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PDBsum entry 1i8h

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Membrane protein/isomerase PDB id
1i8h
Jmol
Contents
Protein chains
13 a.a.
39 a.a. *
* Residue conservation analysis
HEADER    MEMBRANE PROTEIN/ISOMERASE              14-MAR-01   1I8H
TITLE     SOLUTION STRUCTURE OF PIN1 WW DOMAIN COMPLEXED WITH HUMAN
TITLE    2 TAU PHOSPHOTHREONINE PEPTIDE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: MICROTUBULE-ASSOCIATED PROTEIN TAU;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: (RESIDUES 541-553);
COMPND   5 SYNONYM: PHF-TAU;
COMPND   6 ENGINEERED: YES;
COMPND   7 MOL_ID: 2;
COMPND   8 MOLECULE: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE NIMA-
COMPND   9 INTERACTING 1;
COMPND  10 CHAIN: B;
COMPND  11 FRAGMENT: WW DOMAIN (RESIDUES 6-44);
COMPND  12 EC: 5.2.1.8;
COMPND  13 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 SYNTHETIC: YES;
SOURCE   3 OTHER_DETAILS: THE LIGAND PHOSPHOPEPTIDE WAS SYNTHESIZED
SOURCE   4 FROM RINK AMIDE RESIN USING FMOC STRATEGY AND ACTIVATION
SOURCE   5 BY HBTU AND HOBT IN A 431A PEPTIDE SYNTHESIZER. THE
SOURCE   6 SEQUENCE OF THE PEPTIDE IS NATURALLY FOUND IN HOMO SAPIENS
SOURCE   7 (HUMAN).;
SOURCE   8 MOL_ID: 2;
SOURCE   9 SYNTHETIC: YES;
SOURCE  10 OTHER_DETAILS: THE PIN1 WW DOMAIN WAS OBTAINED BY PEPTIDE
SOURCE  11 SYNTHESIS USING THE BOC-BENZYL STRATEGY AND THE HBTU IN
SOURCE  12 SITU ACTIVATION PROTOCOL ON AN APPLIED 430A PEPTIDE
SOURCE  13 SYNTHESIZER. THE SEQUENCE OF THE PEPTIDE IS NATURALLY
SOURCE  14 FOUND IN HOMO SAPIENS (HUMAN).
KEYWDS    CYTOSKELETON, NUCLEAR PROTEIN, MEMBRANE PROTEIN/ISOMERASE
KEYWDS   2 COMPLEX
EXPDTA    SOLUTION NMR
NUMMDL    10
AUTHOR    R.WINTJENS,J.-M.WIERUSZESKI,H.DROBECQ,G.LIPPENS,I.LANDRIEU
REVDAT   3   24-FEB-09 1I8H    1       VERSN
REVDAT   2   30-SEP-03 1I8H    1       JRNL   DBREF
REVDAT   1   18-JUL-01 1I8H    0
JRNL        AUTH   R.WINTJENS,J.M.WIERUSZESKI,H.DROBECQ,
JRNL        AUTH 2 P.ROUSSELOT-PAILLEY,L.BUEE,G.LIPPENS,I.LANDRIEU
JRNL        TITL   1H NMR STUDY ON THE BINDING OF PIN1 TRP-TRP DOMAIN
JRNL        TITL 2 WITH PHOSPHOTHREONINE PEPTIDES.
JRNL        REF    J.BIOL.CHEM.                  V. 276 25150 2001
JRNL        REFN                   ISSN 0021-9258
JRNL        PMID   11313338
JRNL        DOI    10.1074/JBC.M010327200
REMARK   1
REMARK   2
REMARK   2 RESOLUTION. NOT APPLICABLE.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : DISCOVER 2.98
REMARK   3   AUTHORS     : MOLECULAR SIMULATION INC.
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYBRID OF DISTANCE GEOMETRY /
REMARK   3  SIMULATED ANNEALING PROTOCOL MINIMIZATION PROCEDURE USING CVFF
REMARK   3  AS FORCE FIELD
REMARK   4
REMARK   4 1I8H COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-MAR-01.
REMARK 100 THE RCSB ID CODE IS RCSB013036.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210  EXPERIMENT TYPE                : NMR
REMARK 210  TEMPERATURE           (KELVIN) : 285
REMARK 210  PH                             : 6.4
REMARK 210  IONIC STRENGTH                 : 100 MM NACL
REMARK 210  PRESSURE                       : AMBIENT
REMARK 210  SAMPLE CONTENTS                : SAMPLE OF 1MM PIN1 WW DOMAIN
REMARK 210                                   / 11MM TAU LIGAND BUFFER OF 50
REMARK 210                                   MM DEUTERED TRIS-D2O, PH 6.4,
REMARK 210                                   100 MM NACL
REMARK 210
REMARK 210  NMR EXPERIMENTS CONDUCTED      : 2D NOESY
REMARK 210  SPECTROMETER FIELD STRENGTH    : 600 MHZ
REMARK 210  SPECTROMETER MODEL             : DMX
REMARK 210  SPECTROMETER MANUFACTURER      : BRUKER
REMARK 210
REMARK 210  STRUCTURE DETERMINATION.
REMARK 210   SOFTWARE USED                 : X-PLOR 3.851
REMARK 210   METHOD USED                   : DISTANCE GEOMETRY SIMULATED
REMARK 210                                   ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED   : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA  : STRUCTURES WITH THE LOWEST
REMARK 210                                   ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: NULL
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA.  PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
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  1 ARG A   6   NE  -  CZ  -  NH1 ANGL. DEV. =   4.6 DEGREES
REMARK 500  1 TRP B   6   CD1 -  NE1 -  CE2 ANGL. DEV. =  -5.6 DEGREES
REMARK 500  1 ARG B   9   NE  -  CZ  -  NH1 ANGL. DEV. =   4.9 DEGREES
REMARK 500  1 ARG B   9   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES
REMARK 500  1 ARG B  12   NE  -  CZ  -  NH1 ANGL. DEV. =   4.9 DEGREES
REMARK 500  1 ARG B  16   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES
REMARK 500  1 HIS B  22   ND1 -  CE1 -  NE2 ANGL. DEV. =   8.4 DEGREES
REMARK 500  1 ARG B  31   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES
REMARK 500  2 ARG A   6   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES
REMARK 500  2 TRP B   6   CD1 -  NE1 -  CE2 ANGL. DEV. =  -5.6 DEGREES
REMARK 500  2 ARG B   9   NE  -  CZ  -  NH1 ANGL. DEV. =   3.9 DEGREES
REMARK 500  2 ARG B  16   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES
REMARK 500  2 HIS B  22   ND1 -  CE1 -  NE2 ANGL. DEV. =   8.1 DEGREES
REMARK 500  2 ARG B  31   N   -  CA  -  CB  ANGL. DEV. = -13.3 DEGREES
REMARK 500  2 ARG B  31   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES
REMARK 500  3 ARG A   6   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES
REMARK 500  3 TRP B   6   CD1 -  NE1 -  CE2 ANGL. DEV. =  -5.7 DEGREES
REMARK 500  3 ARG B   9   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES
REMARK 500  3 ARG B  12   NE  -  CZ  -  NH1 ANGL. DEV. =   5.0 DEGREES
REMARK 500  3 ARG B  16   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES
REMARK 500  3 HIS B  22   ND1 -  CE1 -  NE2 ANGL. DEV. =   8.6 DEGREES
REMARK 500  3 ARG B  31   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES
REMARK 500  4 ARG A   6   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES
REMARK 500  4 TRP B   6   CD1 -  NE1 -  CE2 ANGL. DEV. =  -5.4 DEGREES
REMARK 500  4 ARG B   9   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES
REMARK 500  4 ARG B  12   NE  -  CZ  -  NH1 ANGL. DEV. =   4.6 DEGREES
REMARK 500  4 ARG B  12   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES
REMARK 500  4 ARG B  16   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES
REMARK 500  4 HIS B  22   ND1 -  CE1 -  NE2 ANGL. DEV. =   8.3 DEGREES
REMARK 500  4 ARG B  31   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES
REMARK 500  5 ARG A   6   NE  -  CZ  -  NH1 ANGL. DEV. =   4.2 DEGREES
REMARK 500  5 ARG A   6   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES
REMARK 500  5 TRP B   6   CD1 -  NE1 -  CE2 ANGL. DEV. =  -5.6 DEGREES
REMARK 500  5 ARG B   9   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES
REMARK 500  5 ARG B  16   NE  -  CZ  -  NH1 ANGL. DEV. =   3.9 DEGREES
REMARK 500  5 ARG B  16   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES
REMARK 500  5 HIS B  22   ND1 -  CE1 -  NE2 ANGL. DEV. =   8.4 DEGREES
REMARK 500  5 ARG B  31   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES
REMARK 500  6 TRP B   6   CD1 -  NE1 -  CE2 ANGL. DEV. =  -5.8 DEGREES
REMARK 500  6 ARG B   9   NE  -  CZ  -  NH1 ANGL. DEV. =   4.1 DEGREES
REMARK 500  6 ARG B  12   NE  -  CZ  -  NH1 ANGL. DEV. =   4.2 DEGREES
REMARK 500  6 ARG B  16   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES
REMARK 500  6 HIS B  22   ND1 -  CE1 -  NE2 ANGL. DEV. =   8.3 DEGREES
REMARK 500  6 ARG B  31   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES
REMARK 500  7 ARG A   6   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES
REMARK 500  7 TRP B   6   CD1 -  NE1 -  CE2 ANGL. DEV. =  -5.6 DEGREES
REMARK 500  7 ARG B   9   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES
REMARK 500  7 ARG B  12   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES
REMARK 500  7 ARG B  16   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES
REMARK 500  7 VAL B  17   CB  -  CA  -  C   ANGL. DEV. =  11.6 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS      80 ANGLE DEVIATIONS.
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  1 PRO A   9     -117.62    -83.06
REMARK 500  1 PRO A  12       49.56    -78.19
REMARK 500  1 SER B  11      146.63     74.99
REMARK 500  1 ARG B  12      -68.64   -130.00
REMARK 500  1 SER B  13      -70.65   -115.68
REMARK 500  1 VAL B  17      148.66    135.10
REMARK 500  1 TYR B  18      -48.20   -135.95
REMARK 500  1 ASN B  25       68.41     77.97
REMARK 500  1 PRO B  32       17.90    -60.52
REMARK 500  1 SER B  33      -76.69     67.58
REMARK 500  1 SER B  37      -59.49   -148.60
REMARK 500  2 VAL A   5      112.42     76.94
REMARK 500  2 PRO A   9     -111.37    -80.06
REMARK 500  2 LEU B   2      163.62     50.41
REMARK 500  2 SER B  11       64.99     60.68
REMARK 500  2 SER B  13     -112.29   -144.64
REMARK 500  2 VAL B  17      135.76     73.27
REMARK 500  2 TYR B  18        7.07   -175.02
REMARK 500  2 ASN B  25       67.91     79.04
REMARK 500  2 SER B  33      -41.10     73.00
REMARK 500  2 SER B  36      -62.10   -136.82
REMARK 500  3 SER A   3      -65.82    -94.41
REMARK 500  3 GLU B   7     -154.58   -145.17
REMARK 500  3 SER B  11       75.83     71.59
REMARK 500  3 SER B  13     -157.03   -144.23
REMARK 500  3 VAL B  17      129.87     85.84
REMARK 500  3 TYR B  18        5.69   -177.09
REMARK 500  3 ASN B  25       65.55     82.76
REMARK 500  3 TRP B  29       42.54   -101.01
REMARK 500  4 VAL A   4     -115.47     68.21
REMARK 500  4 GLU B   7     -151.01   -145.38
REMARK 500  4 SER B  11      132.35     71.05
REMARK 500  4 ARG B  12      -56.21   -124.87
REMARK 500  4 SER B  14      -54.72   -158.47
REMARK 500  4 VAL B  17      130.69     79.73
REMARK 500  4 TYR B  18        4.32   -175.34
REMARK 500  4 ASN B  25       74.85     75.79
REMARK 500  4 SER B  33      -65.01     72.68
REMARK 500  5 VAL A   5      106.10     65.58
REMARK 500  5 GLU B   7     -155.15   -145.71
REMARK 500  5 SER B  11     -163.10     65.93
REMARK 500  5 ARG B  12      -75.18   -124.87
REMARK 500  5 SER B  14      -27.69   -155.70
REMARK 500  5 VAL B  17      141.44     71.82
REMARK 500  5 TYR B  18       10.48   -170.39
REMARK 500  5 ASN B  25       65.98     76.21
REMARK 500  5 PRO B  32        6.50    -61.25
REMARK 500  5 SER B  33      -63.31     78.77
REMARK 500  6 VAL A   2      -95.31     56.52
REMARK 500  6 SER A   3      -42.40     70.14
REMARK 500  6 PRO A   9     -103.26    -70.83
REMARK 500  6 SER A  11      155.94    -49.99
REMARK 500  6 SER B  14       96.30    -68.75
REMARK 500  6 VAL B  17      132.79     66.23
REMARK 500  6 TYR B  18        2.57   -165.80
REMARK 500  6 ASN B  25       58.83     82.60
REMARK 500  6 PRO B  32       11.11    -64.76
REMARK 500  6 SER B  33      -70.58     73.60
REMARK 500  6 SER B  38      -75.26   -140.97
REMARK 500  7 VAL A   5      119.08     71.49
REMARK 500  7 PRO A  12       70.03      4.17
REMARK 500  7 LEU B   2      175.76     47.82
REMARK 500  7 SER B  11      131.29     67.70
REMARK 500  7 ARG B  12      -68.92   -133.61
REMARK 500  7 VAL B  17      148.56    110.40
REMARK 500  7 TYR B  18       12.23   -170.46
REMARK 500  7 ASN B  25       64.74     83.72
REMARK 500  7 PRO B  32       65.70    -69.21
REMARK 500  7 SER B  38      -42.70   -171.92
REMARK 500  8 VAL A   4      127.75     75.75
REMARK 500  8 LYS A  10      104.02    -54.71
REMARK 500  8 SER B  11      157.85     78.42
REMARK 500  8 ARG B  12      -50.55   -151.42
REMARK 500  8 SER B  13      -61.89   -100.16
REMARK 500  8 VAL B  17      124.84     73.45
REMARK 500  8 TYR B  18       18.30   -172.29
REMARK 500  8 SER B  33      -49.81     86.18
REMARK 500  8 SER B  38      -52.36   -163.00
REMARK 500  9 SER A   3       77.86   -106.37
REMARK 500  9 VAL A   5      111.86     73.60
REMARK 500  9 SER A  11      149.06    -36.69
REMARK 500  9 GLU B   7     -148.62   -147.75
REMARK 500  9 SER B  11       62.11     65.57
REMARK 500  9 SER B  14      102.26    -35.23
REMARK 500  9 VAL B  17      135.45     99.46
REMARK 500  9 TYR B  18        9.49   -173.74
REMARK 500  9 ALA B  26       96.85    -58.90
REMARK 500  9 TRP B  29       49.12   -102.42
REMARK 500  9 SER B  33      -47.97     69.31
REMARK 500  9 SER B  36      -68.23    124.87
REMARK 500  9 SER B  38      -60.91    170.23
REMARK 500 10 VAL A   4      141.35     73.05
REMARK 500 10 PRO A   9     -111.61    -80.25
REMARK 500 10 SER A  11      168.65    -35.51
REMARK 500 10 GLU B   7     -148.10   -145.95
REMARK 500 10 SER B  11       87.33     46.70
REMARK 500 10 SER B  13       55.49   -160.60
REMARK 500 10 SER B  14     -114.34   -164.82
REMARK 500 10 VAL B  17      131.46     93.31
REMARK 500 10 TYR B  18        8.73   -177.83
REMARK 500 10 ASN B  25       73.02     77.50
REMARK 500 10 GLU B  30       38.89   -157.56
REMARK 500 10 ARG B  31      142.67     54.28
REMARK 500 10 PRO B  32        3.24    -69.45
REMARK 500 10 SER B  33      -47.72     78.07
REMARK 500 10 ASN B  35      -44.66   -132.04
REMARK 500 10 SER B  38      -83.30   -144.17
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 TRP B    6     GLU B    7          1       147.35
REMARK 500 SER B   38     GLY B   39          1      -145.44
REMARK 500 TRP B    6     GLU B    7          2       147.42
REMARK 500 ARG B    9     MET B   10          2      -138.12
REMARK 500 MET B   10     SER B   11          2       137.23
REMARK 500 SER B   37     SER B   38          2       138.47
REMARK 500 PRO A    9     LYS A   10          3      -144.89
REMARK 500 TRP B    6     GLU B    7          3       147.32
REMARK 500 ARG B    9     MET B   10          3      -139.80
REMARK 500 ARG B    9     MET B   10          4      -130.67
REMARK 500 ARG B   16     VAL B   17          4      -144.58
REMARK 500 LYS A   10     SER A   11          5       107.94
REMARK 500 PRO A   12     SER A   13          5       140.07
REMARK 500 TRP B    6     GLU B    7          5       149.72
REMARK 500 ARG B   12     SER B   13          5       144.98
REMARK 500 ARG A    6     TPO A    7          6       141.18
REMARK 500 TRP B    6     GLU B    7          6       144.67
REMARK 500 MET B   10     SER B   11          6       137.50
REMARK 500 SER B   38     GLY B   39          6      -138.59
REMARK 500 ARG A    6     TPO A    7          7       131.91
REMARK 500 SER A   11     PRO A   12          7      -148.61
REMARK 500 PRO A   12     SER A   13          7       129.20
REMARK 500 GLU B    7     LYS B    8          7       142.76
REMARK 500 SER B   38     GLY B   39          7      -133.20
REMARK 500 ARG B    9     MET B   10          8      -132.43
REMARK 500 ARG B   16     VAL B   17          8      -142.68
REMARK 500 SER B   38     GLY B   39          8      -141.36
REMARK 500 TRP B    6     GLU B    7          9       149.74
REMARK 500 TRP B   29     GLU B   30          9      -148.95
REMARK 500 SER B   37     SER B   38          9      -145.50
REMARK 500 SER B   38     GLY B   39          9      -131.91
REMARK 500 LYS A   10     SER A   11         10       113.38
REMARK 500 SER B   38     GLY B   39         10      -119.39
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500  M RES CSSEQI        RMS     TYPE
REMARK 500  1 TYR B  18         0.18    SIDE_CHAIN
REMARK 500  2 ARG B  12         0.24    SIDE_CHAIN
REMARK 500  2 TYR B  18         0.18    SIDE_CHAIN
REMARK 500  2 ARG B  31         0.11    SIDE_CHAIN
REMARK 500  3 ARG B   9         0.12    SIDE_CHAIN
REMARK 500  3 TYR B  18         0.14    SIDE_CHAIN
REMARK 500  4 ARG A   6         0.15    SIDE_CHAIN
REMARK 500  4 ARG B   9         0.13    SIDE_CHAIN
REMARK 500  4 TYR B  18         0.14    SIDE_CHAIN
REMARK 500  4 TYR B  19         0.07    SIDE_CHAIN
REMARK 500  5 ARG A   6         0.13    SIDE_CHAIN
REMARK 500  5 ARG B   9         0.12    SIDE_CHAIN
REMARK 500  5 ARG B  12         0.22    SIDE_CHAIN
REMARK 500  5 TYR B  18         0.15    SIDE_CHAIN
REMARK 500  6 ARG A   6         0.15    SIDE_CHAIN
REMARK 500  6 TYR B  18         0.15    SIDE_CHAIN
REMARK 500  7 ARG B   9         0.13    SIDE_CHAIN
REMARK 500  7 ARG B  12         0.14    SIDE_CHAIN
REMARK 500  7 TYR B  18         0.15    SIDE_CHAIN
REMARK 500  7 ARG B  31         0.08    SIDE_CHAIN
REMARK 500  8 ARG A   6         0.10    SIDE_CHAIN
REMARK 500  8 ARG B   9         0.14    SIDE_CHAIN
REMARK 500  8 ARG B  12         0.10    SIDE_CHAIN
REMARK 500  8 TYR B  18         0.15    SIDE_CHAIN
REMARK 500  9 ARG B   9         0.12    SIDE_CHAIN
REMARK 500  9 TYR B  18         0.16    SIDE_CHAIN
REMARK 500 10 ARG B   9         0.14    SIDE_CHAIN
REMARK 500 10 TYR B  18         0.19    SIDE_CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1I6C   RELATED DB: PDB
REMARK 900 1I6C CONTAINS THE SAME PROTEIN IN A FREE (NOT COMPLEXED)
REMARK 900 FORM
REMARK 900 RELATED ID: 1I8G   RELATED DB: PDB
REMARK 900 1I8G CONTAINS THE SAME PROTEIN COMPLEXED WITH A CDC25
REMARK 900 PHOSPHOPEPTIDE
DBREF  1I8H A    1    13  UNP    P10636   TAU_HUMAN      541    553
DBREF  1I8H B    1    39  UNP    Q13526   PIN1_HUMAN       6     44
SEQADV 1I8H SER A    3  UNP  P10636    ALA   543 ENGINEERED
SEQADV 1I8H TPO A    7  UNP  P10636    THR   547 MODIFIED RESIDUE
SEQRES   1 A   13  LYS VAL SER VAL VAL ARG TPO PRO PRO LYS SER PRO SER
SEQRES   1 B   39  LYS LEU PRO PRO GLY TRP GLU LYS ARG MET SER ARG SER
SEQRES   2 B   39  SER GLY ARG VAL TYR TYR PHE ASN HIS ILE THR ASN ALA
SEQRES   3 B   39  SER GLN TRP GLU ARG PRO SER GLY ASN SER SER SER GLY
MODRES 1I8H TPO A    7  THR  PHOSPHOTHREONINE
HET    TPO  A   7      17
HETNAM     TPO PHOSPHOTHREONINE
HETSYN     TPO PHOSPHONOTHREONINE
FORMUL   1  TPO    C4 H10 N O6 P
SHEET    1   A 3 TRP B   6  MET B  10  0
SHEET    2   A 3 VAL B  17  ASN B  21 -1  O  TYR B  18   N  ARG B   9
SHEET    3   A 3 ALA B  26  GLN B  28 -1  O  ALA B  26   N  ASN B  21
LINK         C   ARG A   6                 N   TPO A   7     1555   1555  1.34
LINK         C   TPO A   7                 N   PRO A   8     1555   1555  1.37
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           1
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      1.000000  0.000000  0.000000        0.00000
SCALE2      0.000000  1.000000  0.000000        0.00000
SCALE3      0.000000  0.000000  1.000000        0.00000
      
PROCHECK
Go to PROCHECK summary
 References