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PDBsum entry 1rrp

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Complex (small gtpase/nuclear protein) PDB id
1rrp
Jmol
Contents
Protein chains
204 a.a. *
134 a.a. *
180 a.a. *
Ligands
GNP ×2
Metals
_MG ×2
Waters ×36
* Residue conservation analysis
HEADER    COMPLEX (SMALL GTPASE/NUCLEAR PROTEIN)  15-JAN-99   1RRP
TITLE     STRUCTURE OF THE RAN-GPPNHP-RANBD1 COMPLEX
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: RAN;
COMPND   3 CHAIN: A, C;
COMPND   4 ENGINEERED: YES;
COMPND   5 MOL_ID: 2;
COMPND   6 MOLECULE: NUCLEAR PORE COMPLEX PROTEIN NUP358;
COMPND   7 CHAIN: B, D;
COMPND   8 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;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: GST-FUSION;
SOURCE   9 MOL_ID: 2;
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE  11 ORGANISM_COMMON: HUMAN;
SOURCE  12 ORGANISM_TAXID: 9606;
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE  15 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE  16 EXPRESSION_SYSTEM_PLASMID: GST-FUSION
KEYWDS    COMPLEX (SMALL GTPASE/NUCLEAR PROTEIN), SMALL GTPASE,
KEYWDS   2 NUCLEAR TRANSPORT
EXPDTA    X-RAY DIFFRACTION
AUTHOR    I.R.VETTER,C.NOWAK,T.NISHIMOTO,J.KUHLMANN,A.WITTINGHOFER
REVDAT   2   24-FEB-09 1RRP    1       VERSN
REVDAT   1   18-MAY-99 1RRP    0
JRNL        AUTH   I.R.VETTER,C.NOWAK,T.NISHIMOTO,J.KUHLMANN,
JRNL        AUTH 2 A.WITTINGHOFER
JRNL        TITL   STRUCTURE OF A RAN-BINDING DOMAIN COMPLEXED WITH
JRNL        TITL 2 RAN BOUND TO A GTP ANALOGUE: IMPLICATIONS FOR
JRNL        TITL 3 NUCLEAR TRANSPORT.
JRNL        REF    NATURE                        V. 398    39 1999
JRNL        REFN                   ISSN 0028-0836
JRNL        PMID   10078529
JRNL        DOI    10.1038/17969
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   F.R.BISCHOFF,D.GORLICH
REMARK   1  TITL   RANBP1 IS CRUCIAL FOR THE RELEASE OF RANGTP FROM
REMARK   1  TITL 2 IMPORTIN BETA-RELATED NUCLEAR TRANSPORT FACTORS
REMARK   1  REF    FEBS LETT.                    V. 419   249 1997
REMARK   1  REFN                   ISSN 0014-5793
REMARK   1 REFERENCE 2
REMARK   1  AUTH   J.KUHLMANN,I.MACARA,A.WITTINGHOFER
REMARK   1  TITL   DYNAMIC AND EQUILIBRIUM STUDIES ON THE INTERACTION
REMARK   1  TITL 2 OF RAN WITH ITS EFFECTOR, RANBP1
REMARK   1  REF    BIOCHEMISTRY                  V.  36 12027 1997
REMARK   1  REFN                   ISSN 0006-2960
REMARK   1 REFERENCE 3
REMARK   1  AUTH   E.HARTMANN,D.GORLICH
REMARK   1  TITL   A RAN-BINDING MOTIF FOUND IN NUCLEAR PORE PROTEINS
REMARK   1  REF    TRENDS CELL BIOL.             V.   5   192 1995
REMARK   1  REFN                   ISSN 0962-8924
REMARK   1 REFERENCE 4
REMARK   1  AUTH   N.YOKOYAMA,N.HAYASHI,T.SEKI,N.PANTE,T.OHBA,
REMARK   1  AUTH 2 K.NISHII,K.KUMA,T.HAYASHIDA,T.MIYATA,U.AEBI,
REMARK   1  AUTH 3 M.FUKUI,T.NISHIMOTO
REMARK   1  TITL   A GIANT NUCLEOPORE PROTEIN THAT BINDS RAN/TC4
REMARK   1  REF    NATURE                        V. 376   184 1995
REMARK   1  REFN                   ISSN 0028-0836
REMARK   1 REFERENCE 5
REMARK   1  AUTH   S.A.RICHARDS,K.M.LOUNSBURY,I.G.MACARA
REMARK   1  TITL   THE C TERMINUS OF THE NUCLEAR RAN/TC4 GTPASE
REMARK   1  TITL 2 STABILIZES THE GDP-BOUND STATE AND MEDIATES
REMARK   1  TITL 3 INTERACTIONS WITH RCC1, RAN-GAP, AND HTF9A/RANBP1
REMARK   1  REF    J.BIOL.CHEM.                  V. 270 14405 1995
REMARK   1  REFN                   ISSN 0021-9258
REMARK   1 REFERENCE 6
REMARK   1  AUTH   F.R.BISCHOFF,H.KREBBER,E.SMIRNOVA,W.DONG,
REMARK   1  AUTH 2 H.PONSTINGL
REMARK   1  TITL   CO-ACTIVATION OF RANGTPASE AND INHIBITION OF GTP
REMARK   1  TITL 2 DISSOCIATION BY RAN-GTP BINDING PROTEIN RANBP1
REMARK   1  REF    EMBO J.                       V.  14   705 1995
REMARK   1  REFN                   ISSN 0261-4189
REMARK   2
REMARK   2 RESOLUTION.    2.96 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS 0.4
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) : 2.96
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 12.50
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 86.0
REMARK   3   NUMBER OF REFLECTIONS             : 17709
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) : 0.252
REMARK   3   FREE R VALUE                     : 0.304
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1676
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.007
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : NULL
REMARK   3   BIN FREE R VALUE                    : NULL
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 5302
REMARK   3   NUCLEIC ACID ATOMS       : 64
REMARK   3   HETEROGEN ATOMS          : 2
REMARK   3   SOLVENT ATOMS            : 36
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 75.40
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 56.10
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : NULL
REMARK   3    B22 (A**2) : NULL
REMARK   3    B33 (A**2) : NULL
REMARK   3    B12 (A**2) : NULL
REMARK   3    B13 (A**2) : NULL
REMARK   3    B23 (A**2) : NULL
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.51
REMARK   3   ESD FROM SIGMAA              (A) : 0.53
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) : 0.64
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.81
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.008
REMARK   3   BOND ANGLES            (DEGREES) : 1.40
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.30
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.98
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) : NULL  ; NULL
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : FLAT MODEL
REMARK   3   KSOL        : 0.24
REMARK   3   BSOL        : 38.40
REMARK   3
REMARK   3  NCS MODEL : CONSTR
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  : GNP.PAR
REMARK   3  PARAMETER FILE  4  : WATER_REP.PARAM
REMARK   3  PARAMETER FILE  5  : NULL
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP
REMARK   3  TOPOLOGY FILE  2   : NULL
REMARK   3  TOPOLOGY FILE  3   : NULL
REMARK   3  TOPOLOGY FILE  4   : NULL
REMARK   3  TOPOLOGY FILE  5   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1RRP COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : APR-98
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 6.25
REMARK 200  NUMBER OF CRYSTALS USED        : 2
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG
REMARK 200  BEAMLINE                       : BW7B
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.84
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : SIEMENS
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200  DATA SCALING SOFTWARE          : XSCALE
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20286
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 86.0
REMARK 200  DATA REDUNDANCY                : 4.500
REMARK 200  R MERGE                    (I) : 0.09100
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 13.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.00
REMARK 200  COMPLETENESS FOR SHELL     (%) : 66.0
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.19100
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 3.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS 0.4
REMARK 200 STARTING MODEL: RAN-GDP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 60.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.25
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       60.66950
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       69.73150
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       60.66950
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       69.73150
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5730 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16180 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.0 KCAL/MOL
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 350
REMARK 350 BIOMOLECULE: 2
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: 4430 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15200 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 25430 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 57640 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -150.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 350   BIOMT1   2 -1.000000  0.000000  0.000000       55.65358
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       63.92090
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11370 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30170 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -62.0 KCAL/MOL
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 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000       55.65358
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       63.92090
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     VAL C   188
REMARK 465     MET C   189
REMARK 465     ASP C   190
REMARK 465     PRO C   191
REMARK 465     ALA C   192
REMARK 465     LEU C   193
REMARK 465     ALA C   194
REMARK 465     ALA C   195
REMARK 465     GLN C   196
REMARK 465     TYR C   197
REMARK 465     GLU C   198
REMARK 465     HIS C   199
REMARK 465     ASP C   200
REMARK 465     LEU C   201
REMARK 465     GLU C   202
REMARK 465     VAL C   203
REMARK 465     ALA C   204
REMARK 465     GLN C   205
REMARK 465     THR C   206
REMARK 465     THR C   207
REMARK 465     ALA C   208
REMARK 465     LEU C   209
REMARK 465     PRO C   210
REMARK 465     ASP C   211
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    GLU B    35     N    GLU B    37              2.14
REMARK 500   O    GLU D    35     N    GLU D    37              2.15
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    ALA A  41      135.33    -39.35
REMARK 500    VAL A  45      141.40     49.41
REMARK 500    ASP A  65       93.54    -68.79
REMARK 500    LYS A  71       -7.99    -51.68
REMARK 500    ARG A  76       59.62    -69.79
REMARK 500    ASP A  77      -28.94   -140.84
REMARK 500    VAL A  92      -29.03     67.77
REMARK 500    ARG A  95      -36.45    -30.73
REMARK 500    VAL A 109        7.52    -63.14
REMARK 500    GLU A 113      178.39    -50.65
REMARK 500    ASN A 114     -125.97     33.64
REMARK 500    ILE A 115      130.84     68.77
REMARK 500    VAL A 124        7.83    -57.04
REMARK 500    ASP A 128       54.69    -64.50
REMARK 500    LYS A 132      156.26    -48.80
REMARK 500    VAL A 137      -35.17   -147.48
REMARK 500    SER A 150       75.69   -169.39
REMARK 500    ALA A 151       -8.98    -46.77
REMARK 500    ASN A 154       -6.61     61.16
REMARK 500    TYR A 155      115.46    -39.38
REMARK 500    ASN A 156        3.73     55.94
REMARK 500    PHE A 157       -2.72    -56.64
REMARK 500    PRO A 172      -17.04    -48.95
REMARK 500    ALA A 178     -147.93     39.98
REMARK 500    LEU A 182      154.17    -37.35
REMARK 500    VAL A 188     -169.49   -103.96
REMARK 500    MET A 189      120.44     72.59
REMARK 500    PRO A 191     -128.63      6.59
REMARK 500    LEU A 193      -83.77    -28.62
REMARK 500    ALA A 204      -75.12    -72.31
REMARK 500    GLN A 205       -7.61    -47.35
REMARK 500    ALA A 208      145.82    -36.21
REMARK 500    LYS B  27     -172.66    -57.03
REMARK 500    VAL B  30       93.92    -28.52
REMARK 500    LYS B  31     -105.45    -60.97
REMARK 500    THR B  32      -11.64    127.68
REMARK 500    GLU B  34     -104.52    -71.02
REMARK 500    GLU B  35     -150.47     12.46
REMARK 500    ASP B  36       16.33     32.61
REMARK 500    GLU B  39       87.93    -63.47
REMARK 500    PHE B  41      147.81    179.01
REMARK 500    CYS B  42      101.93   -166.29
REMARK 500    VAL B  52      -46.30     66.75
REMARK 500    SER B  54      -96.84   -128.58
REMARK 500    LYS B  55       -1.47    175.72
REMARK 500    THR B  72      -86.30    -86.81
REMARK 500    GLN B  84      -64.96     68.22
REMARK 500    LEU B  86       91.27     59.15
REMARK 500    CYS B  89       19.80   -148.94
REMARK 500    ALA B  90      137.08   -175.40
REMARK 500    ASN B  91      -11.30   -152.86
REMARK 500    PRO B 102     -115.21    -54.35
REMARK 500    ASN B 103       96.93    153.93
REMARK 500    SER B 106       88.42    -59.14
REMARK 500    ASP B 107       23.49    -70.61
REMARK 500    CYS B 142      -77.36    -47.92
REMARK 500    ALA C  41      134.76    -38.91
REMARK 500    VAL C  45      142.60     48.83
REMARK 500    LYS C  71       -8.29    -51.66
REMARK 500    ASP C  77      -29.63   -140.84
REMARK 500    VAL C  92      -29.73     67.70
REMARK 500    ARG C  95      -36.76    -29.79
REMARK 500    VAL C 109        7.20    -62.43
REMARK 500    GLU C 113      178.07    -51.13
REMARK 500    ASN C 114     -125.85     34.13
REMARK 500    ILE C 115      130.56     68.32
REMARK 500    VAL C 124        8.48    -55.25
REMARK 500    ASP C 128       55.40    -64.76
REMARK 500    LYS C 132      155.94    -48.00
REMARK 500    VAL C 137      -35.10   -147.22
REMARK 500    SER C 150       76.35   -169.06
REMARK 500    ALA C 151       -9.06    -46.90
REMARK 500    ASN C 154       -5.67     60.97
REMARK 500    ASN C 156        4.45     55.98
REMARK 500    PHE C 157       -2.38    -57.24
REMARK 500    PRO C 172      -17.32    -48.75
REMARK 500    ALA C 178     -146.42     41.38
REMARK 500    LEU C 182      154.13    -37.87
REMARK 500    VAL D  22      151.44    170.29
REMARK 500    VAL D  30       88.46    -54.18
REMARK 500    LYS D  31     -104.27    -61.11
REMARK 500    THR D  32      -12.94    126.25
REMARK 500    GLU D  34     -104.76    -72.04
REMARK 500    GLU D  35     -150.08     12.09
REMARK 500    ASP D  36       16.56     32.38
REMARK 500    GLU D  39       87.52    -64.93
REMARK 500    PHE D  41      148.00    179.38
REMARK 500    CYS D  42      102.23   -167.03
REMARK 500    VAL D  52      -45.42     67.58
REMARK 500    SER D  54      -97.60   -128.86
REMARK 500    LYS D  55       -1.64    176.58
REMARK 500    THR D  72      -86.71    -86.84
REMARK 500    GLN D  84      -65.01     68.36
REMARK 500    LEU D  86       91.93     58.22
REMARK 500    CYS D  89       20.22   -150.87
REMARK 500    ALA D  90      136.65   -175.98
REMARK 500    ASN D  91      -11.73   -152.83
REMARK 500    PRO D 102     -115.30    -54.88
REMARK 500    ASN D 103       96.59    154.01
REMARK 500    SER D 106       88.35    -59.54
REMARK 500    ASP D 107       23.31    -70.64
REMARK 500    CYS D 142      -77.47    -47.43
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 A 482        DISTANCE =  5.73 ANGSTROMS
REMARK 525    HOH D 478        DISTANCE =  7.46 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG A 251  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GNP A 250   O2B
REMARK 620 2 THR A  24   OG1  65.3
REMARK 620 3 THR A  42   OG1  97.6  58.0
REMARK 620 4 GNP A 250   O2G  57.8  77.4  55.7
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG C 251  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR C  24   OG1
REMARK 620 2 GNP C 250   O2G  78.1
REMARK 620 3 GNP C 250   O2B  65.6  58.0
REMARK 620 4 THR C  42   OG1  57.7  56.9  98.3
REMARK 620 N                    1     2     3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 251
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 251
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GNP A 250
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GNP C 250
DBREF  1RRP A    8   211  UNP    P62826   RAN_HUMAN        8    211
DBREF  1RRP B   17   150  UNP    P49792   RBP2_HUMAN    1171   1304
DBREF  1RRP C    8   211  UNP    P62826   RAN_HUMAN        8    211
DBREF  1RRP D   17   150  UNP    P49792   RBP2_HUMAN    1171   1304
SEQADV 1RRP ARG A  129  UNP  P62826    SER   129 SEE REMARK 999
SEQADV 1RRP ARG C  129  UNP  P62826    SER   129 SEE REMARK 999
SEQRES   1 A  204  GLN VAL GLN PHE LYS LEU VAL LEU VAL GLY ASP GLY GLY
SEQRES   2 A  204  THR GLY LYS THR THR PHE VAL LYS ARG HIS LEU THR GLY
SEQRES   3 A  204  GLU PHE GLU LYS LYS TYR VAL ALA THR LEU GLY VAL GLU
SEQRES   4 A  204  VAL HIS PRO LEU VAL PHE HIS THR ASN ARG GLY PRO ILE
SEQRES   5 A  204  LYS PHE ASN VAL TRP ASP THR ALA GLY GLN GLU LYS PHE
SEQRES   6 A  204  GLY GLY LEU ARG ASP GLY TYR TYR ILE GLN ALA GLN CYS
SEQRES   7 A  204  ALA ILE ILE MET PHE ASP VAL THR SER ARG VAL THR TYR
SEQRES   8 A  204  LYS ASN VAL PRO ASN TRP HIS ARG ASP LEU VAL ARG VAL
SEQRES   9 A  204  CYS GLU ASN ILE PRO ILE VAL LEU CYS GLY ASN LYS VAL
SEQRES  10 A  204  ASP ILE LYS ASP ARG LYS VAL LYS ALA LYS SER ILE VAL
SEQRES  11 A  204  PHE HIS ARG LYS LYS ASN LEU GLN TYR TYR ASP ILE SER
SEQRES  12 A  204  ALA LYS SER ASN TYR ASN PHE GLU LYS PRO PHE LEU TRP
SEQRES  13 A  204  LEU ALA ARG LYS LEU ILE GLY ASP PRO ASN LEU GLU PHE
SEQRES  14 A  204  VAL ALA MET PRO ALA LEU ALA PRO PRO GLU VAL VAL MET
SEQRES  15 A  204  ASP PRO ALA LEU ALA ALA GLN TYR GLU HIS ASP LEU GLU
SEQRES  16 A  204  VAL ALA GLN THR THR ALA LEU PRO ASP
SEQRES   1 B  134  HIS PHE GLU PRO VAL VAL PRO LEU PRO ASP LYS ILE GLU
SEQRES   2 B  134  VAL LYS THR GLY GLU GLU ASP GLU GLU GLU PHE PHE CYS
SEQRES   3 B  134  ASN ARG ALA LYS LEU PHE ARG PHE ASP VAL GLU SER LYS
SEQRES   4 B  134  GLU TRP LYS GLU ARG GLY ILE GLY ASN VAL LYS ILE LEU
SEQRES   5 B  134  ARG HIS LYS THR SER GLY LYS ILE ARG LEU LEU MET ARG
SEQRES   6 B  134  ARG GLU GLN VAL LEU LYS ILE CYS ALA ASN HIS TYR ILE
SEQRES   7 B  134  SER PRO ASP MET LYS LEU THR PRO ASN ALA GLY SER ASP
SEQRES   8 B  134  ARG SER PHE VAL TRP HIS ALA LEU ASP TYR ALA ASP GLU
SEQRES   9 B  134  LEU PRO LYS PRO GLU GLN LEU ALA ILE ARG PHE LYS THR
SEQRES  10 B  134  PRO GLU GLU ALA ALA LEU PHE LYS CYS LYS PHE GLU GLU
SEQRES  11 B  134  ALA GLN SER ILE
SEQRES   1 C  204  GLN VAL GLN PHE LYS LEU VAL LEU VAL GLY ASP GLY GLY
SEQRES   2 C  204  THR GLY LYS THR THR PHE VAL LYS ARG HIS LEU THR GLY
SEQRES   3 C  204  GLU PHE GLU LYS LYS TYR VAL ALA THR LEU GLY VAL GLU
SEQRES   4 C  204  VAL HIS PRO LEU VAL PHE HIS THR ASN ARG GLY PRO ILE
SEQRES   5 C  204  LYS PHE ASN VAL TRP ASP THR ALA GLY GLN GLU LYS PHE
SEQRES   6 C  204  GLY GLY LEU ARG ASP GLY TYR TYR ILE GLN ALA GLN CYS
SEQRES   7 C  204  ALA ILE ILE MET PHE ASP VAL THR SER ARG VAL THR TYR
SEQRES   8 C  204  LYS ASN VAL PRO ASN TRP HIS ARG ASP LEU VAL ARG VAL
SEQRES   9 C  204  CYS GLU ASN ILE PRO ILE VAL LEU CYS GLY ASN LYS VAL
SEQRES  10 C  204  ASP ILE LYS ASP ARG LYS VAL LYS ALA LYS SER ILE VAL
SEQRES  11 C  204  PHE HIS ARG LYS LYS ASN LEU GLN TYR TYR ASP ILE SER
SEQRES  12 C  204  ALA LYS SER ASN TYR ASN PHE GLU LYS PRO PHE LEU TRP
SEQRES  13 C  204  LEU ALA ARG LYS LEU ILE GLY ASP PRO ASN LEU GLU PHE
SEQRES  14 C  204  VAL ALA MET PRO ALA LEU ALA PRO PRO GLU VAL VAL MET
SEQRES  15 C  204  ASP PRO ALA LEU ALA ALA GLN TYR GLU HIS ASP LEU GLU
SEQRES  16 C  204  VAL ALA GLN THR THR ALA LEU PRO ASP
SEQRES   1 D  134  HIS PHE GLU PRO VAL VAL PRO LEU PRO ASP LYS ILE GLU
SEQRES   2 D  134  VAL LYS THR GLY GLU GLU ASP GLU GLU GLU PHE PHE CYS
SEQRES   3 D  134  ASN ARG ALA LYS LEU PHE ARG PHE ASP VAL GLU SER LYS
SEQRES   4 D  134  GLU TRP LYS GLU ARG GLY ILE GLY ASN VAL LYS ILE LEU
SEQRES   5 D  134  ARG HIS LYS THR SER GLY LYS ILE ARG LEU LEU MET ARG
SEQRES   6 D  134  ARG GLU GLN VAL LEU LYS ILE CYS ALA ASN HIS TYR ILE
SEQRES   7 D  134  SER PRO ASP MET LYS LEU THR PRO ASN ALA GLY SER ASP
SEQRES   8 D  134  ARG SER PHE VAL TRP HIS ALA LEU ASP TYR ALA ASP GLU
SEQRES   9 D  134  LEU PRO LYS PRO GLU GLN LEU ALA ILE ARG PHE LYS THR
SEQRES  10 D  134  PRO GLU GLU ALA ALA LEU PHE LYS CYS LYS PHE GLU GLU
SEQRES  11 D  134  ALA GLN SER ILE
HET     MG  A 251       1
HET     MG  C 251       1
HET    GNP  A 250      32
HET    GNP  C 250      32
HETNAM      MG MAGNESIUM ION
HETNAM     GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER
FORMUL   5   MG    2(MG 2+)
FORMUL   7  GNP    2(C10 H17 N6 O13 P3)
FORMUL   9  HOH   *36(H2 O)
HELIX    1   1 LYS A   23  THR A   32  1                                  10
HELIX    2   2 GLU A   70  PHE A   72  5                                   3
HELIX    3   3 ARG A   95  VAL A  111  1                                  17
HELIX    4   4 ALA A  133  SER A  135  5                                   3
HELIX    5   5 PHE A  138  LYS A  141  1                                   4
HELIX    6   6 LYS A  159  ILE A  169  1                                  11
HELIX    7   7 PRO A  191  GLN A  205  1                                  15
HELIX    8   8 PRO B  134  GLU B  146  1                                  13
HELIX    9   9 LYS C   23  THR C   32  1                                  10
HELIX   10  10 GLU C   70  PHE C   72  5                                   3
HELIX   11  11 ARG C   95  VAL C  111  1                                  17
HELIX   12  12 ALA C  133  SER C  135  5                                   3
HELIX   13  13 PHE C  138  LYS C  141  1                                   4
HELIX   14  14 LYS C  159  ILE C  169  1                                  11
HELIX   15  15 PRO D  134  GLU D  146  1                                  13
SHEET    1   A 6 GLN A 145  ASP A 148  0
SHEET    2   A 6 PRO A 116  GLY A 121  1  N  LEU A 119   O  GLN A 145
SHEET    3   A 6 CYS A  85  PHE A  90  1  N  ALA A  86   O  PRO A 116
SHEET    4   A 6 GLN A  10  VAL A  16  1  N  VAL A  14   O  CYS A  85
SHEET    5   A 6 GLY A  57  ASP A  65  1  N  LYS A  60   O  PHE A  11
SHEET    6   A 6 GLU A  46  THR A  54 -1  N  THR A  54   O  GLY A  57
SHEET    1   B 3 GLU B  37  GLU B  39  0
SHEET    2   B 3 GLY B  63  HIS B  70 -1  N  ARG B  69   O  GLU B  38
SHEET    3   B 3 ARG B  77  ARG B  82 -1  N  ARG B  81   O  ASN B  64
SHEET    1   C 4 SER B 109  ASP B 116  0
SHEET    2   C 4 LYS B 123  ARG B 130 -1  N  ILE B 129   O  PHE B 110
SHEET    3   C 4 CYS B  42  PHE B  50 -1  N  PHE B  48   O  ALA B 128
SHEET    4   C 4 TRP B  57  LYS B  66 -1  N  VAL B  65   O  ASN B  43
SHEET    1   D 6 GLN C 145  ASP C 148  0
SHEET    2   D 6 PRO C 116  GLY C 121  1  N  LEU C 119   O  GLN C 145
SHEET    3   D 6 CYS C  85  PHE C  90  1  N  ALA C  86   O  PRO C 116
SHEET    4   D 6 GLN C  10  VAL C  16  1  N  VAL C  14   O  CYS C  85
SHEET    5   D 6 GLY C  57  ASP C  65  1  N  LYS C  60   O  PHE C  11
SHEET    6   D 6 GLU C  46  THR C  54 -1  N  THR C  54   O  GLY C  57
SHEET    1   E 3 GLU D  37  GLU D  39  0
SHEET    2   E 3 VAL D  65  HIS D  70 -1  N  ARG D  69   O  GLU D  38
SHEET    3   E 3 ARG D  77  MET D  80 -1  N  LEU D  79   O  LYS D  66
SHEET    1   F 4 SER D 109  ASP D 116  0
SHEET    2   F 4 LYS D 123  ARG D 130 -1  N  ILE D 129   O  PHE D 110
SHEET    3   F 4 CYS D  42  PHE D  50 -1  N  PHE D  48   O  ALA D 128
SHEET    4   F 4 TRP D  57  LYS D  66 -1  N  VAL D  65   O  ASN D  43
LINK        MG    MG A 251                 O2B GNP A 250     1555   1555  2.63
LINK        MG    MG A 251                 OG1 THR A  24     1555   1555  2.70
LINK        MG    MG A 251                 OG1 THR A  42     1555   1555  2.73
LINK        MG    MG A 251                 O2G GNP A 250     1555   1555  2.85
LINK        MG    MG C 251                 OG1 THR C  24     1555   1555  2.68
LINK        MG    MG C 251                 O2G GNP C 250     1555   1555  2.83
LINK        MG    MG C 251                 O2B GNP C 250     1555   1555  2.61
LINK        MG    MG C 251                 OG1 THR C  42     1555   1555  2.72
SITE     1 AC1  4 THR A  24  VAL A  40  THR A  42  GNP A 250
SITE     1 AC2  4 THR C  24  VAL C  40  THR C  42  GNP C 250
SITE     1 AC3 23 GLY A  19  GLY A  20  THR A  21  GLY A  22
SITE     2 AC3 23 LYS A  23  THR A  24  THR A  25  PHE A  35
SITE     3 AC3 23 GLU A  36  LYS A  37  LYS A  38  TYR A  39
SITE     4 AC3 23 ALA A  41  THR A  42  ALA A  67  GLY A  68
SITE     5 AC3 23 ASN A 122  LYS A 123  ASP A 125  SER A 150
SITE     6 AC3 23 ALA A 151  LYS A 152   MG A 251
SITE     1 AC4 23 GLY C  19  GLY C  20  THR C  21  GLY C  22
SITE     2 AC4 23 LYS C  23  THR C  24  THR C  25  PHE C  35
SITE     3 AC4 23 GLU C  36  LYS C  37  LYS C  38  TYR C  39
SITE     4 AC4 23 ALA C  41  THR C  42  ALA C  67  GLY C  68
SITE     5 AC4 23 ASN C 122  LYS C 123  ASP C 125  SER C 150
SITE     6 AC4 23 ALA C 151  LYS C 152   MG C 251
CRYST1  121.339  139.463   91.654  90.00 135.78  90.00 C 1 2 1       8
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      0.008241  0.000000  0.008469        0.00000
SCALE2      0.000000  0.007170  0.000000        0.00000
SCALE3      0.000000  0.000000  0.015644        0.00000
MTRIX1   1  0.993600 -0.046000  0.103200       -4.69520    1
MTRIX2   1 -0.043000 -0.998600 -0.030700      -12.10150    1
MTRIX3   1  0.104400  0.026100 -0.994200       63.52460    1
      
PROCHECK
Go to PROCHECK summary
 References