HEADER TRANSFERASE 21-NOV-13 4CG9
TITLE HUMAN CHOLINE KINASE A1 IN COMPLEX WITH COMPOUND 12
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHOLINE KINASE ALPHA;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 75-457;
COMPND 5 SYNONYM: CK, CHETK-ALPHA, ETHANOLAMINE KINASE, EK, CHOLINE KINASE A1;
COMPND 6 EC: 2.7.1.32, 2.7.1.82;
COMPND 7 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: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: STAR;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMALC2X
KEYWDS TRANSFERASE, CANCER, DRUG TARGET, BISCATIONIC COMPOUNDS
EXPDTA X-RAY DIFFRACTION
AUTHOR B.RUBIO-RUIZ,A.FIGUEROLA-CONCHAS,J.RAMOS-TORRECILLAS,F.CAPITAN-
AUTHOR 2 CANADAS,P.RIOS-MARCO,M.P.CARRASCO,M.A.GALLO,A.ESPINOSA,C.MARCO,
AUTHOR 3 C.CONCEPCION,A.ENTRENA-GUADIX,R.HURTADO-GUERRERO,A.CONEJO-GARCIA
REVDAT 4 20-DEC-23 4CG9 1 REMARK
REVDAT 3 12-MAR-14 4CG9 1 SOURCE
REVDAT 2 05-FEB-14 4CG9 1 JRNL
REVDAT 1 15-JAN-14 4CG9 0
JRNL AUTH B.RUBIO-RUIZ,A.FIGUEROLA-CONCHAS,J.RAMOS-TORRECILLAS,
JRNL AUTH 2 F.CAPITAN-CANADAS,P.RIOS-MARCO,M.P.CARRASCO,M.A.GALLO,
JRNL AUTH 3 A.ESPINOSA,C.MARCO,C.CONCEPCION,A.ENTRENA-GUADIX,
JRNL AUTH 4 R.HURTADO-GUERRERO,A.CONEJO-GARCIA
JRNL TITL DISCOVERY OF A NEW BINDING SITE ON HUMAN CHOLINE KINASE A1:
JRNL TITL 2 DESIGN, SYNTHESIS, CRYSTALLOGRAPHIC STUDIES AND BIOLOGICAL
JRNL TITL 3 EVALUATION OF ASYMMETRICAL BISPYRIDINIUM DERIVATIVES
JRNL REF J.MED.CHEM. V. 57 507 2014
JRNL REFN ISSN 0022-2623
JRNL PMID 24387243
JRNL DOI 10.1021/JM401665X
REMARK 2
REMARK 2 RESOLUTION. 1.83 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
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) : 1.83
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 61.08
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 35792
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) : 0.230
REMARK 3 R VALUE (WORKING SET) : 0.229
REMARK 3 FREE R VALUE : 0.256
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1883
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) : 1.83
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.88
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2319
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2820
REMARK 3 BIN FREE R VALUE SET COUNT : 120
REMARK 3 BIN FREE R VALUE : 0.3540
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2933
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 22
REMARK 3 SOLVENT ATOMS : 80
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.04
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.49000
REMARK 3 B22 (A**2) : -0.49000
REMARK 3 B33 (A**2) : 0.97000
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): 0.153
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.140
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.100
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.737
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.935
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.926
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3044 ; 0.009 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4102 ; 1.324 ; 1.976
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 355 ; 5.131 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 152 ;33.681 ;23.355
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 554 ;15.550 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 23 ;17.019 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 421 ; 0.098 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2330 ; 0.006 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : 1
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 81 A 457
REMARK 3 ORIGIN FOR THE GROUP (A): -16.8922 17.1806 6.5413
REMARK 3 T TENSOR
REMARK 3 T11: 0.0363 T22: 0.0140
REMARK 3 T33: 0.0492 T12: -0.0113
REMARK 3 T13: -0.0045 T23: -0.0010
REMARK 3 L TENSOR
REMARK 3 L11: 0.0834 L22: 0.1523
REMARK 3 L33: 0.2593 L12: -0.0829
REMARK 3 L13: 0.0459 L23: -0.1628
REMARK 3 S TENSOR
REMARK 3 S11: -0.0188 S12: 0.0110 S13: -0.0278
REMARK 3 S21: 0.0170 S22: 0.0046 S23: -0.0048
REMARK 3 S31: -0.0064 S32: -0.0223 S33: 0.0142
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
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 4CG9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 21-NOV-13.
REMARK 100 THE DEPOSITION ID IS D_1290059052.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 73
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.976
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37763
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.830
REMARK 200 RESOLUTION RANGE LOW (A) : 61.080
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 6.400
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.83
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.88
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.70
REMARK 200 R MERGE FOR SHELL (I) : 0.55000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 3G15
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.24
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+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 110.28000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 30.54000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 30.54000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 165.42000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 30.54000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 30.54000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 55.14000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 30.54000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 30.54000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 165.42000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 30.54000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 30.54000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 55.14000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 110.28000
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 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 PRO A 75
REMARK 465 GLN A 76
REMARK 465 PRO A 77
REMARK 465 PRO A 78
REMARK 465 ALA A 79
REMARK 465 ASP A 80
REMARK 465 ILE A 151
REMARK 465 LEU A 152
REMARK 465 GLN A 153
REMARK 465 MET A 154
REMARK 465 ARG A 155
REMARK 465 SER A 156
REMARK 465 CYS A 157
REMARK 465 ASN A 158
REMARK 465 LYS A 159
REMARK 465 GLU A 160
REMARK 465 GLY A 161
REMARK 465 SER A 162
REMARK 465 GLU A 163
REMARK 465 GLN A 164
REMARK 465 ALA A 165
REMARK 465 GLN A 166
REMARK 465 LYS A 167
REMARK 465 GLU A 168
REMARK 465 ASN A 169
REMARK 465 GLU A 170
REMARK 465 PHE A 171
REMARK 465 GLN A 172
REMARK 465 GLY A 173
REMARK 465 ALA A 174
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 O HOH A 2002 O HOH A 2050 3454 1.59
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 PRO A 241 44.12 -89.89
REMARK 500 ASN A 281 71.08 68.92
REMARK 500 ASP A 306 44.93 -149.59
REMARK 500 ASP A 330 81.90 62.77
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GQG A 0
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4CG8 RELATED DB: PDB
REMARK 900 HUMAN CHOLINE KINASE A1 IN COMPLEX WITH COMPOUND 14
REMARK 900 RELATED ID: 4CGA RELATED DB: PDB
REMARK 900 HUMAN CHOLINE KINASE A1 IN COMPLEX WITH COMPOUND 5
DBREF 4CG9 A 75 457 UNP P35790 CHKA_HUMAN 75 457
SEQRES 1 A 383 PRO GLN PRO PRO ALA ASP GLU GLN PRO GLU PRO ARG THR
SEQRES 2 A 383 ARG ARG ARG ALA TYR LEU TRP CYS LYS GLU PHE LEU PRO
SEQRES 3 A 383 GLY ALA TRP ARG GLY LEU ARG GLU ASP GLU PHE HIS ILE
SEQRES 4 A 383 SER VAL ILE ARG GLY GLY LEU SER ASN MET LEU PHE GLN
SEQRES 5 A 383 CYS SER LEU PRO ASP THR THR ALA THR LEU GLY ASP GLU
SEQRES 6 A 383 PRO ARG LYS VAL LEU LEU ARG LEU TYR GLY ALA ILE LEU
SEQRES 7 A 383 GLN MET ARG SER CYS ASN LYS GLU GLY SER GLU GLN ALA
SEQRES 8 A 383 GLN LYS GLU ASN GLU PHE GLN GLY ALA GLU ALA MET VAL
SEQRES 9 A 383 LEU GLU SER VAL MET PHE ALA ILE LEU ALA GLU ARG SER
SEQRES 10 A 383 LEU GLY PRO LYS LEU TYR GLY ILE PHE PRO GLN GLY ARG
SEQRES 11 A 383 LEU GLU GLN PHE ILE PRO SER ARG ARG LEU ASP THR GLU
SEQRES 12 A 383 GLU LEU SER LEU PRO ASP ILE SER ALA GLU ILE ALA GLU
SEQRES 13 A 383 LYS MET ALA THR PHE HIS GLY MET LYS MET PRO PHE ASN
SEQRES 14 A 383 LYS GLU PRO LYS TRP LEU PHE GLY THR MET GLU LYS TYR
SEQRES 15 A 383 LEU LYS GLU VAL LEU ARG ILE LYS PHE THR GLU GLU SER
SEQRES 16 A 383 ARG ILE LYS LYS LEU HIS LYS LEU LEU SER TYR ASN LEU
SEQRES 17 A 383 PRO LEU GLU LEU GLU ASN LEU ARG SER LEU LEU GLU SER
SEQRES 18 A 383 THR PRO SER PRO VAL VAL PHE CYS HIS ASN ASP CYS GLN
SEQRES 19 A 383 GLU GLY ASN ILE LEU LEU LEU GLU GLY ARG GLU ASN SER
SEQRES 20 A 383 GLU LYS GLN LYS LEU MET LEU ILE ASP PHE GLU TYR SER
SEQRES 21 A 383 SER TYR ASN TYR ARG GLY PHE ASP ILE GLY ASN HIS PHE
SEQRES 22 A 383 CYS GLU TRP MET TYR ASP TYR SER TYR GLU LYS TYR PRO
SEQRES 23 A 383 PHE PHE ARG ALA ASN ILE ARG LYS TYR PRO THR LYS LYS
SEQRES 24 A 383 GLN GLN LEU HIS PHE ILE SER SER TYR LEU PRO ALA PHE
SEQRES 25 A 383 GLN ASN ASP PHE GLU ASN LEU SER THR GLU GLU LYS SER
SEQRES 26 A 383 ILE ILE LYS GLU GLU MET LEU LEU GLU VAL ASN ARG PHE
SEQRES 27 A 383 ALA LEU ALA SER HIS PHE LEU TRP GLY LEU TRP SER ILE
SEQRES 28 A 383 VAL GLN ALA LYS ILE SER SER ILE GLU PHE GLY TYR MET
SEQRES 29 A 383 ASP TYR ALA GLN ALA ARG PHE ASP ALA TYR PHE HIS GLN
SEQRES 30 A 383 LYS ARG LYS LEU GLY VAL
HET GQG A 0 22
HETNAM GQG N,N-DIMETHYL-1-[(4-PHENYLPHENYL)METHYL]PYRIDIN-1-IUM-4-
HETNAM 2 GQG AMINE
FORMUL 2 GQG C20 H21 N2 1+
FORMUL 3 HOH *80(H2 O)
HELIX 1 1 GLU A 84 LEU A 99 1 16
HELIX 2 2 PRO A 100 LEU A 106 5 7
HELIX 3 3 ARG A 107 PHE A 111 5 5
HELIX 4 4 GLU A 175 ARG A 190 1 16
HELIX 5 5 ASP A 215 SER A 220 5 6
HELIX 6 6 LEU A 221 GLY A 237 1 17
HELIX 7 7 LYS A 247 LEU A 261 1 15
HELIX 8 8 GLU A 267 SER A 279 1 13
HELIX 9 9 ASN A 281 SER A 295 1 15
HELIX 10 10 GLN A 308 GLY A 310 5 3
HELIX 11 11 ARG A 339 TRP A 350 1 12
HELIX 12 12 ILE A 366 TYR A 369 5 4
HELIX 13 13 THR A 371 GLN A 387 1 17
HELIX 14 14 ASN A 388 LEU A 393 5 6
HELIX 15 15 SER A 394 SER A 431 1 38
HELIX 16 16 GLY A 436 GLY A 456 1 21
SHEET 1 AA 5 HIS A 112 ARG A 117 0
SHEET 2 AA 5 MET A 123 SER A 128 -1 O LEU A 124 N ILE A 116
SHEET 3 AA 5 LYS A 142 LEU A 147 -1 O VAL A 143 N CYS A 127
SHEET 4 AA 5 GLY A 203 GLN A 207 -1 O ARG A 204 N ARG A 146
SHEET 5 AA 5 LEU A 196 PHE A 200 -1 N TYR A 197 O LEU A 205
SHEET 1 AB 3 SER A 211 ARG A 213 0
SHEET 2 AB 3 ILE A 312 LEU A 315 -1 O LEU A 314 N ARG A 212
SHEET 3 AB 3 LEU A 326 LEU A 328 -1 O MET A 327 N LEU A 313
SHEET 1 AC 2 VAL A 300 CYS A 303 0
SHEET 2 AC 2 SER A 335 TYR A 338 -1 O SER A 335 N CYS A 303
SHEET 1 AD 2 TYR A 352 ASP A 353 0
SHEET 2 AD 2 ARG A 363 ALA A 364 -1 O ARG A 363 N ASP A 353
CISPEP 1 TYR A 359 PRO A 360 0 8.28
SITE 1 AC1 9 ASP A 306 GLN A 308 TYR A 333 GLU A 349
SITE 2 AC1 9 TYR A 354 TRP A 420 TRP A 423 PHE A 435
SITE 3 AC1 9 TYR A 440
CRYST1 61.080 61.080 220.560 90.00 90.00 90.00 P 43 21 2 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 0.016372 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016372 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004534 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
