HEADER TRANSFERASE 09-OCT-03 1R59
TITLE ENTEROCOCCUS CASSELIFLAVUS GLYCEROL KINASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLYCEROL KINASE;
COMPND 3 CHAIN: O, X;
COMPND 4 FRAGMENT: GLYCEROL KINASE;
COMPND 5 SYNONYM: ATP:GLYCEROL 3-PHOSPHOTRANSFERASE, GLYCEROKINASE, GK;
COMPND 6 EC: 2.7.1.30;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ENTEROCOCCUS CASSELIFLAVUS;
SOURCE 3 ORGANISM_TAXID: 37734;
SOURCE 4 GENE: GLPK;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: JM109DE3;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: POXO4
KEYWDS TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.I.YEH,V.CHARRIER,J.PAULO,L.HOU,E.DARBON,A.CLAIBORNE,W.G.HOL,
AUTHOR 2 J.DEUTSCHER
REVDAT 3 14-FEB-24 1R59 1 REMARK
REVDAT 2 24-FEB-09 1R59 1 VERSN
REVDAT 1 12-OCT-04 1R59 0
JRNL AUTH J.I.YEH,V.CHARRIER,J.PAULO,L.HOU,E.DARBON,A.CLAIBORNE,
JRNL AUTH 2 W.G.HOL,J.DEUTSCHER
JRNL TITL STRUCTURES OF ENTEROCOCCAL GLYCEROL KINASE IN THE ABSENCE
JRNL TITL 2 AND PRESENCE OF GLYCEROL: CORRELATION OF CONFORMATION TO
JRNL TITL 3 SUBSTRATE BINDING AND A MECHANISM OF ACTIVATION BY
JRNL TITL 4 PHOSPHORYLATION
JRNL REF BIOCHEMISTRY V. 43 362 2004
JRNL REFN ISSN 0006-2960
JRNL PMID 14717590
JRNL DOI 10.1021/BI034258O
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 6.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
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 : 29592
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) : 0.221
REMARK 3 FREE R VALUE : 0.243
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 : 7430
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 102
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.70
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) : 0.10
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) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
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) : 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 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 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:
REMARK 3 RESIDUE (O SER 230 ) AND RESIDUE (O VAL 238 ) ARE LINKED TOGETHER.
REMARK 3 RESIDUE (X SER 230 ) AND RESIDUE (X VAL 238 ) ARE LINKED TOGETHE.
REMARK 4
REMARK 4 1R59 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-OCT-03.
REMARK 100 THE DEPOSITION ID IS D_1000020453.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL; NULL
REMARK 200 TEMPERATURE (KELVIN) : 100; NULL
REMARK 200 PH : 5.9
REMARK 200 NUMBER OF CRYSTALS USED : 3
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; NULL
REMARK 200 RADIATION SOURCE : NSLS; NULL
REMARK 200 BEAMLINE : X8C; NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9788, 0.9791, 0.954, 1.0; NULL
REMARK 200 MONOCHROMATOR : GRAPHITE; GRAPHITE
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; NULL
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4; NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40746
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.3
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.07200
REMARK 200 R SYM (I) : 0.04500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.61
REMARK 200 COMPLETENESS FOR SHELL (%) : 74.7
REMARK 200 DATA REDUNDANCY IN SHELL : 4.10
REMARK 200 R MERGE FOR SHELL (I) : 0.27000
REMARK 200 R SYM FOR SHELL (I) : 0.27000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.28
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG400, POTASSIUM PHOSPHATE, 1,10
REMARK 280 -PHENANTHROLINE, PH 5.9, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
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 33.91450
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 100.56000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 53.55500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 100.56000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 33.91450
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 53.55500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: O, X
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 ALA O 2
REMARK 465 GLU O 3
REMARK 465 LYS O 4
REMARK 465 TYR O 231
REMARK 465 HIS O 232
REMARK 465 PHE O 233
REMARK 465 TYR O 234
REMARK 465 GLY O 235
REMARK 465 SER O 236
REMARK 465 GLU O 237
REMARK 465 ALA O 492
REMARK 465 ALA O 493
REMARK 465 THR O 494
REMARK 465 GLN O 495
REMARK 465 THR O 496
REMARK 465 PHE O 497
REMARK 465 LYS O 498
REMARK 465 PHE O 499
REMARK 465 LYS O 500
REMARK 465 ALA O 501
REMARK 465 LYS O 502
REMARK 465 LYS O 503
REMARK 465 GLU O 504
REMARK 465 GLY O 505
REMARK 465 GLU O 506
REMARK 465 ALA X 2
REMARK 465 GLU X 3
REMARK 465 LYS X 4
REMARK 465 TYR X 231
REMARK 465 HIS X 232
REMARK 465 PHE X 233
REMARK 465 TYR X 234
REMARK 465 GLY X 235
REMARK 465 SER X 236
REMARK 465 GLU X 237
REMARK 465 ALA X 492
REMARK 465 ALA X 493
REMARK 465 THR X 494
REMARK 465 GLN X 495
REMARK 465 THR X 496
REMARK 465 PHE X 497
REMARK 465 LYS X 498
REMARK 465 PHE X 499
REMARK 465 LYS X 500
REMARK 465 ALA X 501
REMARK 465 LYS X 502
REMARK 465 LYS X 503
REMARK 465 GLU X 504
REMARK 465 GLY X 505
REMARK 465 GLU X 506
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 ALA X 74 O ILE X 75 1.72
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 O 229 C SER O 230 N 0.158
REMARK 500 SER O 230 N SER O 230 CA 0.165
REMARK 500 SER O 230 CA SER O 230 C 0.226
REMARK 500 SER O 230 C VAL O 238 N 0.235
REMARK 500 VAL O 238 N VAL O 238 CA 0.266
REMARK 500 GLY X 69 CA GLY X 69 C 0.102
REMARK 500 ILE X 70 N ILE X 70 CA 0.138
REMARK 500 PRO X 72 N PRO X 72 CA 0.124
REMARK 500 GLU X 154 C LYS X 155 N 0.298
REMARK 500 THR X 228 C ARG X 229 N -0.224
REMARK 500 SER X 230 CA SER X 230 C 0.181
REMARK 500 SER X 230 C VAL X 238 N 0.196
REMARK 500 VAL X 238 N VAL X 238 CA 0.218
REMARK 500 VAL X 238 CA VAL X 238 C 0.230
REMARK 500 VAL X 238 C PRO X 239 N 0.216
REMARK 500 PRO X 239 N PRO X 239 CA 0.134
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 PRO O 37 C - N - CD ANGL. DEV. = -14.3 DEGREES
REMARK 500 PRO O 37 CA - N - CD ANGL. DEV. = -15.5 DEGREES
REMARK 500 PRO O 41 C - N - CD ANGL. DEV. = -26.1 DEGREES
REMARK 500 PRO O 41 CA - N - CD ANGL. DEV. = -21.5 DEGREES
REMARK 500 PRO O 72 CA - N - CD ANGL. DEV. = -8.9 DEGREES
REMARK 500 PRO O 97 C - N - CD ANGL. DEV. = -14.7 DEGREES
REMARK 500 PRO O 97 CA - N - CD ANGL. DEV. = -24.3 DEGREES
REMARK 500 PRO O 111 CA - N - CD ANGL. DEV. = -24.8 DEGREES
REMARK 500 PRO O 211 C - N - CD ANGL. DEV. = -14.8 DEGREES
REMARK 500 PRO O 211 CA - N - CD ANGL. DEV. = -26.0 DEGREES
REMARK 500 PRO O 216 C - N - CD ANGL. DEV. = -18.3 DEGREES
REMARK 500 PRO O 216 CA - N - CD ANGL. DEV. = -13.8 DEGREES
REMARK 500 ARG O 229 CB - CA - C ANGL. DEV. = 14.7 DEGREES
REMARK 500 SER O 230 C - N - CA ANGL. DEV. = 28.3 DEGREES
REMARK 500 VAL O 238 C - N - CA ANGL. DEV. = 22.1 DEGREES
REMARK 500 VAL O 238 CA - C - N ANGL. DEV. = 18.9 DEGREES
REMARK 500 PRO O 239 CA - N - CD ANGL. DEV. = -30.7 DEGREES
REMARK 500 PRO O 239 CB - CA - C ANGL. DEV. = -14.5 DEGREES
REMARK 500 PRO O 280 C - N - CD ANGL. DEV. = -15.1 DEGREES
REMARK 500 PRO O 280 CA - N - CD ANGL. DEV. = -19.4 DEGREES
REMARK 500 SER O 306 N - CA - C ANGL. DEV. = 16.9 DEGREES
REMARK 500 ILE O 307 N - CA - C ANGL. DEV. = 25.0 DEGREES
REMARK 500 ILE O 307 CA - C - N ANGL. DEV. = -21.6 DEGREES
REMARK 500 ILE O 307 O - C - N ANGL. DEV. = 10.5 DEGREES
REMARK 500 PHE O 308 C - N - CA ANGL. DEV. = 22.1 DEGREES
REMARK 500 PRO O 328 CA - N - CD ANGL. DEV. = -29.5 DEGREES
REMARK 500 PRO O 328 N - CD - CG ANGL. DEV. = 9.8 DEGREES
REMARK 500 PRO O 347 CA - N - CD ANGL. DEV. = -19.1 DEGREES
REMARK 500 PRO O 355 CA - N - CD ANGL. DEV. = -27.7 DEGREES
REMARK 500 TRP O 357 CA - C - N ANGL. DEV. = -13.8 DEGREES
REMARK 500 PRO O 405 C - N - CD ANGL. DEV. = -19.9 DEGREES
REMARK 500 PRO O 405 CA - N - CD ANGL. DEV. = -15.8 DEGREES
REMARK 500 PRO O 473 CA - N - CD ANGL. DEV. = -19.1 DEGREES
REMARK 500 PRO O 476 C - N - CD ANGL. DEV. = -17.2 DEGREES
REMARK 500 PRO O 476 CA - N - CD ANGL. DEV. = -21.0 DEGREES
REMARK 500 ALA X 9 C - N - CA ANGL. DEV. = -17.1 DEGREES
REMARK 500 ILE X 10 C - N - CA ANGL. DEV. = 15.5 DEGREES
REMARK 500 ASN X 25 CA - CB - CG ANGL. DEV. = -13.5 DEGREES
REMARK 500 ASN X 25 N - CA - C ANGL. DEV. = 25.2 DEGREES
REMARK 500 ASN X 25 CA - C - N ANGL. DEV. = -19.9 DEGREES
REMARK 500 ASN X 25 O - C - N ANGL. DEV. = 10.4 DEGREES
REMARK 500 GLY X 26 C - N - CA ANGL. DEV. = 14.5 DEGREES
REMARK 500 SER X 32 N - CA - C ANGL. DEV. = 21.7 DEGREES
REMARK 500 SER X 32 CA - C - N ANGL. DEV. = -15.6 DEGREES
REMARK 500 GLN X 33 C - N - CA ANGL. DEV. = 16.5 DEGREES
REMARK 500 GLN X 33 N - CA - C ANGL. DEV. = 18.4 DEGREES
REMARK 500 PRO X 37 C - N - CD ANGL. DEV. = -16.5 DEGREES
REMARK 500 PRO X 37 CA - N - CD ANGL. DEV. = -15.2 DEGREES
REMARK 500 PRO X 41 C - N - CD ANGL. DEV. = -24.1 DEGREES
REMARK 500 PRO X 41 CA - N - CD ANGL. DEV. = -12.9 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 92 ANGLE DEVIATIONS.
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 ALA O 19 85.91 -158.77
REMARK 500 ASP O 23 -157.24 -85.06
REMARK 500 ASN O 25 93.49 71.26
REMARK 500 SER O 43 -49.57 -1.88
REMARK 500 ASN O 51 37.58 -69.38
REMARK 500 GLU O 52 45.10 -174.53
REMARK 500 TRP O 54 -71.71 -87.13
REMARK 500 ASN O 55 -40.03 -28.34
REMARK 500 SER O 56 27.71 -67.76
REMARK 500 VAL O 57 -49.69 -132.50
REMARK 500 SER O 68 -35.40 -133.47
REMARK 500 PRO O 72 -14.21 -39.30
REMARK 500 GLU O 85 -15.47 65.09
REMARK 500 LYS O 92 -38.65 83.64
REMARK 500 THR O 94 -127.60 -153.86
REMARK 500 ALA O 99 -96.82 -161.53
REMARK 500 ASN O 100 166.08 171.54
REMARK 500 TRP O 104 7.33 -63.37
REMARK 500 LEU O 131 -154.55 -96.79
REMARK 500 TRP O 144 32.53 -76.29
REMARK 500 LEU O 145 -58.33 -120.85
REMARK 500 ALA O 152 -31.87 85.09
REMARK 500 GLU O 160 -70.10 -92.57
REMARK 500 THR O 165 -164.96 -72.11
REMARK 500 LEU O 174 18.33 -65.46
REMARK 500 ASP O 176 51.86 -69.92
REMARK 500 GLN O 178 -85.87 -87.67
REMARK 500 MET O 214 -93.60 -87.93
REMARK 500 LEU O 215 130.70 -21.18
REMARK 500 LYS O 219 -165.30 -109.19
REMARK 500 ARG O 229 38.89 -80.88
REMARK 500 SER O 230 -91.02 -116.02
REMARK 500 VAL O 238 -132.11 -175.61
REMARK 500 ALA O 244 173.97 174.62
REMARK 500 ALA O 256 -86.96 -88.55
REMARK 500 PHE O 257 109.95 6.40
REMARK 500 GLU O 258 152.34 148.86
REMARK 500 TYR O 266 63.68 -107.92
REMARK 500 ASN O 296 -67.27 -94.55
REMARK 500 SER O 306 -85.15 -137.20
REMARK 500 PHE O 308 -65.83 -10.75
REMARK 500 ALA O 310 -56.75 -153.17
REMARK 500 GLU O 325 -39.24 67.15
REMARK 500 LYS O 338 -27.55 67.05
REMARK 500 PRO O 347 43.33 -63.41
REMARK 500 ALA O 348 45.10 -91.66
REMARK 500 ALA O 354 -147.40 66.89
REMARK 500 TRP O 357 121.52 -9.69
REMARK 500 ASP O 358 -149.60 -122.79
REMARK 500 SER O 359 -12.51 -149.64
REMARK 500
REMARK 500 THIS ENTRY HAS 153 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR X 266 0.07 SIDE CHAIN
REMARK 500 TYR X 446 0.07 SIDE CHAIN
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 GLU X 154 -17.06
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1R5F RELATED DB: PDB
REMARK 900 ENTEROCOCCUS CASSELIFLAVUS GLYCEROL KINASE COMPLEXED WITH GLYCEROL
DBREF 1R59 O 2 506 UNP O34153 GLPK_ENTCA 1 505
DBREF 1R59 X 2 506 UNP O34153 GLPK_ENTCA 1 505
SEQRES 1 O 505 ALA GLU LYS ASN TYR VAL MET ALA ILE ASP GLN GLY THR
SEQRES 2 O 505 THR SER SER ARG ALA ILE ILE PHE ASP ARG ASN GLY LYS
SEQRES 3 O 505 LYS ILE GLY SER SER GLN LYS GLU PHE PRO GLN TYR PHE
SEQRES 4 O 505 PRO LYS SER GLY TRP VAL GLU HIS ASN ALA ASN GLU ILE
SEQRES 5 O 505 TRP ASN SER VAL GLN SER VAL ILE ALA GLY ALA PHE ILE
SEQRES 6 O 505 GLU SER GLY ILE ARG PRO GLU ALA ILE ALA GLY ILE GLY
SEQRES 7 O 505 ILE THR ASN GLN ARG GLU THR THR VAL VAL TRP ASP LYS
SEQRES 8 O 505 THR THR GLY GLN PRO ILE ALA ASN ALA ILE VAL TRP GLN
SEQRES 9 O 505 SER ARG GLN SER SER PRO ILE ALA ASP GLN LEU LYS VAL
SEQRES 10 O 505 ASP GLY HIS THR GLU MET ILE HIS GLU LYS THR GLY LEU
SEQRES 11 O 505 VAL ILE ASP ALA TYR PHE SER ALA THR LYS VAL ARG TRP
SEQRES 12 O 505 LEU LEU ASP ASN ILE GLU GLY ALA GLN GLU LYS ALA ASP
SEQRES 13 O 505 ASN GLY GLU LEU LEU PHE GLY THR ILE ASP SER TRP LEU
SEQRES 14 O 505 VAL TRP LYS LEU THR ASP GLY GLN VAL HIS VAL THR ASP
SEQRES 15 O 505 TYR SER ASN ALA SER ARG THR MET LEU TYR ASN ILE HIS
SEQRES 16 O 505 LYS LEU GLU TRP ASP GLN GLU ILE LEU ASP LEU LEU ASN
SEQRES 17 O 505 ILE PRO SER SER MET LEU PRO GLU VAL LYS SER ASN SER
SEQRES 18 O 505 GLU VAL TYR GLY HIS THR ARG SER TYR HIS PHE TYR GLY
SEQRES 19 O 505 SER GLU VAL PRO ILE ALA GLY MET ALA GLY ASP GLN GLN
SEQRES 20 O 505 ALA ALA LEU PHE GLY GLN MET ALA PHE GLU LYS GLY MET
SEQRES 21 O 505 ILE LYS ASN THR TYR GLY THR GLY ALA PHE ILE VAL MET
SEQRES 22 O 505 ASN THR GLY GLU GLU PRO GLN LEU SER ASP ASN ASP LEU
SEQRES 23 O 505 LEU THR THR ILE GLY TYR GLY ILE ASN GLY LYS VAL TYR
SEQRES 24 O 505 TYR ALA LEU GLU GLY SER ILE PHE VAL ALA GLY SER ALA
SEQRES 25 O 505 ILE GLN TRP LEU ARG ASP GLY LEU ARG MET ILE GLU THR
SEQRES 26 O 505 SER PRO GLN SER GLU GLU LEU ALA ALA LYS ALA LYS GLY
SEQRES 27 O 505 ASP ASN GLU VAL TYR VAL VAL PRO ALA PHE THR GLY LEU
SEQRES 28 O 505 GLY ALA PRO TYR TRP ASP SER GLU ALA ARG GLY ALA VAL
SEQRES 29 O 505 PHE GLY LEU THR ARG GLY THR THR LYS GLU ASP PHE VAL
SEQRES 30 O 505 ARG ALA THR LEU GLN ALA VAL ALA TYR GLN SER LYS ASP
SEQRES 31 O 505 VAL ILE ASP THR MET LYS LYS ASP SER GLY ILE ASP ILE
SEQRES 32 O 505 PRO LEU LEU LYS VAL ASP GLY GLY ALA ALA LYS ASN ASP
SEQRES 33 O 505 LEU LEU MET GLN PHE GLN ALA ASP ILE LEU ASP ILE ASP
SEQRES 34 O 505 VAL GLN ARG ALA ALA ASN LEU GLU THR THR ALA LEU GLY
SEQRES 35 O 505 ALA ALA TYR LEU ALA GLY LEU ALA VAL GLY PHE TRP LYS
SEQRES 36 O 505 ASP LEU ASP GLU LEU LYS SER MET ALA GLU GLU GLY GLN
SEQRES 37 O 505 MET PHE THR PRO GLU MET PRO ALA GLU GLU ARG ASP ASN
SEQRES 38 O 505 LEU TYR GLU GLY TRP LYS GLN ALA VAL ALA ALA THR GLN
SEQRES 39 O 505 THR PHE LYS PHE LYS ALA LYS LYS GLU GLY GLU
SEQRES 1 X 505 ALA GLU LYS ASN TYR VAL MET ALA ILE ASP GLN GLY THR
SEQRES 2 X 505 THR SER SER ARG ALA ILE ILE PHE ASP ARG ASN GLY LYS
SEQRES 3 X 505 LYS ILE GLY SER SER GLN LYS GLU PHE PRO GLN TYR PHE
SEQRES 4 X 505 PRO LYS SER GLY TRP VAL GLU HIS ASN ALA ASN GLU ILE
SEQRES 5 X 505 TRP ASN SER VAL GLN SER VAL ILE ALA GLY ALA PHE ILE
SEQRES 6 X 505 GLU SER GLY ILE ARG PRO GLU ALA ILE ALA GLY ILE GLY
SEQRES 7 X 505 ILE THR ASN GLN ARG GLU THR THR VAL VAL TRP ASP LYS
SEQRES 8 X 505 THR THR GLY GLN PRO ILE ALA ASN ALA ILE VAL TRP GLN
SEQRES 9 X 505 SER ARG GLN SER SER PRO ILE ALA ASP GLN LEU LYS VAL
SEQRES 10 X 505 ASP GLY HIS THR GLU MET ILE HIS GLU LYS THR GLY LEU
SEQRES 11 X 505 VAL ILE ASP ALA TYR PHE SER ALA THR LYS VAL ARG TRP
SEQRES 12 X 505 LEU LEU ASP ASN ILE GLU GLY ALA GLN GLU LYS ALA ASP
SEQRES 13 X 505 ASN GLY GLU LEU LEU PHE GLY THR ILE ASP SER TRP LEU
SEQRES 14 X 505 VAL TRP LYS LEU THR ASP GLY GLN VAL HIS VAL THR ASP
SEQRES 15 X 505 TYR SER ASN ALA SER ARG THR MET LEU TYR ASN ILE HIS
SEQRES 16 X 505 LYS LEU GLU TRP ASP GLN GLU ILE LEU ASP LEU LEU ASN
SEQRES 17 X 505 ILE PRO SER SER MET LEU PRO GLU VAL LYS SER ASN SER
SEQRES 18 X 505 GLU VAL TYR GLY HIS THR ARG SER TYR HIS PHE TYR GLY
SEQRES 19 X 505 SER GLU VAL PRO ILE ALA GLY MET ALA GLY ASP GLN GLN
SEQRES 20 X 505 ALA ALA LEU PHE GLY GLN MET ALA PHE GLU LYS GLY MET
SEQRES 21 X 505 ILE LYS ASN THR TYR GLY THR GLY ALA PHE ILE VAL MET
SEQRES 22 X 505 ASN THR GLY GLU GLU PRO GLN LEU SER ASP ASN ASP LEU
SEQRES 23 X 505 LEU THR THR ILE GLY TYR GLY ILE ASN GLY LYS VAL TYR
SEQRES 24 X 505 TYR ALA LEU GLU GLY SER ILE PHE VAL ALA GLY SER ALA
SEQRES 25 X 505 ILE GLN TRP LEU ARG ASP GLY LEU ARG MET ILE GLU THR
SEQRES 26 X 505 SER PRO GLN SER GLU GLU LEU ALA ALA LYS ALA LYS GLY
SEQRES 27 X 505 ASP ASN GLU VAL TYR VAL VAL PRO ALA PHE THR GLY LEU
SEQRES 28 X 505 GLY ALA PRO TYR TRP ASP SER GLU ALA ARG GLY ALA VAL
SEQRES 29 X 505 PHE GLY LEU THR ARG GLY THR THR LYS GLU ASP PHE VAL
SEQRES 30 X 505 ARG ALA THR LEU GLN ALA VAL ALA TYR GLN SER LYS ASP
SEQRES 31 X 505 VAL ILE ASP THR MET LYS LYS ASP SER GLY ILE ASP ILE
SEQRES 32 X 505 PRO LEU LEU LYS VAL ASP GLY GLY ALA ALA LYS ASN ASP
SEQRES 33 X 505 LEU LEU MET GLN PHE GLN ALA ASP ILE LEU ASP ILE ASP
SEQRES 34 X 505 VAL GLN ARG ALA ALA ASN LEU GLU THR THR ALA LEU GLY
SEQRES 35 X 505 ALA ALA TYR LEU ALA GLY LEU ALA VAL GLY PHE TRP LYS
SEQRES 36 X 505 ASP LEU ASP GLU LEU LYS SER MET ALA GLU GLU GLY GLN
SEQRES 37 X 505 MET PHE THR PRO GLU MET PRO ALA GLU GLU ARG ASP ASN
SEQRES 38 X 505 LEU TYR GLU GLY TRP LYS GLN ALA VAL ALA ALA THR GLN
SEQRES 39 X 505 THR PHE LYS PHE LYS ALA LYS LYS GLU GLY GLU
FORMUL 3 HOH *102(H2 O)
HELIX 1 1 ASN O 49 ILE O 53 5 5
HELIX 2 2 ILE O 61 ILE O 66 1 6
HELIX 3 3 SER O 110 GLY O 120 1 11
HELIX 4 4 HIS O 121 HIS O 126 1 6
HELIX 5 5 PHE O 137 VAL O 142 1 6
HELIX 6 6 VAL O 142 ASP O 147 1 6
HELIX 7 7 THR O 165 LYS O 173 1 9
HELIX 8 8 ASP O 183 SER O 188 1 6
HELIX 9 9 ASP O 201 ASP O 206 1 6
HELIX 10 10 ALA O 249 GLN O 254 1 6
HELIX 11 11 GLY O 311 LEU O 317 1 7
HELIX 12 12 THR O 326 GLU O 331 5 6
HELIX 13 13 THR O 373 GLY O 401 1 29
HELIX 14 14 ASN O 416 ASP O 428 1 13
HELIX 15 15 ALA O 441 GLY O 453 1 13
HELIX 16 16 LEU O 461 ALA O 465 5 5
HELIX 17 17 GLU O 479 GLU O 485 1 7
HELIX 18 18 ALA X 50 PHE X 65 1 16
HELIX 19 19 ASP X 114 GLY X 120 1 7
HELIX 20 20 HIS X 121 HIS X 126 1 6
HELIX 21 21 SER X 138 ILE X 149 1 12
HELIX 22 22 ILE X 166 LYS X 173 1 8
HELIX 23 23 ASN X 186 THR X 190 5 5
HELIX 24 24 ASP X 201 LEU X 208 1 8
HELIX 25 25 ASP X 376 THR X 381 1 6
HELIX 26 26 TYR X 387 ASP X 394 1 8
HELIX 27 27 GLY X 411 LYS X 415 5 5
HELIX 28 28 LEU X 418 PHE X 422 5 5
HELIX 29 29 TYR X 446 LEU X 450 5 5
HELIX 30 30 ASP X 481 GLY X 486 1 6
HELIX 31 31 TRP X 487 ALA X 490 5 4
SHEET 1 A 4 ILE O 21 PHE O 22 0
SHEET 2 A 4 TYR O 6 ILE O 10 -1 N VAL O 7 O PHE O 22
SHEET 3 A 4 ILE O 75 ILE O 80 1 O ALA O 76 N TYR O 6
SHEET 4 A 4 ILE O 240 MET O 243 1 O GLY O 242 N ILE O 80
SHEET 1 B 2 VAL O 181 THR O 182 0
SHEET 2 B 2 GLU O 217 VAL O 218 1 O GLU O 217 N THR O 182
SHEET 1 C 5 ALA O 270 PHE O 271 0
SHEET 2 C 5 THR O 265 TYR O 266 -1 N THR O 265 O PHE O 271
SHEET 3 C 5 LEU O 406 GLY O 411 1 O ASP O 410 N TYR O 266
SHEET 4 C 5 ASP O 430 ALA O 434 1 O GLN O 432 N VAL O 409
SHEET 5 C 5 GLU O 467 PHE O 471 -1 O PHE O 471 N VAL O 431
SHEET 1 D 3 VAL O 273 ASN O 275 0
SHEET 2 D 3 TYR O 301 GLU O 304 -1 O LEU O 303 N MET O 274
SHEET 3 D 3 LEU O 288 ILE O 291 -1 N THR O 290 O ALA O 302
SHEET 1 E 2 TYR O 344 VAL O 346 0
SHEET 2 E 2 ALA O 364 PHE O 366 -1 O PHE O 366 N TYR O 344
SHEET 1 F 2 GLU X 47 HIS X 48 0
SHEET 2 F 2 ALA X 101 ILE X 102 -1 O ALA X 101 N HIS X 48
SHEET 1 G 2 TRP X 90 ASP X 91 0
SHEET 2 G 2 LEU X 161 LEU X 162 -1 O LEU X 162 N TRP X 90
SHEET 1 H 2 VAL X 181 THR X 182 0
SHEET 2 H 2 GLU X 217 VAL X 218 1 O GLU X 217 N THR X 182
SHEET 1 I 4 MET X 261 ILE X 262 0
SHEET 2 I 4 VAL X 273 ASN X 275 -1 O ASN X 275 N MET X 261
SHEET 3 I 4 ALA X 302 GLU X 304 -1 N LEU X 303 O MET X 274
SHEET 4 I 4 LEU X 288 THR X 290 -1 N THR X 290 O ALA X 302
SHEET 1 J 2 ASN X 264 THR X 265 0
SHEET 2 J 2 VAL X 409 ASP X 410 1 O ASP X 410 N ASN X 264
CRYST1 67.829 107.110 201.120 90.00 90.00 90.00 P 21 21 21 8
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 0.014743 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009336 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004972 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
