HEADER TRANSFERASE 03-AUG-10 3O8M
TITLE CRYSTAL STRUCTURE OF MONOMERIC KLHXK1 IN CRYSTAL FORM XI WITH GLUCOSE
TITLE 2 BOUND (CLOSED STATE)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEXOKINASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 2.7.1.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;
SOURCE 3 ORGANISM_COMMON: YEAST;
SOURCE 4 ORGANISM_TAXID: 28985;
SOURCE 5 STRAIN: CBS2359/152;
SOURCE 6 GENE: KLLA0D11352G, RAG5;
SOURCE 7 EXPRESSION_SYSTEM: KLUYVEROMYCES LACTIS;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 28985;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: JA6-DELTA-RAG5;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PTS32X;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PTSRAG5
KEYWDS RNASEH-LIKE FOLD, HEXOKINASE, GLYCOLYSIS, GLUCOSE REPRESSION, ATP
KEYWDS 2 BINDING, MIG1 BINDING, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.B.KUETTNER,K.KETTNER,A.KEIM,T.M.KRIEGEL,N.STRATER
REVDAT 5 06-SEP-23 3O8M 1 HETSYN
REVDAT 4 29-JUL-20 3O8M 1 COMPND REMARK HETNAM SITE
REVDAT 3 08-NOV-17 3O8M 1 REMARK
REVDAT 2 29-DEC-10 3O8M 1 JRNL
REVDAT 1 13-OCT-10 3O8M 0
JRNL AUTH E.B.KUETTNER,K.KETTNER,A.KEIM,D.I.SVERGUN,D.VOLKE,D.SINGER,
JRNL AUTH 2 R.HOFFMANN,E.C.MULLER,A.OTTO,T.M.KRIEGEL,N.STRATER
JRNL TITL CRYSTAL STRUCTURE OF HEXOKINASE KLHXK1 OF KLUYVEROMYCES
JRNL TITL 2 LACTIS: A MOLECULAR BASIS FOR UNDERSTANDING THE CONTROL OF
JRNL TITL 3 YEAST HEXOKINASE FUNCTIONS VIA COVALENT MODIFICATION AND
JRNL TITL 4 OLIGOMERIZATION.
JRNL REF J.BIOL.CHEM. V. 285 41019 2010
JRNL REFN ISSN 0021-9258
JRNL PMID 20943665
JRNL DOI 10.1074/JBC.M110.185850
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH E.B.KUETTNER,T.M.KRIEGEL,A.KEIM,M.NAUMANN,N.STRATER
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY DIFFRACTION STUDIES OF
REMARK 1 TITL 2 HEXOKINASE KLHXK1 FROM KLUYVEROMYCES LACTIS
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.F V. 63 430 2007
REMARK 1 REFN ESSN 1744-3091
REMARK 1 PMID 17565189
REMARK 2
REMARK 2 RESOLUTION. 1.42 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.42
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.70
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.2
REMARK 3 NUMBER OF REFLECTIONS : 91406
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) : 0.187
REMARK 3 R VALUE (WORKING SET) : 0.187
REMARK 3 FREE R VALUE : 0.216
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.500
REMARK 3 FREE R VALUE TEST SET COUNT : 1367
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.42
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.46
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5037
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 72.78
REMARK 3 BIN R VALUE (WORKING SET) : 0.2570
REMARK 3 BIN FREE R VALUE SET COUNT : 91
REMARK 3 BIN FREE R VALUE : 0.2680
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3669
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 28
REMARK 3 SOLVENT ATOMS : 611
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 23.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.35000
REMARK 3 B22 (A**2) : -0.99000
REMARK 3 B33 (A**2) : 1.34000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.068
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.051
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.865
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.963
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.961
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3832 ; 0.028 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5188 ; 2.313 ; 1.983
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 473 ; 6.565 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 172 ;36.218 ;25.116
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 692 ;12.534 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 18 ;16.890 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 584 ; 0.163 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2858 ; 0.015 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2344 ; 1.679 ; 3.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3811 ; 2.224 ; 4.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1488 ; 3.257 ; 6.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1374 ; 4.365 ; 9.000
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 14 A 119
REMARK 3 ORIGIN FOR THE GROUP (A): 35.0183 46.4389 18.4213
REMARK 3 T TENSOR
REMARK 3 T11: 0.0790 T22: 0.0467
REMARK 3 T33: 0.0648 T12: 0.0168
REMARK 3 T13: 0.0045 T23: 0.0061
REMARK 3 L TENSOR
REMARK 3 L11: 1.2415 L22: 0.6789
REMARK 3 L33: 0.5067 L12: 0.3587
REMARK 3 L13: 0.1699 L23: 0.0026
REMARK 3 S TENSOR
REMARK 3 S11: -0.0208 S12: 0.0785 S13: 0.0377
REMARK 3 S21: -0.0756 S22: -0.0143 S23: 0.0286
REMARK 3 S31: 0.0154 S32: 0.0166 S33: 0.0351
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 120 A 281
REMARK 3 ORIGIN FOR THE GROUP (A): 46.2385 42.0389 25.4846
REMARK 3 T TENSOR
REMARK 3 T11: 0.0230 T22: 0.0337
REMARK 3 T33: 0.0340 T12: 0.0009
REMARK 3 T13: -0.0074 T23: 0.0215
REMARK 3 L TENSOR
REMARK 3 L11: 1.4441 L22: 1.1585
REMARK 3 L33: 0.6018 L12: 0.1435
REMARK 3 L13: -0.0817 L23: 0.0362
REMARK 3 S TENSOR
REMARK 3 S11: 0.0139 S12: -0.1196 S13: -0.0918
REMARK 3 S21: 0.0708 S22: -0.0304 S23: -0.1566
REMARK 3 S31: 0.0405 S32: 0.0946 S33: 0.0165
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 282 A 391
REMARK 3 ORIGIN FOR THE GROUP (A): 26.1134 37.5869 0.0994
REMARK 3 T TENSOR
REMARK 3 T11: 0.1104 T22: 0.0424
REMARK 3 T33: 0.0586 T12: 0.0002
REMARK 3 T13: -0.0114 T23: -0.0048
REMARK 3 L TENSOR
REMARK 3 L11: 0.8692 L22: 0.6903
REMARK 3 L33: 2.7823 L12: -0.2716
REMARK 3 L13: 0.8517 L23: -0.9076
REMARK 3 S TENSOR
REMARK 3 S11: 0.0301 S12: 0.1583 S13: -0.0489
REMARK 3 S21: -0.2619 S22: -0.0273 S23: 0.0189
REMARK 3 S31: 0.2337 S32: 0.0718 S33: -0.0028
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 392 A 485
REMARK 3 ORIGIN FOR THE GROUP (A): 33.4125 55.0182 23.1446
REMARK 3 T TENSOR
REMARK 3 T11: 0.0369 T22: 0.0098
REMARK 3 T33: 0.0340 T12: -0.0073
REMARK 3 T13: 0.0053 T23: -0.0116
REMARK 3 L TENSOR
REMARK 3 L11: 2.2412 L22: 1.0591
REMARK 3 L33: 0.8004 L12: -0.0126
REMARK 3 L13: 0.2790 L23: 0.2093
REMARK 3 S TENSOR
REMARK 3 S11: 0.0107 S12: -0.0500 S13: 0.1738
REMARK 3 S21: -0.0192 S22: -0.0705 S23: 0.0348
REMARK 3 S31: -0.1131 S32: -0.0228 S33: 0.0598
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS. FULL B FACTORS AND ANISO RECORDS WERE COMPUTED BY
REMARK 3 CCP4 PROGRAMM TLSANL.
REMARK 4
REMARK 4 3O8M COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-AUG-10.
REMARK 100 THE DEPOSITION ID IS D_1000060802.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JUL-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91841
REMARK 200 MONOCHROMATOR : SI-111 CRYSTAL
REMARK 200 OPTICS : 1ST MIRROR: SILICON, ACTIVE
REMARK 200 SURFACE 50 NM RH-COATED, 2ND
REMARK 200 MIRROR: GLAS, ACTIVE SURFACE 50
REMARK 200 NM RH-COATED
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 92838
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.420
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.2
REMARK 200 DATA REDUNDANCY : 7.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.42
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.46
REMARK 200 COMPLETENESS FOR SHELL (%) : 72.7
REMARK 200 DATA REDUNDANCY IN SHELL : 4.10
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.49100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 3O08
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.92
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2MICROL RESERVOIR + 0.2MICROL
REMARK 280 PROTEIN, RESERVOIR: 20% PEG6000, 1M LICL, 0.1M HEPES PH 7.0,
REMARK 280 PROTEIN: 6.6MG/ML KLHXK1, 10MM TRIS PH 7.4, 1MM EDTA, 1MM DTT,
REMARK 280 0.5MM PMSF, 10MM AMPPNP, 10MM GLUCOSE, 10MM MGCL2, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 292K
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 32.28750
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 51.92850
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.79950
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 51.92850
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 32.28750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 37.79950
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 VAL A 2
REMARK 465 ARG A 3
REMARK 465 LEU A 4
REMARK 465 GLY A 5
REMARK 465 PRO A 6
REMARK 465 LYS A 7
REMARK 465 LYS A 8
REMARK 465 PRO A 9
REMARK 465 PRO A 10
REMARK 465 ALA A 11
REMARK 465 ARG A 12
REMARK 465 LYS A 13
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 GLU A 275 CG GLU A 275 CD 0.106
REMARK 500 GLU A 428 CG GLU A 428 CD 0.159
REMARK 500 GLU A 428 CD GLU A 428 OE2 0.137
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 81 CB - CG - OD1 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ARG A 172 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG A 281 CG - CD - NE ANGL. DEV. = 16.8 DEGREES
REMARK 500 ASP A 289 CB - CG - OD2 ANGL. DEV. = -8.3 DEGREES
REMARK 500 ARG A 294 NE - CZ - NH2 ANGL. DEV. = 3.9 DEGREES
REMARK 500 TYR A 307 CB - CG - CD2 ANGL. DEV. = -4.7 DEGREES
REMARK 500 ASP A 319 CB - CG - OD1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ASP A 352 CB - CG - OD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 ASP A 359 CB - CG - OD2 ANGL. DEV. = 7.7 DEGREES
REMARK 500 ARG A 381 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ASP A 404 CB - CG - OD2 ANGL. DEV. = -6.7 DEGREES
REMARK 500 ARG A 406 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 ASP A 416 CB - CG - OD1 ANGL. DEV. = 7.2 DEGREES
REMARK 500 GLU A 428 OE1 - CD - OE2 ANGL. DEV. = -7.4 DEGREES
REMARK 500 GLU A 428 CG - CD - OE1 ANGL. DEV. = -16.0 DEGREES
REMARK 500 GLU A 428 CG - CD - OE2 ANGL. DEV. = 23.5 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 157 48.65 -83.74
REMARK 500 ASN A 166 42.56 -98.83
REMARK 500 ASP A 178 53.10 -158.66
REMARK 500 PRO A 223 1.65 -67.40
REMARK 500 VAL A 278 -32.13 -136.66
REMARK 500 VAL A 278 -31.67 -137.05
REMARK 500 ALA A 411 144.05 -170.73
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3O08 RELATED DB: PDB
REMARK 900 CRYSTAL FORM I OF KLHXK1 (DIMER)
REMARK 900 RELATED ID: 3O1B RELATED DB: PDB
REMARK 900 CRYSTAL FORM II OF KLHXK1 (DIMER)
REMARK 900 RELATED ID: 3O1W RELATED DB: PDB
REMARK 900 CRYSTAL FORM III OF KLHXK1 (DIMER)
REMARK 900 RELATED ID: 3O4W RELATED DB: PDB
REMARK 900 CRYSTAL FORM IV OF KLHXK1 (DIMER)
REMARK 900 RELATED ID: 3O5B RELATED DB: PDB
REMARK 900 CRYSTAL FORM VII OF KLHXK1 (DIMER) WITH GLUCOSE BOUND
REMARK 900 RELATED ID: 3O6W RELATED DB: PDB
REMARK 900 CRYSTAL FORM VIII OF KLHXK1 (MONOMER)
REMARK 900 RELATED ID: 3O80 RELATED DB: PDB
REMARK 900 CRYSTAL FORM IX OF KLHXK1 (MONOMER)
DBREF 3O8M A 1 485 UNP P33284 HXK_KLULA 1 485
SEQRES 1 A 485 MET VAL ARG LEU GLY PRO LYS LYS PRO PRO ALA ARG LYS
SEQRES 2 A 485 GLY SER MET ALA ASP VAL PRO ALA ASN LEU MET GLU GLN
SEQRES 3 A 485 ILE HIS GLY LEU GLU THR LEU PHE THR VAL SER SER GLU
SEQRES 4 A 485 LYS MET ARG SER ILE VAL LYS HIS PHE ILE SER GLU LEU
SEQRES 5 A 485 ASP LYS GLY LEU SER LYS LYS GLY GLY ASN ILE PRO MET
SEQRES 6 A 485 ILE PRO GLY TRP VAL VAL GLU TYR PRO THR GLY LYS GLU
SEQRES 7 A 485 THR GLY ASP PHE LEU ALA LEU ASP LEU GLY GLY THR ASN
SEQRES 8 A 485 LEU ARG VAL VAL LEU VAL LYS LEU GLY GLY ASN HIS ASP
SEQRES 9 A 485 PHE ASP THR THR GLN ASN LYS TYR ARG LEU PRO ASP HIS
SEQRES 10 A 485 LEU ARG THR GLY THR SER GLU GLN LEU TRP SER PHE ILE
SEQRES 11 A 485 ALA LYS CYS LEU LYS GLU PHE VAL ASP GLU TRP TYR PRO
SEQRES 12 A 485 ASP GLY VAL SER GLU PRO LEU PRO LEU GLY PHE THR PHE
SEQRES 13 A 485 SER TYR PRO ALA SER GLN LYS LYS ILE ASN SER GLY VAL
SEQRES 14 A 485 LEU GLN ARG TRP THR LYS GLY PHE ASP ILE GLU GLY VAL
SEQRES 15 A 485 GLU GLY HIS ASP VAL VAL PRO MET LEU GLN GLU GLN ILE
SEQRES 16 A 485 GLU LYS LEU ASN ILE PRO ILE ASN VAL VAL ALA LEU ILE
SEQRES 17 A 485 ASN ASP THR THR GLY THR LEU VAL ALA SER LEU TYR THR
SEQRES 18 A 485 ASP PRO GLN THR LYS MET GLY ILE ILE ILE GLY THR GLY
SEQRES 19 A 485 VAL ASN GLY ALA TYR TYR ASP VAL VAL SER GLY ILE GLU
SEQRES 20 A 485 LYS LEU GLU GLY LEU LEU PRO GLU ASP ILE GLY PRO ASP
SEQRES 21 A 485 SER PRO MET ALA ILE ASN CYS GLU TYR GLY SER PHE ASP
SEQRES 22 A 485 ASN GLU HIS LEU VAL LEU PRO ARG THR LYS TYR ASP VAL
SEQRES 23 A 485 ILE ILE ASP GLU GLU SER PRO ARG PRO GLY GLN GLN ALA
SEQRES 24 A 485 PHE GLU LYS MET THR SER GLY TYR TYR LEU GLY GLU ILE
SEQRES 25 A 485 MET ARG LEU VAL LEU LEU ASP LEU TYR ASP SER GLY PHE
SEQRES 26 A 485 ILE PHE LYS ASP GLN ASP ILE SER LYS LEU LYS GLU ALA
SEQRES 27 A 485 TYR VAL MET ASP THR SER TYR PRO SER LYS ILE GLU ASP
SEQRES 28 A 485 ASP PRO PHE GLU ASN LEU GLU ASP THR ASP ASP LEU PHE
SEQRES 29 A 485 LYS THR ASN LEU ASN ILE GLU THR THR VAL VAL GLU ARG
SEQRES 30 A 485 LYS LEU ILE ARG LYS LEU ALA GLU LEU VAL GLY THR ARG
SEQRES 31 A 485 ALA ALA ARG LEU THR VAL CYS GLY VAL SER ALA ILE CYS
SEQRES 32 A 485 ASP LYS ARG GLY TYR LYS THR ALA HIS ILE ALA ALA ASP
SEQRES 33 A 485 GLY SER VAL PHE ASN ARG TYR PRO GLY TYR LYS GLU LYS
SEQRES 34 A 485 ALA ALA GLN ALA LEU LYS ASP ILE TYR ASN TRP ASP VAL
SEQRES 35 A 485 GLU LYS MET GLU ASP HIS PRO ILE GLN LEU VAL ALA ALA
SEQRES 36 A 485 GLU ASP GLY SER GLY VAL GLY ALA ALA ILE ILE ALA CYS
SEQRES 37 A 485 LEU THR GLN LYS ARG LEU ALA ALA GLY LYS SER VAL GLY
SEQRES 38 A 485 ILE LYS GLY GLU
HET GLC A 486 12
HET BGC A 487 12
HET CL A 488 1
HET CL A 489 1
HET CL A 490 1
HET CL A 491 1
HETNAM GLC ALPHA-D-GLUCOPYRANOSE
HETNAM BGC BETA-D-GLUCOPYRANOSE
HETNAM CL CHLORIDE ION
HETSYN GLC ALPHA-D-GLUCOSE; D-GLUCOSE; GLUCOSE
HETSYN BGC BETA-D-GLUCOSE; D-GLUCOSE; GLUCOSE
FORMUL 2 GLC C6 H12 O6
FORMUL 3 BGC C6 H12 O6
FORMUL 4 CL 4(CL 1-)
FORMUL 8 HOH *611(H2 O)
HELIX 1 1 PRO A 20 THR A 35 1 16
HELIX 2 2 SER A 37 SER A 57 1 21
HELIX 3 3 HIS A 117 GLY A 121 5 5
HELIX 4 4 THR A 122 TYR A 142 1 21
HELIX 5 5 ASP A 186 LEU A 198 1 13
HELIX 6 6 ASN A 209 ASP A 222 1 14
HELIX 7 7 SER A 244 GLU A 250 5 7
HELIX 8 8 GLU A 268 PHE A 272 5 5
HELIX 9 9 THR A 282 SER A 292 1 11
HELIX 10 10 GLN A 298 SER A 305 1 8
HELIX 11 11 TYR A 308 SER A 323 1 16
HELIX 12 12 ILE A 332 GLU A 337 5 6
HELIX 13 13 THR A 343 ASP A 352 1 10
HELIX 14 14 LEU A 357 ASN A 369 1 13
HELIX 15 15 THR A 373 GLY A 407 1 35
HELIX 16 16 GLY A 417 TYR A 423 1 7
HELIX 17 17 GLY A 425 ASN A 439 1 15
HELIX 18 18 LYS A 444 HIS A 448 5 5
HELIX 19 19 GLY A 460 GLY A 477 1 18
SHEET 1 A 6 ILE A 66 PRO A 67 0
SHEET 2 A 6 PRO A 262 ASN A 266 -1 O ASN A 266 N ILE A 66
SHEET 3 A 6 VAL A 235 VAL A 242 -1 N TYR A 239 O ILE A 265
SHEET 4 A 6 THR A 225 ILE A 231 -1 N GLY A 228 O ALA A 238
SHEET 5 A 6 ALA A 411 ASP A 416 1 O ASP A 416 N ILE A 231
SHEET 6 A 6 ILE A 450 ALA A 454 1 O VAL A 453 N ALA A 415
SHEET 1 B 5 PHE A 105 ARG A 113 0
SHEET 2 B 5 ASN A 91 GLY A 100 -1 N LEU A 96 O THR A 108
SHEET 3 B 5 THR A 79 LEU A 87 -1 N ASP A 86 O ARG A 93
SHEET 4 B 5 LEU A 150 PHE A 156 1 O THR A 155 N LEU A 85
SHEET 5 B 5 ILE A 202 ILE A 208 1 O ALA A 206 N PHE A 154
SHEET 1 C 2 ALA A 160 SER A 161 0
SHEET 2 C 2 VAL A 169 LEU A 170 -1 O VAL A 169 N SER A 161
CRYST1 64.575 75.599 103.857 90.00 90.00 90.00 P 21 21 21 4
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 0.015486 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013228 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009629 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
