HEADER TRANSFERASE/INHIBITOR 16-JUN-17 5W6O
TITLE CHOLINE KINASE ALPHA IN COMPLEX WITH TCD-717
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHOLINE KINASE ALPHA;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 80-457;
COMPND 5 SYNONYM: CK,CHETK-ALPHA,ETHANOLAMINE KINASE,EK;
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 GENE: CHKA, CHK, CKI;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ENZYME, INHIBITOR, DRUG, TRANSFERASE-INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR S.K.KALL,A.LAVIE
REVDAT 3 11-DEC-19 5W6O 1 REMARK
REVDAT 2 07-MAR-18 5W6O 1 JRNL
REVDAT 1 14-FEB-18 5W6O 0
JRNL AUTH S.L.KALL,E.J.DELIKATNY,A.LAVIE
JRNL TITL IDENTIFICATION OF A UNIQUE INHIBITOR-BINDING SITE ON CHOLINE
JRNL TITL 2 KINASE ALPHA.
JRNL REF BIOCHEMISTRY V. 57 1316 2018
JRNL REFN ISSN 1520-4995
JRNL PMID 29389115
JRNL DOI 10.1021/ACS.BIOCHEM.7B01257
REMARK 2
REMARK 2 RESOLUTION. 2.35 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0158
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) : 2.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 89.54
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 36241
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) : 0.210
REMARK 3 R VALUE (WORKING SET) : 0.207
REMARK 3 FREE R VALUE : 0.268
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1951
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) : 2.35
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.41
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2653
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.96
REMARK 3 BIN R VALUE (WORKING SET) : 0.3700
REMARK 3 BIN FREE R VALUE SET COUNT : 144
REMARK 3 BIN FREE R VALUE : 0.3470
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5859
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 144
REMARK 3 SOLVENT ATOMS : 175
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 53.83
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.61000
REMARK 3 B22 (A**2) : 1.85000
REMARK 3 B33 (A**2) : -1.23000
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): 0.370
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.267
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.274
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.012
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.953
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.916
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6257 ; 0.012 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 5767 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8438 ; 1.498 ; 1.990
REMARK 3 BOND ANGLES OTHERS (DEGREES): 13367 ; 0.993 ; 3.003
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 715 ; 5.660 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 308 ;33.484 ;23.149
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1114 ;15.536 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 49 ;17.548 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 848 ; 0.088 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6846 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1427 ; 0.001 ; 0.020
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): 2851 ; 3.892 ; 5.197
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2850 ; 3.891 ; 5.196
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3569 ; 6.133 ; 7.782
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 3570 ; 6.133 ; 7.783
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3406 ; 4.204 ; 5.604
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 3406 ; 4.204 ; 5.604
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 4870 ; 6.666 ; 8.224
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 7095 ; 9.507 ;56.670
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 7096 ; 9.507 ;56.673
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 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 1
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 81 456 B 81 456 23124 0.07 0.05
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 : 1.20
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 5W6O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-JUN-17.
REMARK 100 THE DEPOSITION ID IS D_1000228519.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-AUG-16
REMARK 200 TEMPERATURE (KELVIN) : 80
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-F
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97872
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38250
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.340
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 4.880
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.3500
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.34
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES PH 6.5 18% PEG 3350, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 298K
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 27.97500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 65.70000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 61.17500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 65.70000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.97500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 61.17500
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2580 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33760 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ASP A 80
REMARK 465 ALA A 150
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 465 ALA B 150
REMARK 465 ILE B 151
REMARK 465 LEU B 152
REMARK 465 GLN B 153
REMARK 465 MET B 154
REMARK 465 ARG B 155
REMARK 465 SER B 156
REMARK 465 CYS B 157
REMARK 465 ASN B 158
REMARK 465 LYS B 159
REMARK 465 GLU B 160
REMARK 465 GLY B 161
REMARK 465 SER B 162
REMARK 465 GLU B 163
REMARK 465 GLN B 164
REMARK 465 ALA B 165
REMARK 465 GLN B 166
REMARK 465 LYS B 167
REMARK 465 GLU B 168
REMARK 465 ASN B 169
REMARK 465 GLU B 170
REMARK 465 PHE B 171
REMARK 465 GLN B 172
REMARK 465 GLY B 173
REMARK 465 ALA B 174
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLU A 81 CG CD OE1 OE2
REMARK 470 ASP B 80 CG OD1 OD2
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 ARG B 444 NE - CZ - NH1 ANGL. DEV. = 3.2 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 ASN A 122 80.39 48.54
REMARK 500 PRO A 241 41.43 -81.68
REMARK 500 ASN A 281 75.32 58.66
REMARK 500 ASP A 306 42.05 -157.48
REMARK 500 ASP A 330 77.35 64.66
REMARK 500 THR A 395 -50.02 -27.03
REMARK 500 ASN B 122 80.77 50.64
REMARK 500 PRO B 241 43.42 -83.27
REMARK 500 ASN B 281 76.06 56.61
REMARK 500 ASP B 306 41.21 -157.98
REMARK 500 ASP B 330 77.28 65.27
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 679 DISTANCE = 6.41 ANGSTROMS
REMARK 525 HOH A 680 DISTANCE = 7.13 ANGSTROMS
REMARK 525 HOH B 695 DISTANCE = 7.70 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 9X1 A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MES A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MES B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 9X1 B 501 and TRP B
REMARK 800 248
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 9X1 B 501 and TRP B
REMARK 800 248
DBREF 5W6O A 80 457 UNP P35790 CHKA_HUMAN 80 457
DBREF 5W6O B 80 457 UNP P35790 CHKA_HUMAN 80 457
SEQRES 1 A 378 ASP GLU GLN PRO GLU PRO ARG THR ARG ARG ARG ALA TYR
SEQRES 2 A 378 LEU TRP CYS LYS GLU PHE LEU PRO GLY ALA TRP ARG GLY
SEQRES 3 A 378 LEU ARG GLU ASP GLU PHE HIS ILE SER VAL ILE ARG GLY
SEQRES 4 A 378 GLY LEU SER ASN MET LEU PHE GLN CYS SER LEU PRO ASP
SEQRES 5 A 378 THR THR ALA THR LEU GLY ASP GLU PRO ARG LYS VAL LEU
SEQRES 6 A 378 LEU ARG LEU TYR GLY ALA ILE LEU GLN MET ARG SER CYS
SEQRES 7 A 378 ASN LYS GLU GLY SER GLU GLN ALA GLN LYS GLU ASN GLU
SEQRES 8 A 378 PHE GLN GLY ALA GLU ALA MET VAL LEU GLU SER VAL MET
SEQRES 9 A 378 PHE ALA ILE LEU ALA GLU ARG SER LEU GLY PRO LYS LEU
SEQRES 10 A 378 TYR GLY ILE PHE PRO GLN GLY ARG LEU GLU GLN PHE ILE
SEQRES 11 A 378 PRO SER ARG ARG LEU ASP THR GLU GLU LEU SER LEU PRO
SEQRES 12 A 378 ASP ILE SER ALA GLU ILE ALA GLU LYS MET ALA THR PHE
SEQRES 13 A 378 HIS GLY MET LYS MET PRO PHE ASN LYS GLU PRO LYS TRP
SEQRES 14 A 378 LEU PHE GLY THR MET GLU LYS TYR LEU LYS GLU VAL LEU
SEQRES 15 A 378 ARG ILE LYS PHE THR GLU GLU SER ARG ILE LYS LYS LEU
SEQRES 16 A 378 HIS LYS LEU LEU SER TYR ASN LEU PRO LEU GLU LEU GLU
SEQRES 17 A 378 ASN LEU ARG SER LEU LEU GLU SER THR PRO SER PRO VAL
SEQRES 18 A 378 VAL PHE CYS HIS ASN ASP CYS GLN GLU GLY ASN ILE LEU
SEQRES 19 A 378 LEU LEU GLU GLY ARG GLU ASN SER GLU LYS GLN LYS LEU
SEQRES 20 A 378 MET LEU ILE ASP PHE GLU TYR SER SER TYR ASN TYR ARG
SEQRES 21 A 378 GLY PHE ASP ILE GLY ASN HIS PHE CYS GLU TRP MET TYR
SEQRES 22 A 378 ASP TYR SER TYR GLU LYS TYR PRO PHE PHE ARG ALA ASN
SEQRES 23 A 378 ILE ARG LYS TYR PRO THR LYS LYS GLN GLN LEU HIS PHE
SEQRES 24 A 378 ILE SER SER TYR LEU PRO ALA PHE GLN ASN ASP PHE GLU
SEQRES 25 A 378 ASN LEU SER THR GLU GLU LYS SER ILE ILE LYS GLU GLU
SEQRES 26 A 378 MET LEU LEU GLU VAL ASN ARG PHE ALA LEU ALA SER HIS
SEQRES 27 A 378 PHE LEU TRP GLY LEU TRP SER ILE VAL GLN ALA LYS ILE
SEQRES 28 A 378 SER SER ILE GLU PHE GLY TYR MET ASP TYR ALA GLN ALA
SEQRES 29 A 378 ARG PHE ASP ALA TYR PHE HIS GLN LYS ARG LYS LEU GLY
SEQRES 30 A 378 VAL
SEQRES 1 B 378 ASP GLU GLN PRO GLU PRO ARG THR ARG ARG ARG ALA TYR
SEQRES 2 B 378 LEU TRP CYS LYS GLU PHE LEU PRO GLY ALA TRP ARG GLY
SEQRES 3 B 378 LEU ARG GLU ASP GLU PHE HIS ILE SER VAL ILE ARG GLY
SEQRES 4 B 378 GLY LEU SER ASN MET LEU PHE GLN CYS SER LEU PRO ASP
SEQRES 5 B 378 THR THR ALA THR LEU GLY ASP GLU PRO ARG LYS VAL LEU
SEQRES 6 B 378 LEU ARG LEU TYR GLY ALA ILE LEU GLN MET ARG SER CYS
SEQRES 7 B 378 ASN LYS GLU GLY SER GLU GLN ALA GLN LYS GLU ASN GLU
SEQRES 8 B 378 PHE GLN GLY ALA GLU ALA MET VAL LEU GLU SER VAL MET
SEQRES 9 B 378 PHE ALA ILE LEU ALA GLU ARG SER LEU GLY PRO LYS LEU
SEQRES 10 B 378 TYR GLY ILE PHE PRO GLN GLY ARG LEU GLU GLN PHE ILE
SEQRES 11 B 378 PRO SER ARG ARG LEU ASP THR GLU GLU LEU SER LEU PRO
SEQRES 12 B 378 ASP ILE SER ALA GLU ILE ALA GLU LYS MET ALA THR PHE
SEQRES 13 B 378 HIS GLY MET LYS MET PRO PHE ASN LYS GLU PRO LYS TRP
SEQRES 14 B 378 LEU PHE GLY THR MET GLU LYS TYR LEU LYS GLU VAL LEU
SEQRES 15 B 378 ARG ILE LYS PHE THR GLU GLU SER ARG ILE LYS LYS LEU
SEQRES 16 B 378 HIS LYS LEU LEU SER TYR ASN LEU PRO LEU GLU LEU GLU
SEQRES 17 B 378 ASN LEU ARG SER LEU LEU GLU SER THR PRO SER PRO VAL
SEQRES 18 B 378 VAL PHE CYS HIS ASN ASP CYS GLN GLU GLY ASN ILE LEU
SEQRES 19 B 378 LEU LEU GLU GLY ARG GLU ASN SER GLU LYS GLN LYS LEU
SEQRES 20 B 378 MET LEU ILE ASP PHE GLU TYR SER SER TYR ASN TYR ARG
SEQRES 21 B 378 GLY PHE ASP ILE GLY ASN HIS PHE CYS GLU TRP MET TYR
SEQRES 22 B 378 ASP TYR SER TYR GLU LYS TYR PRO PHE PHE ARG ALA ASN
SEQRES 23 B 378 ILE ARG LYS TYR PRO THR LYS LYS GLN GLN LEU HIS PHE
SEQRES 24 B 378 ILE SER SER TYR LEU PRO ALA PHE GLN ASN ASP PHE GLU
SEQRES 25 B 378 ASN LEU SER THR GLU GLU LYS SER ILE ILE LYS GLU GLU
SEQRES 26 B 378 MET LEU LEU GLU VAL ASN ARG PHE ALA LEU ALA SER HIS
SEQRES 27 B 378 PHE LEU TRP GLY LEU TRP SER ILE VAL GLN ALA LYS ILE
SEQRES 28 B 378 SER SER ILE GLU PHE GLY TYR MET ASP TYR ALA GLN ALA
SEQRES 29 B 378 ARG PHE ASP ALA TYR PHE HIS GLN LYS ARG LYS LEU GLY
SEQRES 30 B 378 VAL
HET 9X1 A 501 52
HET MES A 502 12
HET EDO A 503 4
HET EDO A 504 4
HET EDO A 505 4
HET 9X1 B 501 52
HET MES B 502 12
HET EDO B 503 4
HETNAM 9X1 1,1'-[[1,1'-BIPHENYL]-4,4'-DIYLBIS(METHYLENE)]BIS{4-
HETNAM 2 9X1 [(4-CHLOROPHENYL)(METHYL)AMINO]QUINOLIN-1-IUM}
HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
HETNAM EDO 1,2-ETHANEDIOL
HETSYN 9X1 TCD-717
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 9X1 2(C46 H38 CL2 N4 2+)
FORMUL 4 MES 2(C6 H13 N O4 S)
FORMUL 5 EDO 4(C2 H6 O2)
FORMUL 11 HOH *175(H2 O)
HELIX 1 AA1 GLU A 84 LEU A 99 1 16
HELIX 2 AA2 PRO A 100 LEU A 106 5 7
HELIX 3 AA3 ARG A 107 PHE A 111 5 5
HELIX 4 AA4 ALA A 176 ARG A 190 1 15
HELIX 5 AA5 ASP A 215 SER A 220 5 6
HELIX 6 AA6 LEU A 221 GLY A 237 1 17
HELIX 7 AA7 LYS A 247 ARG A 262 1 16
HELIX 8 AA8 GLU A 267 SER A 279 1 13
HELIX 9 AA9 ASN A 281 SER A 295 1 15
HELIX 10 AB1 GLN A 308 GLY A 310 5 3
HELIX 11 AB2 GLY A 317 SER A 321 5 5
HELIX 12 AB3 ARG A 339 GLU A 349 1 11
HELIX 13 AB4 ILE A 366 TYR A 369 5 4
HELIX 14 AB5 THR A 371 GLN A 387 1 17
HELIX 15 AB6 ASN A 388 LEU A 393 5 6
HELIX 16 AB7 SER A 394 SER A 431 1 38
HELIX 17 AB8 GLY A 436 GLY A 456 1 21
HELIX 18 AB9 GLU B 84 LEU B 99 1 16
HELIX 19 AC1 PRO B 100 LEU B 106 5 7
HELIX 20 AC2 ARG B 107 PHE B 111 5 5
HELIX 21 AC3 ALA B 176 ARG B 190 1 15
HELIX 22 AC4 ASP B 215 SER B 220 5 6
HELIX 23 AC5 LEU B 221 GLY B 237 1 17
HELIX 24 AC6 LYS B 247 ARG B 262 1 16
HELIX 25 AC7 GLU B 267 SER B 279 1 13
HELIX 26 AC8 ASN B 281 SER B 295 1 15
HELIX 27 AC9 GLN B 308 GLY B 310 5 3
HELIX 28 AD1 GLY B 317 SER B 321 5 5
HELIX 29 AD2 ARG B 339 GLU B 349 1 11
HELIX 30 AD3 ILE B 366 TYR B 369 5 4
HELIX 31 AD4 THR B 371 GLN B 387 1 17
HELIX 32 AD5 ASN B 388 LEU B 393 5 6
HELIX 33 AD6 SER B 394 SER B 431 1 38
HELIX 34 AD7 GLY B 436 GLY B 456 1 21
SHEET 1 AA1 5 HIS A 112 ARG A 117 0
SHEET 2 AA1 5 MET A 123 SER A 128 -1 O SER A 128 N HIS A 112
SHEET 3 AA1 5 LYS A 142 LEU A 147 -1 O VAL A 143 N CYS A 127
SHEET 4 AA1 5 GLY A 203 GLN A 207 -1 O GLU A 206 N LEU A 144
SHEET 5 AA1 5 LEU A 196 PHE A 200 -1 N TYR A 197 O LEU A 205
SHEET 1 AA2 3 SER A 211 ARG A 213 0
SHEET 2 AA2 3 ILE A 312 LEU A 315 -1 O LEU A 314 N ARG A 212
SHEET 3 AA2 3 LEU A 326 LEU A 328 -1 O MET A 327 N LEU A 313
SHEET 1 AA3 2 VAL A 300 CYS A 303 0
SHEET 2 AA3 2 SER A 335 TYR A 338 -1 O SER A 335 N CYS A 303
SHEET 1 AA4 2 TYR A 352 ASP A 353 0
SHEET 2 AA4 2 ARG A 363 ALA A 364 -1 O ARG A 363 N ASP A 353
SHEET 1 AA5 5 HIS B 112 ARG B 117 0
SHEET 2 AA5 5 MET B 123 SER B 128 -1 O SER B 128 N HIS B 112
SHEET 3 AA5 5 LYS B 142 LEU B 147 -1 O VAL B 143 N CYS B 127
SHEET 4 AA5 5 GLY B 203 GLN B 207 -1 O GLU B 206 N LEU B 144
SHEET 5 AA5 5 LEU B 196 PHE B 200 -1 N TYR B 197 O LEU B 205
SHEET 1 AA6 3 SER B 211 ARG B 213 0
SHEET 2 AA6 3 ILE B 312 LEU B 315 -1 O LEU B 314 N ARG B 212
SHEET 3 AA6 3 LEU B 326 LEU B 328 -1 O MET B 327 N LEU B 313
SHEET 1 AA7 2 VAL B 300 CYS B 303 0
SHEET 2 AA7 2 SER B 335 TYR B 338 -1 O SER B 335 N CYS B 303
SHEET 1 AA8 2 TYR B 352 ASP B 353 0
SHEET 2 AA8 2 ARG B 363 ALA B 364 -1 O ARG B 363 N ASP B 353
LINK CE3BTRP A 248 CL7 9X1 A 501 1555 1555 1.94
LINK CZ2BTRP A 248 C4 9X1 A 501 1555 1555 1.46
LINK CZ2BTRP A 248 C3 9X1 A 501 1555 1555 1.48
LINK CZ3BTRP A 248 C4 9X1 A 501 1555 1555 1.61
LINK CH2BTRP A 248 C5 9X1 A 501 1555 1555 1.51
LINK CZ2BTRP B 248 C47 9X1 B 501 1555 1555 1.65
LINK CH2BTRP B 248 C48 9X1 B 501 1555 1555 1.08
CISPEP 1 TYR A 359 PRO A 360 0 9.89
CISPEP 2 TYR B 359 PRO B 360 0 10.06
SITE 1 AC1 11 TYR A 148 MET A 177 GLU A 180 PHE A 200
SITE 2 AC1 11 PRO A 201 TRP A 248 THR A 252 TYR A 256
SITE 3 AC1 11 TYR A 333 ASN A 337 PHE A 341
SITE 1 AC2 6 ASP A 306 GLN A 308 GLU A 349 TRP A 420
SITE 2 AC2 6 TRP A 423 PHE A 435
SITE 1 AC3 2 TYR A 352 ALA A 443
SITE 1 AC4 5 MET A 351 HIS A 417 ALA A 447 HIS A 450
SITE 2 AC4 5 GLN A 451
SITE 1 AC5 6 GLU A 217 TRP A 350 MET A 351 ARG A 363
SITE 2 AC5 6 LYS A 368 GLU B 84
SITE 1 AC6 6 ASP B 306 GLN B 308 GLU B 349 TRP B 420
SITE 2 AC6 6 TYR B 440 HOH B 620
SITE 1 AC7 5 TYR B 369 HIS B 417 HIS B 450 GLN B 451
SITE 2 AC7 5 LYS B 454
SITE 1 AC8 20 LEU A 179 TYR B 148 MET B 177 PHE B 200
SITE 2 AC8 20 PRO B 201 PRO B 246 LYS B 247 LEU B 249
SITE 3 AC8 20 PHE B 250 GLY B 251 THR B 252 TYR B 256
SITE 4 AC8 20 ASN B 305 TYR B 333 SER B 335 ASN B 337
SITE 5 AC8 20 PHE B 341 LEU B 419 TRP B 420 TRP B 423
SITE 1 AC9 20 LEU A 179 TYR B 148 MET B 177 PHE B 200
SITE 2 AC9 20 PRO B 201 PRO B 246 LYS B 247 LEU B 249
SITE 3 AC9 20 PHE B 250 GLY B 251 THR B 252 TYR B 256
SITE 4 AC9 20 ASN B 305 TYR B 333 SER B 335 ASN B 337
SITE 5 AC9 20 PHE B 341 LEU B 419 TRP B 420 TRP B 423
CRYST1 55.950 122.350 131.400 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 0.017873 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008173 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007610 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
