114
CRYST1 141.172 141.172 141.172 90.00 90.00 90.00 I 2 3 48
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 0.007084 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007084 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007084 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
