HEADER TRANSFERASE 19-MAR-09 3A0I
TITLE HUMAN GLUCOKINASE IN COMPLEX WITH A SYNTHETIC ACTIVATOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUCOKINASE;
COMPND 3 CHAIN: X;
COMPND 4 FRAGMENT: ENZYME, UNP RESIDUES 12-466;
COMPND 5 SYNONYM: HUMAN HEPATIC GLUCOKINASE, HEXOKINASE TYPE IV, HK IV,
COMPND 6 HEXOKINASE-4, HK4, HEXOKINASE-D;
COMPND 7 EC: 2.7.1.2;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: DH5ALFA;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PFLAG-CTC
KEYWDS GLUCOKINASE, DIABETES, ACTIVATOR, ALTERNATIVE SPLICING, ATP-BINDING,
KEYWDS 2 DIABETES MELLITUS, DISEASE MUTATION, GLYCOLYSIS, KINASE, NUCLEOTIDE-
KEYWDS 3 BINDING, POLYMORPHISM, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.KAMATA,M.MITSUYA
REVDAT 5 01-NOV-23 3A0I 1 HETSYN
REVDAT 4 29-JUL-20 3A0I 1 COMPND REMARK HETNAM SITE
REVDAT 3 11-OCT-17 3A0I 1 REMARK
REVDAT 2 23-JUN-09 3A0I 1 JRNL
REVDAT 1 28-APR-09 3A0I 0
JRNL AUTH M.MITSUYA,K.KAMATA,M.BAMBA,H.WATANABE,Y.SASAKI,K.SASAKI,
JRNL AUTH 2 S.OHYAMA,H.HOSAKA,Y.NAGATA,J.EIKI,T.NISHIMURA
JRNL TITL DISCOVERY OF NOVEL 3,6-DISUBSTITUTED 2-PYRIDINECARBOXAMIDE
JRNL TITL 2 DERIVATIVES AS GK ACTIVATORS
JRNL REF BIOORG.MED.CHEM.LETT. V. 19 2718 2009
JRNL REFN ISSN 0960-894X
JRNL PMID 19362831
JRNL DOI 10.1016/J.BMCL.2009.03.137
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.37
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.7
REMARK 3 NUMBER OF REFLECTIONS : 28759
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) : 0.229
REMARK 3 R VALUE (WORKING SET) : 0.226
REMARK 3 FREE R VALUE : 0.277
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1529
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1784
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 82.16
REMARK 3 BIN R VALUE (WORKING SET) : 0.2660
REMARK 3 BIN FREE R VALUE SET COUNT : 100
REMARK 3 BIN FREE R VALUE : 0.3160
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3505
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 43
REMARK 3 SOLVENT ATOMS : 137
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 36.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.81
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.68000
REMARK 3 B22 (A**2) : 1.68000
REMARK 3 B33 (A**2) : -2.52000
REMARK 3 B12 (A**2) : 0.84000
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): 0.264
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.226
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.156
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.021
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.931
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.887
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3604 ; 0.024 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4848 ; 2.060 ; 1.979
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 447 ; 6.865 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 171 ;39.394 ;24.035
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 659 ;19.340 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 30 ;20.262 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 533 ; 0.146 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2761 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1917 ; 0.239 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2448 ; 0.310 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 144 ; 0.191 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 4 ; 0.142 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 33 ; 0.449 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 3 ; 0.369 ; 0.200
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): 2210 ; 1.305 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3546 ; 2.358 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1426 ; 3.511 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1302 ; 5.673 ; 4.500
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 : NULL
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
REMARK 4
REMARK 4 3A0I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-MAR-09.
REMARK 100 THE DEPOSITION ID IS D_1000028657.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-APR-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-6B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : DIFFRACTOMETER
REMARK 200 DETECTOR MANUFACTURER : WEISSENBERG
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : WEIS, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30342
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.5
REMARK 200 DATA REDUNDANCY : 5.000
REMARK 200 R MERGE (I) : 0.06400
REMARK 200 R SYM (I) : 0.06400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.25400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.860
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 1V4S
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.55
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30 % PEG 1500, HEPES, PH 6.6, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 298.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 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+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
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+1/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+5/6
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 214.65000
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 107.32500
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 160.98750
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 53.66250
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 268.31250
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 214.65000
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 107.32500
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 53.66250
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 160.98750
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 268.31250
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: 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 THR X 11
REMARK 465 ALA X 12
REMARK 465 LEU X 13
REMARK 465 MET X 462
REMARK 465 LEU X 463
REMARK 465 GLY X 464
REMARK 465 GLN X 465
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 GLU X 128 OG SER X 131 2.11
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OE2 GLU X 421 OE2 GLU X 421 11655 1.44
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 X 217 CB - CG - OD1 ANGL. DEV. = 6.8 DEGREES
REMARK 500 MET X 251 CG - SD - CE ANGL. DEV. = -10.8 DEGREES
REMARK 500 ARG X 422 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG X 422 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 GLU X 443 C - N - CA ANGL. DEV. = -15.6 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 THR X 49 -4.99 -140.14
REMARK 500 THR X 65 66.58 26.65
REMARK 500 GLU X 67 103.41 40.68
REMARK 500 GLU X 112 -44.46 -26.24
REMARK 500 THR X 116 9.08 -63.96
REMARK 500 MET X 121 -75.47 -49.89
REMARK 500 ASP X 132 -56.31 -26.10
REMARK 500 LYS X 142 143.88 -32.32
REMARK 500 LYS X 172 15.64 -162.60
REMARK 500 ASP X 187 -76.82 -45.98
REMARK 500 ARG X 192 -41.67 -152.98
REMARK 500 ASP X 194 -74.99 -13.40
REMARK 500 ALA X 201 118.35 -177.76
REMARK 500 ALA X 460 58.07 -95.86
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1V4S RELATED DB: PDB
REMARK 900 HUMAN GLUCOKINASE IN COMPLEX WITH ANOTHER ACTIVATOR
REMARK 900 RELATED ID: 1V4T RELATED DB: PDB
REMARK 900 APO HUMAN GLUCOKINSE STRUCTURE
REMARK 900 RELATED ID: 3FR0 RELATED DB: PDB
REMARK 900 HUMAN GLUCOKINASE IN COMPLEX WITH ANOTHER ACTIVATOR
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE SEQUENCE FOR THIS PROTEIN IS BASED ON ISOFORM 2 OF HXK4_HUMAN
REMARK 999 (UNIPROTKB/SWISS-PROT P35557).
DBREF 3A0I X 11 465 UNP P35557 HXK4_HUMAN 12 466
SEQRES 1 X 455 THR ALA LEU THR LEU VAL GLU GLN ILE LEU ALA GLU PHE
SEQRES 2 X 455 GLN LEU GLN GLU GLU ASP LEU LYS LYS VAL MET ARG ARG
SEQRES 3 X 455 MET GLN LYS GLU MET ASP ARG GLY LEU ARG LEU GLU THR
SEQRES 4 X 455 HIS GLU GLU ALA SER VAL LYS MET LEU PRO THR TYR VAL
SEQRES 5 X 455 ARG SER THR PRO GLU GLY SER GLU VAL GLY ASP PHE LEU
SEQRES 6 X 455 SER LEU ASP LEU GLY GLY THR ASN PHE ARG VAL MET LEU
SEQRES 7 X 455 VAL LYS VAL GLY GLU GLY GLU GLU GLY GLN TRP SER VAL
SEQRES 8 X 455 LYS THR LYS HIS GLN MET TYR SER ILE PRO GLU ASP ALA
SEQRES 9 X 455 MET THR GLY THR ALA GLU MET LEU PHE ASP TYR ILE SER
SEQRES 10 X 455 GLU CYS ILE SER ASP PHE LEU ASP LYS HIS GLN MET LYS
SEQRES 11 X 455 HIS LYS LYS LEU PRO LEU GLY PHE THR PHE SER PHE PRO
SEQRES 12 X 455 VAL ARG HIS GLU ASP ILE ASP LYS GLY ILE LEU LEU ASN
SEQRES 13 X 455 TRP THR LYS GLY PHE LYS ALA SER GLY ALA GLU GLY ASN
SEQRES 14 X 455 ASN VAL VAL GLY LEU LEU ARG ASP ALA ILE LYS ARG ARG
SEQRES 15 X 455 GLY ASP PHE GLU MET ASP VAL VAL ALA MET VAL ASN ASP
SEQRES 16 X 455 THR VAL ALA THR MET ILE SER CYS TYR TYR GLU ASP HIS
SEQRES 17 X 455 GLN CYS GLU VAL GLY MET ILE VAL GLY THR GLY CYS ASN
SEQRES 18 X 455 ALA CYS TYR MET GLU GLU MET GLN ASN VAL GLU LEU VAL
SEQRES 19 X 455 GLU GLY ASP GLU GLY ARG MET CYS VAL ASN THR GLU TRP
SEQRES 20 X 455 GLY ALA PHE GLY ASP SER GLY GLU LEU ASP GLU PHE LEU
SEQRES 21 X 455 LEU GLU TYR ASP ARG LEU VAL ASP GLU SER SER ALA ASN
SEQRES 22 X 455 PRO GLY GLN GLN LEU TYR GLU LYS LEU ILE GLY GLY LYS
SEQRES 23 X 455 TYR MET GLY GLU LEU VAL ARG LEU VAL LEU LEU ARG LEU
SEQRES 24 X 455 VAL ASP GLU ASN LEU LEU PHE HIS GLY GLU ALA SER GLU
SEQRES 25 X 455 GLN LEU ARG THR ARG GLY ALA PHE GLU THR ARG PHE VAL
SEQRES 26 X 455 SER GLN VAL GLU SER ASP THR GLY ASP ARG LYS GLN ILE
SEQRES 27 X 455 TYR ASN ILE LEU SER THR LEU GLY LEU ARG PRO SER THR
SEQRES 28 X 455 THR ASP CYS ASP ILE VAL ARG ARG ALA CYS GLU SER VAL
SEQRES 29 X 455 SER THR ARG ALA ALA HIS MET CYS SER ALA GLY LEU ALA
SEQRES 30 X 455 GLY VAL ILE ASN ARG MET ARG GLU SER ARG SER GLU ASP
SEQRES 31 X 455 VAL MET ARG ILE THR VAL GLY VAL ASP GLY SER VAL TYR
SEQRES 32 X 455 LYS LEU HIS PRO SER PHE LYS GLU ARG PHE HIS ALA SER
SEQRES 33 X 455 VAL ARG ARG LEU THR PRO SER CYS GLU ILE THR PHE ILE
SEQRES 34 X 455 GLU SER GLU GLU GLY SER GLY ARG GLY ALA ALA LEU VAL
SEQRES 35 X 455 SER ALA VAL ALA CYS LYS LYS ALA CYS MET LEU GLY GLN
HET GLC X 500 12
HET AJI X 501 30
HET NA X 600 1
HETNAM GLC ALPHA-D-GLUCOPYRANOSE
HETNAM AJI 3-[(4-FLUOROPHENYL)SULFANYL]-N-(4-METHYL-1,3-THIAZOL-2-
HETNAM 2 AJI YL)-6-[(4-METHYL-4H-1,2,4-TRIAZOL-3-YL)
HETNAM 3 AJI SULFANYL]PYRIDINE-2-CARBOXAMIDE
HETNAM NA SODIUM ION
HETSYN GLC ALPHA-D-GLUCOSE; D-GLUCOSE; GLUCOSE
HETSYN AJI 3-[(4-FLUOROPHENYL)THIO]-N-(4-METHYL-1,3-THIAZOL-2-YL)-
HETSYN 2 AJI 6-[(4-METHYL-4H-1,2,4-TRIAZOL-3-YL)THIO]PYRIDINE-2-
HETSYN 3 AJI CARBOXAMIDE
FORMUL 2 GLC C6 H12 O6
FORMUL 3 AJI C19 H15 F N6 O S3
FORMUL 4 NA NA 1+
FORMUL 5 HOH *137(H2 O)
HELIX 1 1 THR X 14 ALA X 21 1 8
HELIX 2 2 GLU X 22 GLN X 24 5 3
HELIX 3 3 GLN X 26 ARG X 46 1 21
HELIX 4 4 PRO X 111 THR X 116 1 6
HELIX 5 5 THR X 118 HIS X 137 1 20
HELIX 6 6 ASN X 180 ILE X 189 1 10
HELIX 7 7 ASN X 204 CYS X 213 1 10
HELIX 8 8 GLU X 256 PHE X 260 5 5
HELIX 9 9 LEU X 271 SER X 280 1 10
HELIX 10 10 GLN X 287 LEU X 292 1 6
HELIX 11 11 TYR X 297 GLU X 312 1 16
HELIX 12 12 LEU X 315 GLU X 319 5 5
HELIX 13 13 GLU X 331 ASP X 341 1 11
HELIX 14 14 ARG X 345 LEU X 355 1 11
HELIX 15 15 SER X 360 GLU X 395 1 36
HELIX 16 16 GLY X 410 HIS X 416 1 7
HELIX 17 17 SER X 418 THR X 431 1 14
HELIX 18 18 GLU X 443 LYS X 458 1 16
SHEET 1 A 6 LEU X 58 ARG X 63 0
SHEET 2 A 6 ARG X 250 ASN X 254 -1 O CYS X 252 N VAL X 62
SHEET 3 A 6 CYS X 230 GLU X 237 -1 N GLU X 236 O MET X 251
SHEET 4 A 6 CYS X 220 VAL X 226 -1 N ILE X 225 O ASN X 231
SHEET 5 A 6 MET X 402 ASP X 409 1 O GLY X 407 N MET X 224
SHEET 6 A 6 CYS X 434 GLU X 440 1 O ILE X 439 N VAL X 406
SHEET 1 B 5 GLY X 97 SER X 109 0
SHEET 2 B 5 ASN X 83 GLY X 94 -1 N LEU X 88 O THR X 103
SHEET 3 B 5 GLY X 72 LEU X 79 -1 N GLY X 72 O VAL X 91
SHEET 4 B 5 PRO X 145 PHE X 150 1 O GLY X 147 N LEU X 75
SHEET 5 B 5 ASP X 198 VAL X 203 1 O ASP X 198 N LEU X 146
SHEET 1 C 2 VAL X 154 ASP X 158 0
SHEET 2 C 2 LYS X 161 LEU X 164 -1 O LYS X 161 N GLU X 157
CRYST1 79.732 79.732 321.975 90.00 90.00 120.00 P 65 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 0.012542 0.007241 0.000000 0.00000
SCALE2 0.000000 0.014482 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003106 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
