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PDBsum entry 1f8a

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Isomerase PDB id
1f8a
Jmol
Contents
Protein chain
155 a.a. *
Ligands
TYR-SEP-PRO-THR-
SEP-PRO-SER
Waters ×152
* Residue conservation analysis
HEADER    ISOMERASE                               29-JUN-00   1F8A
TITLE     STRUCTURAL BASIS FOR THE PHOSPHOSERINE-PROLINE RECOGNITION BY GROUP IV
TITLE    2 WW DOMAINS
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE NIMA-INTERACTING 1;
COMPND   3 CHAIN: B;
COMPND   4 SYNONYM: PIN1;
COMPND   5 EC: 5.2.1.8;
COMPND   6 ENGINEERED: YES;
COMPND   7 MOL_ID: 2;
COMPND   8 MOLECULE: Y(SEP)PT(SEP)S PEPTIDE;
COMPND   9 CHAIN: C;
COMPND  10 ENGINEERED: 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 MOL_ID: 2;
SOURCE   8 SYNTHETIC: YES;
SOURCE   9 OTHER_DETAILS: SOLID-PHASE PEPTIDE SYNTHESIS
KEYWDS    PEPTIDYL-PROLINE ISOMERASE, WW DOMAIN, PHOSPHOSERINE BINDING,
KEYWDS   2 ISOMERASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    M.A.VERDECIA,M.E.BOWMAN,K.P.LU,T.HUNTER,J.P.NOEL
REVDAT   3   22-MAY-13 1F8A    1       LINK   REMARK VERSN
REVDAT   2   24-FEB-09 1F8A    1       VERSN
REVDAT   1   23-AUG-00 1F8A    0
JRNL        AUTH   M.A.VERDECIA,M.E.BOWMAN,K.P.LU,T.HUNTER,J.P.NOEL
JRNL        TITL   STRUCTURAL BASIS FOR PHOSPHOSERINE-PROLINE RECOGNITION BY
JRNL        TITL 2 GROUP IV WW DOMAINS.
JRNL        REF    NAT.STRUCT.BIOL.              V.   7   639 2000
JRNL        REFN                   ISSN 1072-8368
JRNL        PMID   10932246
JRNL        DOI    10.1038/77929
REMARK   2
REMARK   2 RESOLUTION.    1.84 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS 1.0
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 : ENGH & HUBER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.84
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.41
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1085629.020
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 97.5
REMARK   3   NUMBER OF REFLECTIONS             : 17107
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) : 0.231
REMARK   3   FREE R VALUE                     : 0.271
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 866
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.009
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) : 1.84
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.96
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 94.60
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2555
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2390
REMARK   3   BIN FREE R VALUE                    : 0.2900
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.40
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 147
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.024
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 1294
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 0
REMARK   3   SOLVENT ATOMS            : 152
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 17.40
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.30
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 2.03000
REMARK   3    B22 (A**2) : 3.30000
REMARK   3    B33 (A**2) : -5.32000
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 COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.23
REMARK   3   ESD FROM SIGMAA              (A) : 0.11
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) : 0.28
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.12
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.029
REMARK   3   BOND ANGLES            (DEGREES) : 2.60
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 25.10
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.48
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) : 0.850 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.550 ; 2.000
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.440 ; 2.000
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.040 ; 2.500
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : FLAT MODEL
REMARK   3   KSOL        : 0.37
REMARK   3   BSOL        : 36.00
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  : PROTEIN_REP.PARAM
REMARK   3  PARAMETER FILE  2  : ION.PARAM
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM
REMARK   3  PARAMETER FILE  4  : NULL
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP
REMARK   3  TOPOLOGY FILE  2   : ION.TOP
REMARK   3  TOPOLOGY FILE  3   : WATER_REP.TOP
REMARK   3  TOPOLOGY FILE  4   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1F8A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-JUL-00.
REMARK 100 THE RCSB ID CODE IS RCSB011365.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 15-APR-99
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               : 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) : 0.98
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : MACSCIENCE DIP100S
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 293095
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.840
REMARK 200  RESOLUTION RANGE LOW       (A) : 62.020
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.3
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : 0.06200
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 21.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.84
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.90
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.2
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.33700
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: NULL
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 50.25
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM MOPSO-NA+, 28% PEG 8000, 2 MM
REMARK 280  DTT, PH 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298.0K
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       17.63500
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       62.32950
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       21.95150
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       62.32950
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       17.63500
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       21.95150
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 ASSEMBLY IS A MONOMER OF PIN1 BOUND TO THE
REMARK 300 PHOSPHORYLATED PEPTIDE
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: 1010 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9870 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C
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     GLY B    43
REMARK 465     ASN B    44
REMARK 465     SER B    45
REMARK 465     SER B    46
REMARK 465     SER B    47
REMARK 465     GLY B    48
REMARK 465     GLY B    49
REMARK 465     LYS B    50
REMARK 465     ASN B    51
REMARK 465     GLY B    52
REMARK 465     GLN B    53
REMARK 465     GLY B    54
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    GLU B   9   N   -  CA  -  C   ANGL. DEV. =  25.7 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    GLU B   9     -178.62     28.83
REMARK 500    LYS B  10      -91.18   -128.97
REMARK 500    LEU B  11      104.61     73.36
REMARK 500    ARG B  72       68.16   -165.33
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS
REMARK 500    GLU B   9        18.0      L          L   OUTSIDE RANGE
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 B 322        DISTANCE =  5.46 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1PIN   RELATED DB: PDB
REMARK 900 1PIN CONTAINS THE SAME PROTEIN BUT NOT COMPLEXED
DBREF  1F8A B    5   167  UNP    Q13526   PIN1_HUMAN       1    163
DBREF  1F8A C  170   176  PDB    1F8A     1F8A           170    176
SEQADV 1F8A GLY B    1  UNP  Q13526              CLONING ARTIFACT
SEQADV 1F8A SER B    2  UNP  Q13526              CLONING ARTIFACT
SEQADV 1F8A HIS B    3  UNP  Q13526              CLONING ARTIFACT
SEQADV 1F8A GLY B    4  UNP  Q13526              CLONING ARTIFACT
SEQRES   1 B  167  GLY SER HIS GLY MET ALA ASP GLU GLU LYS LEU PRO PRO
SEQRES   2 B  167  GLY TRP GLU LYS ARG MET SER ARG SER SER GLY ARG VAL
SEQRES   3 B  167  TYR TYR PHE ASN HIS ILE THR ASN ALA SER GLN TRP GLU
SEQRES   4 B  167  ARG PRO SER GLY ASN SER SER SER GLY GLY LYS ASN GLY
SEQRES   5 B  167  GLN GLY GLU PRO ALA ARG VAL ARG CYS SER HIS LEU LEU
SEQRES   6 B  167  VAL LYS HIS SER GLN SER ARG ARG PRO SER SER TRP ARG
SEQRES   7 B  167  GLN GLU LYS ILE THR ARG THR LYS GLU GLU ALA LEU GLU
SEQRES   8 B  167  LEU ILE ASN GLY TYR ILE GLN LYS ILE LYS SER GLY GLU
SEQRES   9 B  167  GLU ASP PHE GLU SER LEU ALA SER GLN PHE SER ASP CYS
SEQRES  10 B  167  SER SER ALA LYS ALA ARG GLY ASP LEU GLY ALA PHE SER
SEQRES  11 B  167  ARG GLY GLN MET GLN LYS PRO PHE GLU ASP ALA SER PHE
SEQRES  12 B  167  ALA LEU ARG THR GLY GLU MET SER GLY PRO VAL PHE THR
SEQRES  13 B  167  ASP SER GLY ILE HIS ILE ILE LEU ARG THR GLU
SEQRES   1 C    7  TYR SEP PRO THR SEP PRO SER
MODRES 1F8A SEP C  171  SER  PHOSPHOSERINE
MODRES 1F8A SEP C  174  SER  PHOSPHOSERINE
HET    SEP  C 171      10
HET    SEP  C 174      10
HETNAM     SEP PHOSPHOSERINE
HETSYN     SEP PHOSPHONOSERINE
FORMUL   2  SEP    2(C3 H8 N O6 P)
FORMUL   3  HOH   *152(H2 O)
HELIX    1   1 THR B   85  SER B  102  1                                  18
HELIX    2   2 ASP B  106  SER B  115  1                                  10
HELIX    3   3 CYS B  117  ARG B  123  5                                   7
HELIX    4   4 GLN B  135  LEU B  145  1                                  11
SHEET    1   A 3 TRP B  15  MET B  19  0
SHEET    2   A 3 VAL B  26  ASN B  30 -1  O  TYR B  27   N  ARG B  18
SHEET    3   A 3 SER B  36  GLN B  37 -1  O  GLN B  37   N  TYR B  28
SHEET    1   B 4 ASP B 125  PHE B 129  0
SHEET    2   B 4 VAL B  59  VAL B  66 -1  O  VAL B  59   N  PHE B 129
SHEET    3   B 4 GLY B 159  GLU B 167 -1  O  ILE B 160   N  VAL B  66
SHEET    4   B 4 VAL B 154  THR B 156 -1  O  VAL B 154   N  HIS B 161
LINK         C   TYR C 170                 N   SEP C 171     1555   1555  1.31
LINK         C   SEP C 171                 N   PRO C 172     1555   1555  1.48
LINK         C   THR C 173                 N   SEP C 174     1555   1555  1.33
LINK         C   SEP C 174                 N   PRO C 175     1555   1555  1.34
CRYST1   35.270   43.903  124.659  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      0.028353  0.000000  0.000000        0.00000
SCALE2      0.000000  0.022777  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008022        0.00000
      
PROCHECK
Go to PROCHECK summary
 References