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PDBsum entry 1ohe

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Hydrolase PDB id
1ohe
Jmol
Contents
Protein chain
339 a.a. *
Ligands
ACE-ALA-SEP-PRO
Waters ×143
* Residue conservation analysis
HEADER    HYDROLASE                               24-MAY-03   1OHE
TITLE     STRUCTURE OF CDC14B PHOSPHATASE WITH A PEPTIDE LIGAND
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CDC14B2 PHOSPHATASE;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: CORE DOMAIN, RESIDUES 39-386;
COMPND   5 SYNONYM: CDC14B;
COMPND   6 ENGINEERED: YES;
COMPND   7 MOL_ID: 2;
COMPND   8 MOLECULE: PEPTIDE LIGAND;
COMPND   9 CHAIN: B;
COMPND  10 OTHER_DETAILS: SUBSTRATE
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 EXPRESSION_SYSTEM: BACULOVIRUS/INSECT CELL;
SOURCE   6 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE   7 MOL_ID: 2;
SOURCE   8 SYNTHETIC: NON-BIOLOGICAL SEQUENCE;
SOURCE   9 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE  10 ORGANISM_TAXID: 562
KEYWDS    PROTEIN PHOSPHATASE, CELL CYCLE, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    C.H.GRAY,V.M.GOOD,N.K.TONKS,D.BARFORD
REVDAT   2   24-FEB-09 1OHE    1       VERSN
REVDAT   1   24-JUL-03 1OHE    0
JRNL        AUTH   C.H.GRAY,V.M.GOOD,N.K.TONKS,D.BARFORD
JRNL        TITL   THE STRUCTURE OF THE CELL CYCLE PROTEIN CDC14
JRNL        TITL 2 REVEALS A PROLINE-DIRECTED PROTEIN PHOSPHATASE
JRNL        REF    EMBO J.                       V.  22  3524 2003
JRNL        REFN                   ISSN 0261-4189
JRNL        PMID   12853468
JRNL        DOI    10.1093/EMBOJ/CDG348
REMARK   2
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS 1.1
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK   3               : READ,RICE,SIMONSON,WARREN
REMARK   3
REMARK   3  REFINEMENT TARGET : NULL
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1404031
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 96.7
REMARK   3   NUMBER OF REFLECTIONS             : 17049
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 SET) : 0.207
REMARK   3   FREE R VALUE                     : 0.253
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.9
REMARK   3   FREE R VALUE TEST SET COUNT      : 998
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.008
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 6
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.20
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.34
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 92.4
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2537
REMARK   3   BIN R VALUE           (WORKING SET) : 0.263
REMARK   3   BIN FREE R VALUE                    : 0.331
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.7
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 154
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.027
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2757
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 13
REMARK   3   SOLVENT ATOMS            : 143
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 24.0
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.9
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -5.64
REMARK   3    B22 (A**2) : 12.86
REMARK   3    B33 (A**2) : -7.22
REMARK   3    B12 (A**2) : 0.00
REMARK   3    B13 (A**2) : 2.67
REMARK   3    B23 (A**2) : 0.00
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.26
REMARK   3   ESD FROM SIGMAA              (A) : 0.25
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.33
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.33
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.013
REMARK   3   BOND ANGLES            (DEGREES) : 1.5
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.8
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.45
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.38  ; 1.50
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.24  ; 2.00
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.17  ; 2.00
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.21  ; 2.50
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : FLAT MODEL
REMARK   3   KSOL        : 0.345209
REMARK   3   BSOL        : 14.266
REMARK   3
REMARK   3  NCS MODEL : NULL
REMARK   3
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  PARAMETER FILE  1  : PARAM19X.PRO
REMARK   3  PARAMETER FILE  2  : NULL
REMARK   3  TOPOLOGY FILE  1   : TOPH19X.PRO
REMARK   3  TOPOLOGY FILE  2   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1OHE COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-MAY-03.
REMARK 100 THE PDBE ID CODE IS EBI-12790.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 15-SEP-02
REMARK 200  TEMPERATURE           (KELVIN) : 100.0
REMARK 200  PH                             : 8.00
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : ESRF
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 16051
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.2
REMARK 200  DATA REDUNDANCY                : 3.700
REMARK 200  R MERGE                    (I) : 0.07100
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 7.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.30
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.2
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.50
REMARK 200  R MERGE FOR SHELL          (I) : 0.33500
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 2.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
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  (%): 50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.6
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 8000, 0.1 M ZINC
REMARK 280  ACETATE PH 8.0, 20 OC HANGING DROP VAPOUR DIFFUSION
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,Y,-Z
REMARK 290       3555   X+1/2,Y+1/2,Z
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        0.00000
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       57.38000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       26.57500
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       57.38000
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       26.57500
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 GENERATING THE BIOMOLECULE
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: PQS
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     PRO A    39
REMARK 465     ARG A    40
REMARK 465     ARG A    41
REMARK 465     GLN A   381
REMARK 465     GLU A   382
REMARK 465     ASN A   383
REMARK 465     GLY A   384
REMARK 465     GLN A   385
REMARK 465     HIS A   386
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     ARG A  42    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ASP A  43    CG   OD1  OD2
REMARK 470     TYR A 373    CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     LYS A 377    CG   CD   CE   NZ
REMARK 470     LYS A 379    CG   CD   CE   NZ
REMARK 470     GLY A 380    CA   C    O
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    LEU A 216   CA  -  CB  -  CG  ANGL. DEV. =  18.5 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 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    PRO A  44       -3.56    -57.83
REMARK 500    TYR A  86     -111.61   -139.24
REMARK 500    ARG A 223      -42.29   -140.29
REMARK 500    ARG A 233      126.49     80.23
REMARK 500    SER A 314     -150.10   -137.45
REMARK 500    VAL A 352      102.27     65.59
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 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1OHC   RELATED DB: PDB
REMARK 900  STRUCTURE OF THE PROLINE DIRECTED PHOSPHATASE
REMARK 900   CDC14
REMARK 900 RELATED ID: 1OHD   RELATED DB: PDB
REMARK 900  STRUCTURE OF CDC14 IN COMPLEX WITH TUNGSTATE
DBREF  1OHE A   39   386  UNP    O60729   O60729          39    386
DBREF  1OHE B    0     3  PDB    1OHE     1OHE             0      3
SEQADV 1OHE SER A  314  UNP  O60729    CYS   314 CONFLICT
SEQRES   1 A  348  PRO ARG ARG ARG ASP PRO GLN ASP ASP VAL TYR LEU ASP
SEQRES   2 A  348  ILE THR ASP ARG LEU CYS PHE ALA ILE LEU TYR SER ARG
SEQRES   3 A  348  PRO LYS SER ALA SER ASN VAL HIS TYR PHE SER ILE ASP
SEQRES   4 A  348  ASN GLU LEU GLU TYR GLU ASN PHE TYR ALA ASP PHE GLY
SEQRES   5 A  348  PRO LEU ASN LEU ALA MET VAL TYR ARG TYR CYS CYS LYS
SEQRES   6 A  348  ILE ASN LYS LYS LEU LYS SER ILE THR MET LEU ARG LYS
SEQRES   7 A  348  LYS ILE VAL HIS PHE THR GLY SER ASP GLN ARG LYS GLN
SEQRES   8 A  348  ALA ASN ALA ALA PHE LEU VAL GLY CYS TYR MET VAL ILE
SEQRES   9 A  348  TYR LEU GLY ARG THR PRO GLU GLU ALA TYR ARG ILE LEU
SEQRES  10 A  348  ILE PHE GLY GLU THR SER TYR ILE PRO PHE ARG ASP ALA
SEQRES  11 A  348  ALA TYR GLY SER CYS ASN PHE TYR ILE THR LEU LEU ASP
SEQRES  12 A  348  CYS PHE HIS ALA VAL LYS LYS ALA MET GLN TYR GLY PHE
SEQRES  13 A  348  LEU ASN PHE ASN SER PHE ASN LEU ASP GLU TYR GLU HIS
SEQRES  14 A  348  TYR GLU LYS ALA GLU ASN GLY ASP LEU ASN TRP ILE ILE
SEQRES  15 A  348  PRO ASP ARG PHE ILE ALA PHE CYS GLY PRO HIS SER ARG
SEQRES  16 A  348  ALA ARG LEU GLU SER GLY TYR HIS GLN HIS SER PRO GLU
SEQRES  17 A  348  THR TYR ILE GLN TYR PHE LYS ASN HIS ASN VAL THR THR
SEQRES  18 A  348  ILE ILE ARG LEU ASN LYS ARG MET TYR ASP ALA LYS ARG
SEQRES  19 A  348  PHE THR ASP ALA GLY PHE ASP HIS HIS ASP LEU PHE PHE
SEQRES  20 A  348  ALA ASP GLY SER THR PRO THR ASP ALA ILE VAL LYS GLU
SEQRES  21 A  348  PHE LEU ASP ILE CYS GLU ASN ALA GLU GLY ALA ILE ALA
SEQRES  22 A  348  VAL HIS SER LYS ALA GLY LEU GLY ARG THR GLY THR LEU
SEQRES  23 A  348  ILE ALA CYS TYR ILE MET LYS HIS TYR ARG MET THR ALA
SEQRES  24 A  348  ALA GLU THR ILE ALA TRP VAL ARG ILE CYS ARG PRO GLY
SEQRES  25 A  348  SER VAL ILE GLY PRO GLN GLN GLN PHE LEU VAL MET LYS
SEQRES  26 A  348  GLN THR ASN LEU TRP LEU GLU GLY ASP TYR PHE ARG GLN
SEQRES  27 A  348  LYS LEU LYS GLY GLN GLU ASN GLY GLN HIS
SEQRES   1 B    4  ACE ALA SEP PRO
MODRES 1OHE SEP B    2  SER  PHOSPHOSERINE
HET    SEP  B   2      10
HET    ACE  B   0       3
HETNAM     SEP PHOSPHOSERINE
HETNAM     ACE ACETYL GROUP
HETSYN     SEP PHOSPHONOSERINE
FORMUL   2  SEP    C3 H8 N O6 P
FORMUL   3  ACE    C2 H4 O
FORMUL   4  HOH   *143(H2 O1)
HELIX    1   1 ASP A   43  ASP A   47  5                                   5
HELIX    2   2 ASN A   93  SER A  110  1                                  18
HELIX    3   3 ILE A  111  LEU A  114  5                                   4
HELIX    4   4 ASP A  125  LEU A  144  1                                  20
HELIX    5   5 THR A  147  ILE A  156  1                                  10
HELIX    6   6 THR A  178  TYR A  192  1                                  15
HELIX    7   7 ASN A  201  LYS A  210  1                                  10
HELIX    8   8 ALA A  211  GLY A  214  5                                   4
HELIX    9   9 PRO A  245  HIS A  255  1                                  11
HELIX   10  10 ALA A  270  ASP A  275  1                                   6
HELIX   11  11 THR A  292  ASN A  305  1                                  14
HELIX   12  12 LEU A  318  ARG A  334  1                                  17
HELIX   13  13 THR A  336  ARG A  348  1                                  13
HELIX   14  14 GLY A  354  LEU A  378  1                                  25
SHEET    1  AA 4 VAL A  48  ASP A  51  0
SHEET    2  AA 4 LEU A  56  ILE A  60 -1  O  PHE A  58   N  LEU A  50
SHEET    3  AA 4 LYS A 117  THR A 122  1  O  ILE A 118   N  CYS A  57
SHEET    4  AA 4 VAL A  71  SER A  75  1  O  HIS A  72   N  VAL A 119
SHEET    1  AB 5 LEU A 216  ILE A 220  0
SHEET    2  AB 5 PHE A 224  PHE A 227 -1  O  PHE A 224   N  ILE A 219
SHEET    3  AB 5 ALA A 309  HIS A 313  1  O  ILE A 310   N  ILE A 225
SHEET    4  AB 5 VAL A 257  ARG A 262  1  N  THR A 258   O  ALA A 309
SHEET    5  AB 5 ASP A 279  ASP A 282  1  O  ASP A 279   N  ILE A 260
LINK         C   ACE B   0                 N   ALA B   1     1555   1555  1.33
LINK         C   ALA B   1                 N   SEP B   2     1555   1555  1.34
LINK         C   SEP B   2                 N   PRO B   3     1555   1555  1.35
CISPEP   1 GLY A   90    PRO A   91          0         0.10
CRYST1  114.760   53.150   64.170  90.00 117.48  90.00 C 1 2 1       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      0.008714  0.000000  0.004532        0.00000
SCALE2      0.000000  0.018815  0.000000        0.00000
SCALE3      0.000000  0.000000  0.017565        0.00000
      
PROCHECK
Go to PROCHECK summary
 References