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PDBsum entry 2fsl

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Transferase PDB id
2fsl
Jmol
Contents
Protein chain
332 a.a.
Ligands
BOG
Waters ×207
HEADER    TRANSFERASE                             23-JAN-06   2FSL
TITLE     MITOGEN ACTIVATED PROTEIN KINASE P38ALPHA (D176A+F327S)
TITLE    2 ACTIVATING MUTANT FORM-A
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 14;
COMPND   3 CHAIN: X;
COMPND   4 SYNONYM: MITOGEN-ACTIVATED PROTEIN KINASE P38 ALPHA, MAP
COMPND   5 KINASE P38 ALPHA, CYTOKINE SUPPRESSIVE ANTI-INFLAMMATORY
COMPND   6 DRUG BINDING PROTEIN, CSAID-BINDING PROTEIN, CSBP, MAX-
COMPND   7 INTERACTING PROTEIN 2, MAP KINASE MXI2, SAPK2A;
COMPND   8 EC: 2.7.1.37;
COMPND   9 ENGINEERED: YES;
COMPND  10 MUTATION: 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_VECTOR_TYPE: PLASMID;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET28
KEYWDS    MITOGEN ACTIVATED PROTEIN KINASE, P38, ACTIVE MUTANTS,
KEYWDS   2 LIPIDS, MAP KINASE INSERTION, AUTOPHOSPHORYLATION,
KEYWDS   3 TRANSFERASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    R.DISKIN,O.LIVNAH
REVDAT   3   24-FEB-09 2FSL    1       VERSN
REVDAT   2   12-DEC-06 2FSL    1       JRNL
REVDAT   1   05-DEC-06 2FSL    0
JRNL        AUTH   R.DISKIN,M.LEBENDIKER,D.ENGELBERG,O.LIVNAH
JRNL        TITL   STRUCTURES OF P38ALPHA ACTIVE MUTANTS REVEAL
JRNL        TITL 2 CONFORMATIONAL CHANGES IN L16 LOOP THAT INDUCE
JRNL        TITL 3 AUTOPHOSPHORYLATION AND ACTIVATION
JRNL        REF    J.MOL.BIOL.                   V. 365    66 2007
JRNL        REFN                   ISSN 0022-2836
JRNL        PMID   17059827
JRNL        DOI    10.1016/J.JMB.2006.08.043
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.1.24
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) : 1.70
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.80
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7
REMARK   3   NUMBER OF REFLECTIONS             : 37426
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) : 0.220
REMARK   3   R VALUE            (WORKING SET) : 0.219
REMARK   3   FREE R VALUE                     : 0.240
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1976
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) : 1.70
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.75
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2642
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2570
REMARK   3   BIN FREE R VALUE SET COUNT          : 149
REMARK   3   BIN FREE R VALUE                    : 0.2830
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2670
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 20
REMARK   3   SOLVENT ATOMS            : 207
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.92
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.04000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : 0.03000
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): 0.127
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.116
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.080
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.403
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.951
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.948
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2748 ; 0.017 ; 0.021
REMARK   3   BOND LENGTHS OTHERS               (A):  2514 ; 0.002 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3726 ; 1.561 ; 1.964
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  5856 ; 0.880 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   328 ; 6.929 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   423 ; 0.112 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2990 ; 0.009 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):   537 ; 0.003 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   575 ; 0.226 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  2808 ; 0.238 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1623 ; 0.085 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   144 ; 0.182 ; 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):     8 ; 0.116 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):    48 ; 0.220 ; 0.200
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    20 ; 0.156 ; 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):  1659 ; 1.077 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2688 ; 1.992 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1089 ; 2.726 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1038 ; 4.521 ; 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  : NULL
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   : 1.40
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
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 2FSL COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-JAN-06.
REMARK 100 THE RCSB ID CODE IS RCSB036261.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 20-DEC-05
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.2
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : ESRF
REMARK 200  BEAMLINE                       : ID29
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.953
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 39481
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7
REMARK 200  DATA REDUNDANCY                : 14.100
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.07200
REMARK 200   FOR THE DATA SET  : 75.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.76
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.2
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.70
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.44200
REMARK 200   FOR SHELL         : 5.800
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 41.23
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 18% PEG 3350, 0.2M KF, 0.1 HEPES,
REMARK 280  25MM BOG, PH 7.2, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280  277K
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       34.00050
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       37.24350
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       34.83850
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       37.24350
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       34.00050
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       34.83850
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 300 REMARK: THE BIOLOGICAL ACTIVE UNIT IS A MONOMER
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 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     MET X    -6
REMARK 465     ALA X    -5
REMARK 465     HIS X    -4
REMARK 465     HIS X    -3
REMARK 465     HIS X    -2
REMARK 465     HIS X    -1
REMARK 465     HIS X     0
REMARK 465     HIS X     1
REMARK 465     SER X     2
REMARK 465     GLN X     3
REMARK 465     TYR X    35
REMARK 465     ILE X   116
REMARK 465     VAL X   117
REMARK 465     LYS X   118
REMARK 465     CYS X   119
REMARK 465     PHE X   169
REMARK 465     GLY X   170
REMARK 465     LEU X   171
REMARK 465     ALA X   172
REMARK 465     ARG X   173
REMARK 465     HIS X   174
REMARK 465     THR X   175
REMARK 465     ALA X   176
REMARK 465     ASP X   177
REMARK 465     GLU X   178
REMARK 465     MET X   179
REMARK 465     THR X   180
REMARK 465     GLY X   181
REMARK 465     TYR X   182
REMARK 465     GLN X   355
REMARK 465     GLU X   356
REMARK 465     GLU X   357
REMARK 465     MET X   358
REMARK 465     GLU X   359
REMARK 465     SER X   360
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     LEU X 353    CB   CG   CD1  CD2
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   OD1  ASN X   201     OG1  THR X   203              1.91
REMARK 500   OE1  GLN X   128     NE2  GLN X   310              2.05
REMARK 500
REMARK 500 REMARK: NULL
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    MET X 194   CG    MET X 194   SD     -0.202
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 227   CB  -  CG  -  OD1 ANGL. DEV. =   5.6 DEGREES
REMARK 500    ASP X 230   CB  -  CG  -  OD2 ANGL. DEV. =   6.1 DEGREES
REMARK 500    ASP X 315   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 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    SER X  32      -84.61    -59.54
REMARK 500    ASN X 100      -30.34   -136.14
REMARK 500    ARG X 149      -10.60     78.29
REMARK 500    ASP X 150       46.55   -143.93
REMARK 500    MET X 198     -171.52     55.12
REMARK 500    PHE X 274       60.27   -108.68
REMARK 500    LEU X 289       61.06   -100.45
REMARK 500    SER X 327       52.88    -63.39
REMARK 500    GLU X 328      -45.24   -179.62
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500                                 MODEL     OMEGA
REMARK 500 VAL X   30     GLY X   31                 -149.09
REMARK 500 SER X  327     GLU X  328                 -138.56
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 X1140        DISTANCE =  6.43 ANGSTROMS
REMARK 525    HOH X1147        DISTANCE =  5.93 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG X 1000
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2FSM   RELATED DB: PDB
REMARK 900 RELATED ID: 2FSO   RELATED DB: PDB
REMARK 900 RELATED ID: 2FST   RELATED DB: PDB
DBREF  2FSL X    2   360  UNP    Q16539   MK14_HUMAN       1    359
SEQADV 2FSL MET X   -6  UNP  Q16539              EXPRESSION TAG
SEQADV 2FSL ALA X   -5  UNP  Q16539              EXPRESSION TAG
SEQADV 2FSL HIS X   -4  UNP  Q16539              EXPRESSION TAG
SEQADV 2FSL HIS X   -3  UNP  Q16539              EXPRESSION TAG
SEQADV 2FSL HIS X   -2  UNP  Q16539              EXPRESSION TAG
SEQADV 2FSL HIS X   -1  UNP  Q16539              EXPRESSION TAG
SEQADV 2FSL HIS X    0  UNP  Q16539              EXPRESSION TAG
SEQADV 2FSL HIS X    1  UNP  Q16539              EXPRESSION TAG
SEQADV 2FSL ALA X  176  UNP  Q16539    ASP   175 ENGINEERED
SEQADV 2FSL SER X  327  UNP  Q16539    PHE   326 ENGINEERED
SEQRES   1 X  367  MET ALA HIS HIS HIS HIS HIS HIS SER GLN GLU ARG PRO
SEQRES   2 X  367  THR PHE TYR ARG GLN GLU LEU ASN LYS THR ILE TRP GLU
SEQRES   3 X  367  VAL PRO GLU ARG TYR GLN ASN LEU SER PRO VAL GLY SER
SEQRES   4 X  367  GLY ALA TYR GLY SER VAL CYS ALA ALA PHE ASP THR LYS
SEQRES   5 X  367  THR GLY LEU ARG VAL ALA VAL LYS LYS LEU SER ARG PRO
SEQRES   6 X  367  PHE GLN SER ILE ILE HIS ALA LYS ARG THR TYR ARG GLU
SEQRES   7 X  367  LEU ARG LEU LEU LYS HIS MET LYS HIS GLU ASN VAL ILE
SEQRES   8 X  367  GLY LEU LEU ASP VAL PHE THR PRO ALA ARG SER LEU GLU
SEQRES   9 X  367  GLU PHE ASN ASP VAL TYR LEU VAL THR HIS LEU MET GLY
SEQRES  10 X  367  ALA ASP LEU ASN ASN ILE VAL LYS CYS GLN LYS LEU THR
SEQRES  11 X  367  ASP ASP HIS VAL GLN PHE LEU ILE TYR GLN ILE LEU ARG
SEQRES  12 X  367  GLY LEU LYS TYR ILE HIS SER ALA ASP ILE ILE HIS ARG
SEQRES  13 X  367  ASP LEU LYS PRO SER ASN LEU ALA VAL ASN GLU ASP CYS
SEQRES  14 X  367  GLU LEU LYS ILE LEU ASP PHE GLY LEU ALA ARG HIS THR
SEQRES  15 X  367  ALA ASP GLU MET THR GLY TYR VAL ALA THR ARG TRP TYR
SEQRES  16 X  367  ARG ALA PRO GLU ILE MET LEU ASN TRP MET HIS TYR ASN
SEQRES  17 X  367  GLN THR VAL ASP ILE TRP SER VAL GLY CYS ILE MET ALA
SEQRES  18 X  367  GLU LEU LEU THR GLY ARG THR LEU PHE PRO GLY THR ASP
SEQRES  19 X  367  HIS ILE ASP GLN LEU LYS LEU ILE LEU ARG LEU VAL GLY
SEQRES  20 X  367  THR PRO GLY ALA GLU LEU LEU LYS LYS ILE SER SER GLU
SEQRES  21 X  367  SER ALA ARG ASN TYR ILE GLN SER LEU THR GLN MET PRO
SEQRES  22 X  367  LYS MET ASN PHE ALA ASN VAL PHE ILE GLY ALA ASN PRO
SEQRES  23 X  367  LEU ALA VAL ASP LEU LEU GLU LYS MET LEU VAL LEU ASP
SEQRES  24 X  367  SER ASP LYS ARG ILE THR ALA ALA GLN ALA LEU ALA HIS
SEQRES  25 X  367  ALA TYR PHE ALA GLN TYR HIS ASP PRO ASP ASP GLU PRO
SEQRES  26 X  367  VAL ALA ASP PRO TYR ASP GLN SER SER GLU SER ARG ASP
SEQRES  27 X  367  LEU LEU ILE ASP GLU TRP LYS SER LEU THR TYR ASP GLU
SEQRES  28 X  367  VAL ILE SER PHE VAL PRO PRO PRO LEU ASP GLN GLU GLU
SEQRES  29 X  367  MET GLU SER
HET    BOG  X1000      20
HETNAM     BOG B-OCTYLGLUCOSIDE
FORMUL   2  BOG    C14 H28 O6
FORMUL   3  HOH   *207(H2 O)
HELIX    1   1 SER X   61  MET X   78  1                                  18
HELIX    2   2 SER X   95  PHE X   99  5                                   5
HELIX    3   3 THR X  123  ALA X  144  1                                  22
HELIX    4   4 LYS X  152  SER X  154  5                                   3
HELIX    5   5 ALA X  190  LEU X  195  1                                   6
HELIX    6   6 THR X  203  GLY X  219  1                                  17
HELIX    7   7 ASP X  227  GLY X  240  1                                  14
HELIX    8   8 GLY X  243  LYS X  248  1                                   6
HELIX    9   9 SER X  252  SER X  261  1                                  10
HELIX   10  10 ASN X  269  VAL X  273  5                                   5
HELIX   11  11 ASN X  278  LEU X  289  1                                  12
HELIX   12  12 ASP X  292  ARG X  296  5                                   5
HELIX   13  13 THR X  298  ALA X  304  1                                   7
HELIX   14  14 HIS X  305  ALA X  309  5                                   5
HELIX   15  15 ASP X  313  GLU X  317  5                                   5
HELIX   16  16 LEU X  333  PHE X  348  1                                  16
SHEET    1   A 2 PHE X   8  LEU X  13  0
SHEET    2   A 2 THR X  16  PRO X  21 -1  O  THR X  16   N  LEU X  13
SHEET    1   B 5 TYR X  24  PRO X  29  0
SHEET    2   B 5 SER X  37  ASP X  43 -1  O  ALA X  40   N  SER X  28
SHEET    3   B 5 LEU X  48  LYS X  54 -1  O  LEU X  48   N  ASP X  43
SHEET    4   B 5 TYR X 103  HIS X 107 -1  O  LEU X 104   N  LYS X  53
SHEET    5   B 5 ASP X  88  PHE X  90 -1  N  ASP X  88   O  VAL X 105
SHEET    1   C 3 ALA X 111  ASP X 112  0
SHEET    2   C 3 LEU X 156  VAL X 158 -1  O  VAL X 158   N  ALA X 111
SHEET    3   C 3 LEU X 164  ILE X 166 -1  O  LYS X 165   N  ALA X 157
SITE     1 AC1 14 LEU X 195  TRP X 197  HIS X 199  ASN X 201
SITE     2 AC1 14 LEU X 246  LYS X 249  LEU X 291  ASP X 292
SITE     3 AC1 14 SER X 293  ASP X 294  HOH X1011  HOH X1024
SITE     4 AC1 14 HOH X1049  HOH X1172
CRYST1   68.001   69.677   74.487  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      0.014706  0.000000  0.000000        0.00000
SCALE2      0.000000  0.014352  0.000000        0.00000
SCALE3      0.000000  0.000000  0.013425        0.00000
      
PROCHECK
Go to PROCHECK summary
 References