spacer
spacer

PDBsum entry 3flw

Go to PDB code: 
Top Page protein ligands links
Signaling protein, transferase PDB id
3flw
Jmol
Contents
Protein chain
345 a.a.
Ligands
FLW
Waters ×278
HEADER    SIGNALING PROTEIN, TRANSFERASE          19-DEC-08   3FLW
TITLE     P38 KINASE CRYSTAL STRUCTURE IN COMPLEX WITH PAMAPIMOD
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 14;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: MITOGEN-ACTIVATED PROTEIN KINASE P38 ALPHA, MAP KINASE P38
COMPND   5 ALPHA, CYTOKINE SUPPRESSIVE ANTI-INFLAMMATORY DRUG-BINDING PROTEIN,
COMPND   6 CSAID-BINDING PROTEIN, CSBP, MAX-INTERACTING PROTEIN 2, MAP KINASE
COMPND   7 MXI2, SAPK2A;
COMPND   8 EC: 2.7.11.24;
COMPND   9 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: CSBP, CSBP1, CSBP2, CSPB1, MAPK14, MXI2;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS    P38; MAP KINASE; SERINE/THREONINE KINASE, ATP-BINDING, KINASE,
KEYWDS   2 NUCLEOTIDE-BINDING, NUCLEUS, PHOSPHOPROTEIN, SERINE/THREONINE-
KEYWDS   3 PROTEIN KINASE, TRANSFERASE, SIGNALING PROTEIN
EXPDTA    X-RAY DIFFRACTION
AUTHOR    A.KUGLSTATTER,M.GHATE
REVDAT   2   13-JUL-11 3FLW    1       VERSN
REVDAT   1   22-DEC-09 3FLW    0
JRNL        AUTH   M.SOTH,A.KUGLSTATTER,D.GOLDSTEIN
JRNL        TITL   THE DISCOVERY OF PAMAPIMOD, R1503 AND R1487 AS ORALLY
JRNL        TITL 2 BIOAVAILABLE AND HIGHLY SELECTIVE INHIBITORS OF P38 MAP
JRNL        TITL 3 KINASE
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   2
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0005
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.81
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.0
REMARK   3   NUMBER OF REFLECTIONS             : 26316
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) : 0.213
REMARK   3   R VALUE            (WORKING SET) : 0.212
REMARK   3   FREE R VALUE                     : 0.237
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 1402
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) : 2.10
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.15
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1614
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 78.44
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2900
REMARK   3   BIN FREE R VALUE SET COUNT          : 89
REMARK   3   BIN FREE R VALUE                    : 0.3420
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2784
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 29
REMARK   3   SOLVENT ATOMS            : 278
REMARK   3
REMARK   3  B VALUES.
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL
REMARK   3   FROM WILSON PLOT           (A**2) : 38.90
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.04
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.54000
REMARK   3    B22 (A**2) : -0.66000
REMARK   3    B33 (A**2) : 1.20000
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): 0.218
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.177
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.124
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.322
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.943
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.933
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2882 ; 0.008 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3915 ; 1.009 ; 1.975
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   342 ; 4.904 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   136 ;36.801 ;24.044
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   493 ;12.209 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    18 ;16.731 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   435 ; 0.065 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2186 ; 0.003 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1287 ; 0.199 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1978 ; 0.300 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   262 ; 0.127 ; 0.200
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):    33 ; 0.157 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    14 ; 0.116 ; 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):  1791 ; 0.608 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2802 ; 0.993 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1285 ; 1.126 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1113 ; 1.831 ; 4.500
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 : 3
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A  1001        A  2486
REMARK   3    RESIDUE RANGE :   A   361        A   361
REMARK   3    RESIDUE RANGE :   A     4        A   352
REMARK   3    ORIGIN FOR THE GROUP (A):  21.1740  17.1631  21.6591
REMARK   3    T TENSOR
REMARK   3      T11:  -0.0128 T22:  -0.0115
REMARK   3      T33:  -0.0320 T12:   0.0187
REMARK   3      T13:  -0.0072 T23:   0.0182
REMARK   3    L TENSOR
REMARK   3      L11:   0.2427 L22:   0.2637
REMARK   3      L33:   0.3031 L12:   0.1885
REMARK   3      L13:  -0.1738 L23:  -0.0499
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0311 S12:   0.0065 S13:  -0.0527
REMARK   3      S21:  -0.0207 S22:   0.0339 S23:  -0.0051
REMARK   3      S31:   0.0035 S32:  -0.0102 S33:  -0.0028
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH 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: NULL
REMARK   4
REMARK   4 3FLW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-DEC-08.
REMARK 100 THE RCSB ID CODE IS RCSB050751.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.6
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SSRL
REMARK 200  BEAMLINE                       : BL9-1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9800
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26366
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 89.1
REMARK 200  DATA REDUNDANCY                : 3.900
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.14700
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.18
REMARK 200  COMPLETENESS FOR SHELL     (%) : 84.9
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.30
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.50100
REMARK 200   FOR SHELL         : 2.050
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 57.06
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.86
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM HEPES PH 7.6, 50 MM CACL2, 17%
REMARK 280  PEG 3350, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 290K
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       22.67100
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       62.79900
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       43.00350
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       62.79900
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       22.67100
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       43.00350
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   -11
REMARK 465     ARG A   -10
REMARK 465     GLY A    -9
REMARK 465     SER A    -8
REMARK 465     HIS A    -7
REMARK 465     HIS A    -6
REMARK 465     HIS A    -5
REMARK 465     HIS A    -4
REMARK 465     HIS A    -3
REMARK 465     HIS A    -2
REMARK 465     GLY A    -1
REMARK 465     SER A     0
REMARK 465     MET A     1
REMARK 465     SER A     2
REMARK 465     GLN A     3
REMARK 465     LYS A    15
REMARK 465     LEU A   171
REMARK 465     ALA A   172
REMARK 465     ARG A   173
REMARK 465     LEU A   353
REMARK 465     ASP A   354
REMARK 465     GLN A   355
REMARK 465     GLU A   356
REMARK 465     GLU A   357
REMARK 465     MET A   358
REMARK 465     GLU A   359
REMARK 465     SER A   360
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   OE2  GLU A   286     O    HOH A  2048              2.18
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    ARG A  57       74.70     33.59
REMARK 500    ASN A 100      -10.31   -144.72
REMARK 500    LYS A 118       61.55     35.09
REMARK 500    CYS A 119       10.62     56.18
REMARK 500    ARG A 149      -13.68     76.82
REMARK 500    ASP A 150       36.75   -144.96
REMARK 500    PHE A 274       62.75   -106.36
REMARK 500    LEU A 289       56.50    -96.39
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 A1004        DISTANCE =  6.02 ANGSTROMS
REMARK 525    HOH A2186        DISTANCE =  5.62 ANGSTROMS
REMARK 525    HOH A2314        DISTANCE =  6.34 ANGSTROMS
REMARK 525    HOH A2379        DISTANCE =  5.08 ANGSTROMS
REMARK 525    HOH A2395        DISTANCE =  5.49 ANGSTROMS
REMARK 525    HOH A2406        DISTANCE =  6.08 ANGSTROMS
REMARK 525    HOH A2433        DISTANCE =  7.58 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FLW A 361
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3FLN   RELATED DB: PDB
REMARK 900 RELATED ID: 3FLQ   RELATED DB: PDB
REMARK 900 RELATED ID: 3FLS   RELATED DB: PDB
REMARK 900 RELATED ID: 3FLY   RELATED DB: PDB
REMARK 900 RELATED ID: 3FLZ   RELATED DB: PDB
REMARK 900 RELATED ID: 3FMH   RELATED DB: PDB
REMARK 900 RELATED ID: 3FMJ   RELATED DB: PDB
REMARK 900 RELATED ID: 3FMK   RELATED DB: PDB
DBREF  3FLW A    1   360  UNP    Q16539   MK14_HUMAN       1    360
SEQADV 3FLW MET A  -11  UNP  Q16539              EXPRESSION TAG
SEQADV 3FLW ARG A  -10  UNP  Q16539              EXPRESSION TAG
SEQADV 3FLW GLY A   -9  UNP  Q16539              EXPRESSION TAG
SEQADV 3FLW SER A   -8  UNP  Q16539              EXPRESSION TAG
SEQADV 3FLW HIS A   -7  UNP  Q16539              EXPRESSION TAG
SEQADV 3FLW HIS A   -6  UNP  Q16539              EXPRESSION TAG
SEQADV 3FLW HIS A   -5  UNP  Q16539              EXPRESSION TAG
SEQADV 3FLW HIS A   -4  UNP  Q16539              EXPRESSION TAG
SEQADV 3FLW HIS A   -3  UNP  Q16539              EXPRESSION TAG
SEQADV 3FLW HIS A   -2  UNP  Q16539              EXPRESSION TAG
SEQADV 3FLW GLY A   -1  UNP  Q16539              EXPRESSION TAG
SEQADV 3FLW SER A    0  UNP  Q16539              EXPRESSION TAG
SEQRES   1 A  372  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER MET
SEQRES   2 A  372  SER GLN GLU ARG PRO THR PHE TYR ARG GLN GLU LEU ASN
SEQRES   3 A  372  LYS THR ILE TRP GLU VAL PRO GLU ARG TYR GLN ASN LEU
SEQRES   4 A  372  SER PRO VAL GLY SER GLY ALA TYR GLY SER VAL CYS ALA
SEQRES   5 A  372  ALA PHE ASP THR LYS THR GLY LEU ARG VAL ALA VAL LYS
SEQRES   6 A  372  LYS LEU SER ARG PRO PHE GLN SER ILE ILE HIS ALA LYS
SEQRES   7 A  372  ARG THR TYR ARG GLU LEU ARG LEU LEU LYS HIS MET LYS
SEQRES   8 A  372  HIS GLU ASN VAL ILE GLY LEU LEU ASP VAL PHE THR PRO
SEQRES   9 A  372  ALA ARG SER LEU GLU GLU PHE ASN ASP VAL TYR LEU VAL
SEQRES  10 A  372  THR HIS LEU MET GLY ALA ASP LEU ASN ASN ILE VAL LYS
SEQRES  11 A  372  CYS GLN LYS LEU THR ASP ASP HIS VAL GLN PHE LEU ILE
SEQRES  12 A  372  TYR GLN ILE LEU ARG GLY LEU LYS TYR ILE HIS SER ALA
SEQRES  13 A  372  ASP ILE ILE HIS ARG ASP LEU LYS PRO SER ASN LEU ALA
SEQRES  14 A  372  VAL ASN GLU ASP CYS GLU LEU LYS ILE LEU ASP PHE GLY
SEQRES  15 A  372  LEU ALA ARG HIS THR ASP ASP GLU MET THR GLY TYR VAL
SEQRES  16 A  372  ALA THR ARG TRP TYR ARG ALA PRO GLU ILE MET LEU ASN
SEQRES  17 A  372  TRP MET HIS TYR ASN GLN THR VAL ASP ILE TRP SER VAL
SEQRES  18 A  372  GLY CYS ILE MET ALA GLU LEU LEU THR GLY ARG THR LEU
SEQRES  19 A  372  PHE PRO GLY THR ASP HIS ILE ASP GLN LEU LYS LEU ILE
SEQRES  20 A  372  LEU ARG LEU VAL GLY THR PRO GLY ALA GLU LEU LEU LYS
SEQRES  21 A  372  LYS ILE SER SER GLU SER ALA ARG ASN TYR ILE GLN SER
SEQRES  22 A  372  LEU THR GLN MET PRO LYS MET ASN PHE ALA ASN VAL PHE
SEQRES  23 A  372  ILE GLY ALA ASN PRO LEU ALA VAL ASP LEU LEU GLU LYS
SEQRES  24 A  372  MET LEU VAL LEU ASP SER ASP LYS ARG ILE THR ALA ALA
SEQRES  25 A  372  GLN ALA LEU ALA HIS ALA TYR PHE ALA GLN TYR HIS ASP
SEQRES  26 A  372  PRO ASP ASP GLU PRO VAL ALA ASP PRO TYR ASP GLN SER
SEQRES  27 A  372  PHE GLU SER ARG ASP LEU LEU ILE ASP GLU TRP LYS SER
SEQRES  28 A  372  LEU THR TYR ASP GLU VAL ILE SER PHE VAL PRO PRO PRO
SEQRES  29 A  372  LEU ASP GLN GLU GLU MET GLU SER
HET    FLW  A 361      29
HETNAM     FLW 6-(2,4-DIFLUOROPHENOXY)-2-{[3-HYDROXY-1-(2-
HETNAM   2 FLW  HYDROXYETHYL)PROPYL]AMINO}-8-METHYLPYRIDO[2,3-
HETNAM   3 FLW  D]PYRIMIDIN-7(8H)-ONE
FORMUL   2  FLW    C19 H20 F2 N4 O4
FORMUL   3  HOH   *278(H2 O)
HELIX    1   1 SER A   61  MET A   78  1                                  18
HELIX    2   2 LEU A  113  LYS A  118  1                                   6
HELIX    3   3 THR A  123  ALA A  144  1                                  22
HELIX    4   4 LYS A  152  SER A  154  5                                   3
HELIX    5   5 ASP A  176  THR A  180  5                                   5
HELIX    6   6 VAL A  183  TYR A  188  1                                   6
HELIX    7   7 ALA A  190  LEU A  195  1                                   6
HELIX    8   8 THR A  203  GLY A  219  1                                  17
HELIX    9   9 ASP A  227  GLY A  240  1                                  14
HELIX   10  10 GLY A  243  ILE A  250  1                                   8
HELIX   11  11 SER A  252  GLN A  260  1                                   9
HELIX   12  12 ASN A  269  PHE A  274  1                                   6
HELIX   13  13 ASN A  278  LEU A  289  1                                  12
HELIX   14  14 ASP A  292  ARG A  296  5                                   5
HELIX   15  15 THR A  298  ALA A  304  1                                   7
HELIX   16  16 HIS A  305  ALA A  309  5                                   5
HELIX   17  17 ASP A  313  GLU A  317  5                                   5
HELIX   18  18 GLN A  325  ARG A  330  5                                   6
HELIX   19  19 LEU A  333  SER A  347  1                                  15
SHEET    1   A 2 PHE A   8  GLU A  12  0
SHEET    2   A 2 ILE A  17  PRO A  21 -1  O  TRP A  18   N  GLN A  11
SHEET    1   B 5 TYR A  24  GLY A  33  0
SHEET    2   B 5 GLY A  36  ASP A  43 -1  O  VAL A  38   N  VAL A  30
SHEET    3   B 5 LEU A  48  LEU A  55 -1  O  VAL A  52   N  CYS A  39
SHEET    4   B 5 TYR A 103  HIS A 107 -1  O  LEU A 104   N  LYS A  53
SHEET    5   B 5 ASP A  88  PHE A  90 -1  N  ASP A  88   O  VAL A 105
SHEET    1   C 3 ALA A 111  ASP A 112  0
SHEET    2   C 3 LEU A 156  VAL A 158 -1  O  VAL A 158   N  ALA A 111
SHEET    3   C 3 LEU A 164  ILE A 166 -1  O  LYS A 165   N  ALA A 157
SITE     1 AC1 16 VAL A  30  GLY A  33  VAL A  38  ALA A  51
SITE     2 AC1 16 LYS A  53  ILE A  84  LEU A  86  LEU A 104
SITE     3 AC1 16 VAL A 105  THR A 106  HIS A 107  MET A 109
SITE     4 AC1 16 ALA A 111  HOH A1002  HOH A1022  HOH A2114
CRYST1   45.342   86.007  125.598  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      0.022055  0.000000  0.000000        0.00000
SCALE2      0.000000  0.011627  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007962        0.00000
      
PROCHECK
Go to PROCHECK summary
 References