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PDBsum entry 1xke

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Protein transport PDB id
1xke
Jmol
Contents
Protein chain
130 a.a.
HEADER    PROTEIN TRANSPORT                       28-SEP-04   1XKE
TITLE     SOLUTION STRUCTURE OF THE SECOND RAN-BINDING DOMAIN FROM
TITLE    2 HUMAN RANBP2
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: RAN-BINDING PROTEIN 2;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: RAN-BINDING DOMAIN 2 (RANBD2);
COMPND   5 SYNONYM: RANBP2, NUCLEAR PORE COMPLEX PROTEIN NUP358,
COMPND   6 NUCLEOPORIN NUP358, 358 KDA NUCLEOPORIN, P270;
COMPND   7 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 BL21(DE3);
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PGEX-2T
KEYWDS    BETA BARREL, PLECKSTRIN-HOMOLOGY (PH) DOMAIN,
KEYWDS   2 PHOSPHOTYROSINE-BINDING (PTB) DOMAIN, PROTEIN TRANSPORT
EXPDTA    SOLUTION NMR
NUMMDL    20
AUTHOR    J.P.GEYER,R.DOEKER,W.KREMER,X.ZHAO,J.KUHLMANN,H.R.KALBITZER
REVDAT   2   24-FEB-09 1XKE    1       VERSN
REVDAT   1   19-APR-05 1XKE    0
JRNL        AUTH   J.P.GEYER,R.DOKER,W.KREMER,X.ZHAO,J.KUHLMANN,
JRNL        AUTH 2 H.R.KALBITZER
JRNL        TITL   SOLUTION STRUCTURE OF THE RAN-BINDING DOMAIN 2 OF
JRNL        TITL 2 RANBP2 AND ITS INTERACTION WITH THE C TERMINUS OF
JRNL        TITL 3 RAN.
JRNL        REF    J.MOL.BIOL.                   V. 348   711 2005
JRNL        REFN                   ISSN 0022-2836
JRNL        PMID   15826666
JRNL        DOI    10.1016/J.JMB.2005.02.033
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   R.DOEKER,X.ZHAO,W.KREMER,B.VILLA,J.KUHLMANN,
REMARK   1  AUTH 2 H.R.KALBITZER
REMARK   1  TITL   SEQUENCE-SPECIFIC RESONANCE ASSIGNMENT OF THE
REMARK   1  TITL 2 SECOND RAN-BINDING DOMAIN OF HUMAN RANBP2
REMARK   1  REF    J.BIOMOL.NMR                  V.  22   185 2002
REMARK   1  REFN                   ISSN 0925-2738
REMARK   1  PMID   11883781
REMARK   1  DOI    10.1023/A:1014275704491
REMARK   2
REMARK   2 RESOLUTION. NOT APPLICABLE.
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,READ,
REMARK   3                 RICE,SIMONSON,WARREN
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL
REMARK   3  OF 1492 RESTRAINTS (1281 NOE-DERIVED DISTANCE RESTRAINTS, 182
REMARK   3  DIHEDRAL ANGLE RESTRAINTS AND 29 HYDROGEN BOND RESTRAINTS).
REMARK   3  THE STRUCTURES WERE ALSO REFINED IN WATER USING XPLOR-NIH
REMARK   3  2.9.6 USING THE PROTOCOL OF LINGE ET AL. (LINGE, J. P.,
REMARK   3  WILLIAMS, M. A., SPRONK, C. A., BONVIN, A. M., & NILGES, M. ,
REMARK   3  2003. REFINEMENT OF PROTEIN STRUCTURES IN EXPLICIT SOLVENT.
REMARK   3  PROTEINS 50, 496-506).
REMARK   4
REMARK   4 1XKE COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-OCT-04.
REMARK 100 THE RCSB ID CODE IS RCSB030454.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210  EXPERIMENT TYPE                : NMR
REMARK 210  TEMPERATURE           (KELVIN) : 298
REMARK 210  PH                             : 6.5
REMARK 210  IONIC STRENGTH                 : 150 MM NA2SO4
REMARK 210  PRESSURE                       : AMBIENT
REMARK 210  SAMPLE CONTENTS                : 1.4MM RANBD2 U-13C; U-15N;
REMARK 210                                   150MM NA2SO4; 10MM DTE; 0.5 MM
REMARK 210                                   EDTA; 1MM NAN3; 0.1MM DSS;
REMARK 210                                   10MM POTASSIUM PHOSPHATE
REMARK 210                                   BUFFER AT PH 6.5;; 0.7MM
REMARK 210                                   RANBD2 U-13C; U-15N; 150MM
REMARK 210                                   NA2SO4; 10MM DTE; 0.5MM EDTA;
REMARK 210                                   1MM NAN3; 0.1MM DSS; 10MM
REMARK 210                                   POTASSIUM PHOSPHATE BUFFER AT
REMARK 210                                   PH 6.5;; 1.0MM RANBD2 U-15N;
REMARK 210                                   150MM NA2SO4; 10MM DTE; 0.5MM
REMARK 210                                   EDTA; 1MM NAN3; 0.1 MM DSS;
REMARK 210                                   10MM POTASSIUM PHOSPHATE
REMARK 210                                   BUFFER AT PH 6.5;; 1.0MM
REMARK 210                                   RANBD2 U-15N; 150MM NA2SO4;
REMARK 210                                   10MM DTE; 0.5MM EDTA; 1MM
REMARK 210                                   NAN3; 0.1MM DSS; 10MM
REMARK 210                                   POTASSIUM PHOSPHATE BUFFER AT
REMARK 210                                   PH 6.5;
REMARK 210
REMARK 210  NMR EXPERIMENTS CONDUCTED      : 2D NOESY, 3D_15N-SEPARATED_
REMARK 210                                   NOESY, 3D_13C-SEPARATED_NOESY
REMARK 210  SPECTROMETER FIELD STRENGTH    : 600 MHZ, 800 MHZ
REMARK 210  SPECTROMETER MODEL             : DRX
REMARK 210  SPECTROMETER MANUFACTURER      : BRUKER
REMARK 210
REMARK 210  STRUCTURE DETERMINATION.
REMARK 210   SOFTWARE USED                 : XWINNMR 2.6, AUREMOL 2.0.3,
REMARK 210                                   CNS 1.1, XPLOR-NIH 2.9.6
REMARK 210   METHOD USED                   : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED   : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 20
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 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  1 MET A  50   N     MET A  50   CA     -0.132
REMARK 500  1 MET A  50   C     ARG A  51   N      -0.150
REMARK 500  1 GLN A  96   N     GLN A  96   CA     -0.125
REMARK 500  2 MET A  50   N     MET A  50   CA     -0.137
REMARK 500  2 MET A  50   C     ARG A  51   N      -0.157
REMARK 500  2 GLN A  96   N     GLN A  96   CA     -0.139
REMARK 500  3 ARG A  19   C     PHE A  20   N      -0.139
REMARK 500  3 MET A  50   N     MET A  50   CA     -0.144
REMARK 500  3 MET A  50   C     ARG A  51   N      -0.154
REMARK 500  3 GLN A  96   N     GLN A  96   CA     -0.135
REMARK 500  4 MET A  50   N     MET A  50   CA     -0.142
REMARK 500  4 MET A  50   C     ARG A  51   N      -0.150
REMARK 500  4 MET A  81   C     TRP A  82   N      -0.141
REMARK 500  4 GLN A  96   N     GLN A  96   CA     -0.135
REMARK 500  5 MET A  50   N     MET A  50   CA     -0.144
REMARK 500  5 MET A  50   C     ARG A  51   N      -0.160
REMARK 500  5 ASP A  86   N     ASP A  86   CA     -0.125
REMARK 500  5 GLN A  96   N     GLN A  96   CA     -0.125
REMARK 500  5 PRO A 104   C     PRO A 104   O      -0.121
REMARK 500  6 MET A  50   N     MET A  50   CA     -0.131
REMARK 500  6 MET A  50   C     ARG A  51   N      -0.143
REMARK 500  6 GLN A  96   N     GLN A  96   CA     -0.126
REMARK 500  7 MET A  50   N     MET A  50   CA     -0.143
REMARK 500  7 MET A  50   C     ARG A  51   N      -0.161
REMARK 500  7 GLN A  96   N     GLN A  96   CA     -0.123
REMARK 500  8 MET A  50   C     ARG A  51   N      -0.153
REMARK 500  9 MET A  50   N     MET A  50   CA     -0.129
REMARK 500  9 MET A  50   C     ARG A  51   N      -0.150
REMARK 500  9 GLY A  90   N     GLY A  90   CA     -0.090
REMARK 500  9 GLN A  96   N     GLN A  96   CA     -0.124
REMARK 500  9 LYS A 100   C     PHE A 101   N      -0.139
REMARK 500 10 LEU A  35   N     LEU A  35   CA     -0.128
REMARK 500 10 MET A  50   N     MET A  50   CA     -0.146
REMARK 500 10 MET A  50   C     ARG A  51   N      -0.151
REMARK 500 10 GLY A  90   N     GLY A  90   CA     -0.092
REMARK 500 10 GLN A  96   N     GLN A  96   CA     -0.128
REMARK 500 11 MET A  50   N     MET A  50   CA     -0.128
REMARK 500 11 MET A  50   C     ARG A  51   N      -0.141
REMARK 500 12 MET A  50   N     MET A  50   CA     -0.141
REMARK 500 12 MET A  50   C     ARG A  51   N      -0.162
REMARK 500 12 ASP A  91   C     ALA A  92   N      -0.144
REMARK 500 12 GLN A  96   N     GLN A  96   CA     -0.120
REMARK 500 13 MET A  50   N     MET A  50   CA     -0.158
REMARK 500 13 MET A  50   C     ARG A  51   N      -0.162
REMARK 500 13 MET A  81   C     TRP A  82   N      -0.142
REMARK 500 13 GLY A  90   N     GLY A  90   CA     -0.097
REMARK 500 13 GLN A  96   N     GLN A  96   CA     -0.135
REMARK 500 14 MET A  50   N     MET A  50   CA     -0.142
REMARK 500 14 MET A  50   C     ARG A  51   N      -0.163
REMARK 500 14 GLN A  96   N     GLN A  96   CA     -0.121
REMARK 500
REMARK 500 THIS ENTRY HAS      68 BOND 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 GLU A   5     -157.92   -140.83
REMARK 500  1 LEU A  56       10.82     52.48
REMARK 500  1 VAL A  58      124.87    -37.64
REMARK 500  1 PHE A  87       61.66   -158.45
REMARK 500  1 ASP A  89       33.87    177.93
REMARK 500  1 ASP A  91      125.97     80.51
REMARK 500  1 PRO A 104       -8.07    -55.95
REMARK 500  2 SER A   2      -79.89     64.58
REMARK 500  2 GLU A   4       43.36   -102.33
REMARK 500  2 ASP A   6       -0.41     88.26
REMARK 500  2 LEU A  10      -65.53    -92.12
REMARK 500  2 GLU A  53      -76.46    -45.45
REMARK 500  2 LEU A  56       10.40     51.31
REMARK 500  2 VAL A  58      122.11    -28.91
REMARK 500  2 ARG A  78       39.12   -152.64
REMARK 500  2 PHE A  87      109.51    158.54
REMARK 500  2 ASP A  91      132.50     86.29
REMARK 500  3 ASP A   6        3.39     81.62
REMARK 500  3 LEU A  56       10.91     52.59
REMARK 500  3 VAL A  58      116.39    -28.95
REMARK 500  3 ARG A  78       37.03   -149.95
REMARK 500  3 PHE A  87       21.03   -141.17
REMARK 500  3 ASP A  89       10.63   -152.75
REMARK 500  3 ASP A  91      159.80     70.92
REMARK 500  4 GLU A   5     -143.18   -129.19
REMARK 500  4 ASP A   6       -1.64    104.19
REMARK 500  4 LEU A  10      -68.41    -94.77
REMARK 500  4 LEU A  56       10.90     50.31
REMARK 500  4 VAL A  58      123.85    -29.97
REMARK 500  4 ARG A  78       48.79   -167.79
REMARK 500  4 PHE A  87       79.78   -152.25
REMARK 500  4 ASP A  89       36.25    162.53
REMARK 500  4 ASP A  91      144.69    178.75
REMARK 500  5 ASP A   6      -12.88    146.68
REMARK 500  5 GLU A  53      -73.31    -48.09
REMARK 500  5 LEU A  56        9.56     52.16
REMARK 500  5 VAL A  58      125.85    -30.39
REMARK 500  5 ARG A  78       43.98    177.45
REMARK 500  5 PHE A  87      108.74   -168.83
REMARK 500  5 ASP A  89       45.05    159.95
REMARK 500  6 SER A   2       86.92   -153.15
REMARK 500  6 GLU A   4       70.26     49.57
REMARK 500  6 GLU A   5     -167.38   -120.27
REMARK 500  6 ASN A  43      -14.23    153.58
REMARK 500  6 GLU A  53      -73.74    -48.50
REMARK 500  6 LEU A  56        9.42     50.58
REMARK 500  6 VAL A  58      126.11    -33.52
REMARK 500  6 ARG A  78       40.74   -167.64
REMARK 500  6 PHE A  87       79.81    176.94
REMARK 500  6 ASP A  89       31.93    171.79
REMARK 500  6 GLN A 127       75.20     54.71
REMARK 500  7 SER A   2      -41.81   -130.87
REMARK 500  7 GLU A   5     -162.25   -114.81
REMARK 500  7 ASP A   6        6.18     80.61
REMARK 500  7 LEU A  56       11.20     51.00
REMARK 500  7 VAL A  58      112.34    -29.63
REMARK 500  7 ARG A  78       45.44   -168.54
REMARK 500  7 PHE A  87       76.02     93.95
REMARK 500  7 ASP A  91      124.90     96.62
REMARK 500  8 LEU A  10      -68.23    -91.22
REMARK 500  8 ASN A  43       34.70     71.51
REMARK 500  8 LEU A  56       11.54     52.93
REMARK 500  8 VAL A  58      124.37    -34.71
REMARK 500  8 ARG A  78       51.56   -169.16
REMARK 500  8 PHE A  87       81.95     90.16
REMARK 500  8 ASP A  91      133.20     81.46
REMARK 500  9 GLU A   4       25.64   -142.31
REMARK 500  9 ASP A   6       -2.18     98.51
REMARK 500  9 TRP A  27       99.13    -64.90
REMARK 500  9 LEU A  56       11.00     52.36
REMARK 500  9 VAL A  58      120.94    -39.68
REMARK 500  9 ARG A  78       49.21   -169.91
REMARK 500  9 PHE A  87      102.00    153.08
REMARK 500  9 ASP A  91      134.89     81.77
REMARK 500 10 SER A   2      113.68     68.26
REMARK 500 10 ASP A   6      -33.00    156.20
REMARK 500 10 GLU A  53      -77.57    -46.65
REMARK 500 10 LEU A  56       11.60     52.66
REMARK 500 10 VAL A  58      137.50    -38.61
REMARK 500 10 PHE A  87      100.08    159.03
REMARK 500 10 ASP A  91      138.52     77.72
REMARK 500 11 SER A   2       13.28   -153.74
REMARK 500 11 GLU A   4      -65.65    -97.97
REMARK 500 11 ASP A   6      -22.08    156.74
REMARK 500 11 GLU A  53      -70.41    -49.84
REMARK 500 11 LEU A  56       10.67     51.88
REMARK 500 11 VAL A  58      124.28    -32.55
REMARK 500 11 ARG A  78       50.79   -176.14
REMARK 500 11 PHE A  87       62.49     81.67
REMARK 500 11 ASP A  91      121.79    102.31
REMARK 500 12 ASP A   6       11.51   -163.22
REMARK 500 12 TRP A  27       97.39    -69.77
REMARK 500 12 GLU A  53      -76.01    -49.65
REMARK 500 12 LEU A  56       10.90     52.03
REMARK 500 12 VAL A  58      125.77    -22.45
REMARK 500 12 ARG A  78       41.67   -157.90
REMARK 500 12 PHE A  87       82.02    173.27
REMARK 500 12 ASP A  89       11.21   -157.18
REMARK 500 13 GLU A   4       56.28    -92.45
REMARK 500 13 ASP A   6        8.79   -154.54
REMARK 500 13 LEU A  56        9.84     51.19
REMARK 500 13 VAL A  58      111.38    -35.45
REMARK 500 13 PHE A  87      103.43    151.46
REMARK 500 13 ASP A  91      142.93     78.29
REMARK 500 13 PRO A 104       -7.78    -55.52
REMARK 500 14 ASP A   6      -12.09     96.84
REMARK 500 14 GLU A  53      -82.66    -41.17
REMARK 500 14 LEU A  56       11.27     53.89
REMARK 500 14 VAL A  58      128.97    -19.88
REMARK 500 14 ARG A  78       38.15   -154.81
REMARK 500 14 PHE A  87       75.93    173.46
REMARK 500 14 ASP A  89       15.14   -155.43
REMARK 500 15 GLU A   5     -129.70   -109.44
REMARK 500 15 LEU A  56        9.73     51.53
REMARK 500 15 VAL A  58      118.59    -34.31
REMARK 500 15 PHE A  87       87.61    174.29
REMARK 500 15 ASP A  89       29.31    170.61
REMARK 500 16 ASP A   6      -13.71    145.21
REMARK 500 16 GLU A  53      -74.95    -48.72
REMARK 500 16 LEU A  56       11.06     50.69
REMARK 500 16 VAL A  58      129.71    -33.78
REMARK 500 16 PHE A  87       60.68   -166.80
REMARK 500 16 ASP A  89       27.85   -157.68
REMARK 500 17 ASP A   6       17.97   -157.69
REMARK 500 17 LEU A  56       11.39     51.06
REMARK 500 17 VAL A  58      131.44    -26.42
REMARK 500 17 PHE A  87       21.69   -154.73
REMARK 500 17 ASP A  89       21.67   -157.60
REMARK 500 17 ASP A  91      150.93     74.28
REMARK 500 18 SER A   2       80.43     62.70
REMARK 500 18 GLU A   4       82.84     62.46
REMARK 500 18 ASP A   6       -9.93    162.07
REMARK 500 18 LEU A  56        9.95     51.23
REMARK 500 18 ARG A  78       27.70   -149.59
REMARK 500 18 PHE A  87       93.12   -167.62
REMARK 500 18 ASP A  89       35.96    169.69
REMARK 500 18 LEU A 126       43.17    -75.60
REMARK 500 19 GLU A   5     -151.99   -113.47
REMARK 500 19 ASP A   6      -14.21     76.52
REMARK 500 19 LEU A  56       10.42     50.77
REMARK 500 19 VAL A  58      119.38    -31.54
REMARK 500 19 PHE A  87       90.17    174.52
REMARK 500 19 ASP A  91      131.94     86.29
REMARK 500 19 PRO A 104       -9.79    -56.43
REMARK 500 20 GLU A   5     -122.29   -105.57
REMARK 500 20 LEU A  56       10.29     52.00
REMARK 500 20 VAL A  58      124.38    -39.56
REMARK 500 20 ARG A  78       50.20   -175.13
REMARK 500 20 PHE A  87       79.43   -159.68
REMARK 500 20 ASP A  89       29.25    170.93
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 ARG A  51         0.09    SIDE_CHAIN
REMARK 500  3 ARG A  30         0.07    SIDE_CHAIN
REMARK 500  3 ARG A  51         0.08    SIDE_CHAIN
REMARK 500  5 ARG A  30         0.10    SIDE_CHAIN
REMARK 500  5 ARG A  51         0.08    SIDE_CHAIN
REMARK 500  5 ARG A  78         0.08    SIDE_CHAIN
REMARK 500  8 ARG A  19         0.07    SIDE_CHAIN
REMARK 500 11 ARG A  30         0.09    SIDE_CHAIN
REMARK 500 12 ARG A  30         0.09    SIDE_CHAIN
REMARK 500 12 ARG A  78         0.09    SIDE_CHAIN
REMARK 500 15 ARG A  51         0.10    SIDE_CHAIN
REMARK 500 16 ARG A  51         0.08    SIDE_CHAIN
REMARK 500 19 ARG A 119         0.11    SIDE_CHAIN
REMARK 500 20 ARG A  51         0.09    SIDE_CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5159   RELATED DB: BMRB
REMARK 900 CHEMICAL SHIFT ASSIGNMENT
DBREF  1XKE A    3   129  UNP    P49792   RBP2_HUMAN    2028   2154
SEQADV 1XKE GLY A    1  UNP  P49792              CLONING ARTIFACT
SEQADV 1XKE SER A    2  UNP  P49792              CLONING ARTIFACT
SEQADV 1XKE LYS A  130  UNP  P49792              CLONING ARTIFACT
SEQRES   1 A  130  GLY SER GLY GLU GLU ASP GLU LYS VAL LEU TYR SER GLN
SEQRES   2 A  130  ARG VAL LYS LEU PHE ARG PHE ASP ALA GLU VAL SER GLN
SEQRES   3 A  130  TRP LYS GLU ARG GLY LEU GLY ASN LEU LYS ILE LEU LYS
SEQRES   4 A  130  ASN GLU VAL ASN GLY LYS LEU ARG MET LEU MET ARG ARG
SEQRES   5 A  130  GLU GLN VAL LEU LYS VAL CYS ALA ASN HIS TRP ILE THR
SEQRES   6 A  130  THR THR MET ASN LEU LYS PRO LEU SER GLY SER ASP ARG
SEQRES   7 A  130  ALA TRP MET TRP LEU ALA SER ASP PHE SER ASP GLY ASP
SEQRES   8 A  130  ALA LYS LEU GLU GLN LEU ALA ALA LYS PHE LYS THR PRO
SEQRES   9 A  130  GLU LEU ALA GLU GLU PHE LYS GLN LYS PHE GLU GLU CYS
SEQRES  10 A  130  GLN ARG LEU LEU LEU ASP ILE PRO LEU GLN THR PRO LYS
HELIX    1   1 THR A  103  LEU A  121  1                                  19
SHEET    1   A 4 GLU A   7  VAL A   9  0
SHEET    2   A 4 GLN A  26  ASN A  40 -1  O  LYS A  39   N  LYS A   8
SHEET    3   A 4 LEU A  46  ARG A  52 -1  O  LEU A  49   N  LYS A  36
SHEET    4   A 4 LYS A  57  TRP A  63 -1  O  HIS A  62   N  MET A  48
SHEET    1   B 6 GLU A   7  VAL A   9  0
SHEET    2   B 6 GLN A  26  ASN A  40 -1  O  LYS A  39   N  LYS A   8
SHEET    3   B 6 GLN A  13  ASP A  21 -1  N  ARG A  19   O  LYS A  28
SHEET    4   B 6 LYS A  93  LYS A 100 -1  O  ALA A  98   N  PHE A  18
SHEET    5   B 6 TRP A  80  ASP A  86 -1  N  ALA A  84   O  GLU A  95
SHEET    6   B 6 LEU A  70  PRO A  72 -1  N  LYS A  71   O  MET A  81
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