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PDBsum entry 3r63

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Transferase PDB id
3r63
Jmol
Contents
Protein chain
347 a.a.
Waters ×161
HEADER    TRANSFERASE                             21-MAR-11   3R63
TITLE     STRUCTURE OF ERK2 (SPE) MUTANT (S246E)
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 1;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: MAP KINASE 1, MAPK 1, ERT1, EXTRACELLULAR SIGNAL-REGULATED
COMPND   5 KINASE 2, ERK-2, MAP KINASE ISOFORM P42, P42-MAPK, MITOGEN-ACTIVATED
COMPND   6 PROTEIN KINASE 2, MAP KINASE 2, MAPK 2;
COMPND   7 EC: 2.7.11.24;
COMPND   8 ENGINEERED: YES;
COMPND   9 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE   3 ORGANISM_COMMON: RAT;
SOURCE   4 ORGANISM_TAXID: 10116;
SOURCE   5 GENE: MAPK1, ERK2, MAPK, PRKM1;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS    NUCLEAR TRANSPORT, PHOSPHORYLATION, KINASE FOLD, KINASE, ATP BINDING,
KEYWDS   2 TRANSFERASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    O.LIVNAH,Y.KARAMANSHA
REVDAT   1   17-AUG-11 3R63    0
JRNL        AUTH   A.PLOTNIKOV,D.CHUDERLAND,Y.KARAMANSHA,O.LIVNAH,R.SEGER
JRNL        TITL   NUCLEAR ERK TRANSLOCATION IS MEDIATED BY PROTEIN KINASE CK2
JRNL        TITL 2 AND ACCELERATED BY AUTOPHOSPHORYLATION.
JRNL        REF    MOL.CELL.BIOL.                V.  31  3515 2011
JRNL        REFN                   ISSN 0270-7306
JRNL        PMID   21730285
JRNL        DOI    10.1128/MCB.05424-11
REMARK   2
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.5.0102
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) : 50.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.9
REMARK   3   NUMBER OF REFLECTIONS             : 38703
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) : 0.191
REMARK   3   R VALUE            (WORKING SET) : 0.188
REMARK   3   FREE R VALUE                     : 0.245
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 2059
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) : 2776
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 94.60
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2120
REMARK   3   BIN FREE R VALUE SET COUNT          : 165
REMARK   3   BIN FREE R VALUE                    : 0.3220
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2828
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 0
REMARK   3   SOLVENT ATOMS            : 161
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 36.48
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.86000
REMARK   3    B22 (A**2) : 0.35000
REMARK   3    B33 (A**2) : -0.02000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : -0.81000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): NULL
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.119
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.073
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.797
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.957
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.934
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2903 ; 0.017 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3936 ; 1.684 ; 1.972
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   346 ; 5.516 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   140 ;39.087 ;24.000
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   512 ;17.410 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    18 ;22.328 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   432 ; 0.134 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2205 ; 0.008 ; 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):  1744 ; 1.694 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2828 ; 2.727 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1159 ; 4.138 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1108 ; 6.032 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2903 ; 2.132 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.20
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 3R63 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-MAR-11.
REMARK 100 THE RCSB ID CODE IS RCSB064535.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 26-FEB-09
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.0
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : ESRF
REMARK 200  BEAMLINE                       : ID23-1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98
REMARK 200  MONOCHROMATOR                  : OPTICAL HATCH
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          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 40979
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.1
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : NULL
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   FOR SHELL         : NULL
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   (%): 47.54
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM BIS-TRIS BUFFER, 61MM AMMONIUM
REMARK 280  SULFATE, 15% PEG 3350, PH 7.0, VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,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        0.00000
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       34.99950
REMARK 290   SMTRY3   2  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     1
REMARK 465     ALA A     2
REMARK 465     ALA A     3
REMARK 465     GLU A    10
REMARK 465     MET A    11
REMARK 465     VAL A    12
REMARK 465     ARG A    13
REMARK 465     GLY A    14
REMARK 465     ASP A   330
REMARK 465     MET A   331
REMARK 465     GLU A   332
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 A  89   CD  -  NE  -  CZ  ANGL. DEV. =  11.2 DEGREES
REMARK 500    ARG A  89   NE  -  CZ  -  NH1 ANGL. DEV. =   9.3 DEGREES
REMARK 500    ARG A  89   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.9 DEGREES
REMARK 500    ARG A 146   NE  -  CZ  -  NH1 ANGL. DEV. =   3.9 DEGREES
REMARK 500    ARG A 146   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.3 DEGREES
REMARK 500    ARG A 170   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 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 A  27      104.39   -160.09
REMARK 500    ILE A  29      -82.11   -127.31
REMARK 500    GLU A  31       16.26   -140.60
REMARK 500    TYR A  34       52.85     38.09
REMARK 500    MET A  36      146.18   -170.13
REMARK 500    ASP A 147       41.72   -145.29
REMARK 500    ASP A 165       77.84     59.55
REMARK 500    ASN A 199       16.13   -159.71
REMARK 500    ASN A 255      102.37    -45.97
REMARK 500    LEU A 292       48.73    -95.93
REMARK 500    ASP A 316       98.97   -160.06
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ERK   RELATED DB: PDB
DBREF  3R63 A    1   358  UNP    P63086   MK01_RAT         1    358
SEQADV 3R63 GLU A  246  UNP  P63086    SER   246 ENGINEERED MUTATION
SEQRES   1 A  358  MET ALA ALA ALA ALA ALA ALA GLY PRO GLU MET VAL ARG
SEQRES   2 A  358  GLY GLN VAL PHE ASP VAL GLY PRO ARG TYR THR ASN LEU
SEQRES   3 A  358  SER TYR ILE GLY GLU GLY ALA TYR GLY MET VAL CYS SER
SEQRES   4 A  358  ALA TYR ASP ASN LEU ASN LYS VAL ARG VAL ALA ILE LYS
SEQRES   5 A  358  LYS ILE SER PRO PHE GLU HIS GLN THR TYR CYS GLN ARG
SEQRES   6 A  358  THR LEU ARG GLU ILE LYS ILE LEU LEU ARG PHE ARG HIS
SEQRES   7 A  358  GLU ASN ILE ILE GLY ILE ASN ASP ILE ILE ARG ALA PRO
SEQRES   8 A  358  THR ILE GLU GLN MET LYS ASP VAL TYR ILE VAL GLN ASP
SEQRES   9 A  358  LEU MET GLU THR ASP LEU TYR LYS LEU LEU LYS THR GLN
SEQRES  10 A  358  HIS LEU SER ASN ASP HIS ILE CYS TYR PHE LEU TYR GLN
SEQRES  11 A  358  ILE LEU ARG GLY LEU LYS TYR ILE HIS SER ALA ASN VAL
SEQRES  12 A  358  LEU HIS ARG ASP LEU LYS PRO SER ASN LEU LEU LEU ASN
SEQRES  13 A  358  THR THR CYS ASP LEU LYS ILE CYS ASP PHE GLY LEU ALA
SEQRES  14 A  358  ARG VAL ALA ASP PRO ASP HIS ASP HIS THR GLY PHE LEU
SEQRES  15 A  358  THR GLU TYR VAL ALA THR ARG TRP TYR ARG ALA PRO GLU
SEQRES  16 A  358  ILE MET LEU ASN SER LYS GLY TYR THR LYS SER ILE ASP
SEQRES  17 A  358  ILE TRP SER VAL GLY CYS ILE LEU ALA GLU MET LEU SER
SEQRES  18 A  358  ASN ARG PRO ILE PHE PRO GLY LYS HIS TYR LEU ASP GLN
SEQRES  19 A  358  LEU ASN HIS ILE LEU GLY ILE LEU GLY SER PRO GLU GLN
SEQRES  20 A  358  GLU ASP LEU ASN CYS ILE ILE ASN LEU LYS ALA ARG ASN
SEQRES  21 A  358  TYR LEU LEU SER LEU PRO HIS LYS ASN LYS VAL PRO TRP
SEQRES  22 A  358  ASN ARG LEU PHE PRO ASN ALA ASP SER LYS ALA LEU ASP
SEQRES  23 A  358  LEU LEU ASP LYS MET LEU THR PHE ASN PRO HIS LYS ARG
SEQRES  24 A  358  ILE GLU VAL GLU GLN ALA LEU ALA HIS PRO TYR LEU GLU
SEQRES  25 A  358  GLN TYR TYR ASP PRO SER ASP GLU PRO ILE ALA GLU ALA
SEQRES  26 A  358  PRO PHE LYS PHE ASP MET GLU LEU ASP ASP LEU PRO LYS
SEQRES  27 A  358  GLU LYS LEU LYS GLU LEU ILE PHE GLU GLU THR ALA ARG
SEQRES  28 A  358  PHE GLN PRO GLY TYR ARG SER
FORMUL   2  HOH   *161(H2 O)
HELIX    1   1 HIS A   59  PHE A   76  1                                  18
HELIX    2   2 LEU A  110  GLN A  117  1                                   8
HELIX    3   3 SER A  120  ALA A  141  1                                  22
HELIX    4   4 LYS A  149  SER A  151  5                                   3
HELIX    5   5 ASP A  173  ASP A  177  5                                   5
HELIX    6   6 THR A  188  ARG A  192  5                                   5
HELIX    7   7 ALA A  193  ASN A  199  1                                   7
HELIX    8   8 LYS A  205  ASN A  222  1                                  18
HELIX    9   9 HIS A  230  GLY A  243  1                                  14
HELIX   10  10 GLU A  246  CYS A  252  1                                   7
HELIX   11  11 ASN A  255  LEU A  265  1                                  11
HELIX   12  12 PRO A  272  PHE A  277  1                                   6
HELIX   13  13 ASP A  281  LEU A  292  1                                  12
HELIX   14  14 GLU A  301  ALA A  307  1                                   7
HELIX   15  15 HIS A  308  GLU A  312  5                                   5
HELIX   16  16 ASP A  316  GLU A  320  5                                   5
HELIX   17  17 PRO A  337  THR A  349  1                                  13
HELIX   18  18 ALA A  350  GLN A  353  5                                   4
SHEET    1   A 5 TYR A  23  TYR A  28  0
SHEET    2   A 5 GLY A  35  ASP A  42 -1  O  SER A  39   N  SER A  27
SHEET    3   A 5 VAL A  47  ILE A  54 -1  O  VAL A  49   N  ALA A  40
SHEET    4   A 5 VAL A  99  ASP A 104 -1  O  VAL A  99   N  ILE A  54
SHEET    5   A 5 ASP A  86  ILE A  88 -1  N  ILE A  88   O  TYR A 100
SHEET    1   B 3 THR A 108  ASP A 109  0
SHEET    2   B 3 LEU A 153  LEU A 155 -1  O  LEU A 155   N  THR A 108
SHEET    3   B 3 LEU A 161  ILE A 163 -1  O  LYS A 162   N  LEU A 154
SHEET    1   C 2 VAL A 143  LEU A 144  0
SHEET    2   C 2 ARG A 170  VAL A 171 -1  O  ARG A 170   N  LEU A 144
CRYST1   48.770   69.999   60.117  90.00 109.04  90.00 P 1 21 1      2
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      0.020504  0.000000  0.007075        0.00000
SCALE2      0.000000  0.014286  0.000000        0.00000
SCALE3      0.000000  0.000000  0.017597        0.00000
      
PROCHECK
Go to PROCHECK summary
 References