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PDBsum entry 1rk4

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Top Page protein Protein-protein interface(s) links
Ion transport/membrane protein PDB id
1rk4
Jmol
Contents
Protein chains
213 a.a. *
Waters ×342
* Residue conservation analysis
HEADER    ION TRANSPORT/MEMBRANE PROTEIN          20-NOV-03   1RK4
TITLE     CRYSTAL STRUCTURE OF A SOLUBLE DIMERIC FORM OF OXIDISED
TITLE    2 CLIC1
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CHLORIDE INTRACELLULAR CHANNEL PROTEIN 1;
COMPND   3 CHAIN: A, B;
COMPND   4 SYNONYM: NUCLEAR CHLORIDE ION CHANNEL 27; NCC27; P64 CLCP;
COMPND   5 CHLORIDE CHANNEL ABP; P64CLCP; CHLORIDE CHANNEL ABP;
COMPND   6 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: CLIC1, NCC27;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PGEX-4T-1
KEYWDS    GLUTATHIONE-S-TRANFERASE SUPERFAMILY; CHLORIDE ION CHANNEL;
KEYWDS   2 REDOX-CONTROLLED STRUCTURAL TRANSITION, ION
KEYWDS   3 TRANSPORT/MEMBRANE PROTEIN COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.R.LITTLER,S.J.HARROP,W.D.FAIRLIE,L.J.BROWN,G.J.PANKHURST,
AUTHOR   2 S.PANKHURST,M.Z.DEMAERE,T.J.CAMPBELL,A.R.BAUSKIN,R.TONINI,
AUTHOR   3 M.MAZZANTI,S.N.BREIT,P.M.CURMI
REVDAT   3   24-FEB-09 1RK4    1       VERSN
REVDAT   2   09-MAR-04 1RK4    1       JRNL
REVDAT   1   02-DEC-03 1RK4    0
JRNL        AUTH   D.R.LITTLER,S.J.HARROP,W.D.FAIRLIE,L.J.BROWN,
JRNL        AUTH 2 G.J.PANKHURST,S.PANKHURST,M.Z.DEMAERE,T.J.CAMPBELL,
JRNL        AUTH 3 A.R.BAUSKIN,R.TONINI,M.MAZZANTI,S.N.BREIT,P.M.CURMI
JRNL        TITL   THE INTRACELLULAR CHLORIDE ION CHANNEL PROTEIN
JRNL        TITL 2 CLIC1 UNDERGOES A REDOX-CONTROLLED STRUCTURAL
JRNL        TITL 3 TRANSITION
JRNL        REF    J.BIOL.CHEM.                  V. 279  9298 2004
JRNL        REFN                   ISSN 0021-9258
JRNL        PMID   14613939
JRNL        DOI    10.1074/JBC.M308444200
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    1.79 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.1.24
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.79
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 57.74
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.6
REMARK   3   NUMBER OF REFLECTIONS             : 38677
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 + TEST SET) : 0.178
REMARK   3   R VALUE            (WORKING SET) : 0.176
REMARK   3   FREE R VALUE                     : 0.213
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 2089
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.79
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.84
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2490
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2230
REMARK   3   BIN FREE R VALUE SET COUNT          : 135
REMARK   3   BIN FREE R VALUE                    : 0.2670
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 3319
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 0
REMARK   3   SOLVENT ATOMS            : 342
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 19.20
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.00
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.70000
REMARK   3    B22 (A**2) : -0.22000
REMARK   3    B33 (A**2) : 0.92000
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 OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.127
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.122
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.081
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.593
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.955
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.935
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3392 ; 0.019 ; 0.021
REMARK   3   BOND LENGTHS OTHERS               (A):  3064 ; 0.002 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4607 ; 1.689 ; 1.978
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  7168 ; 0.885 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   416 ; 5.527 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   522 ; 0.096 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3742 ; 0.010 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):   658 ; 0.010 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   748 ; 0.225 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  3474 ; 0.240 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1988 ; 0.086 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   242 ; 0.174 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    19 ; 0.253 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):    77 ; 0.267 ; 0.200
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    35 ; 0.170 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2096 ; 1.140 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3395 ; 2.046 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1296 ; 3.060 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1212 ; 5.052 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.40
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 1RK4 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-NOV-03.
REMARK 100 THE RCSB ID CODE IS RCSB020825.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-JUL-01
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 4.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : ENRAF-NONIUS
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : RIGAKU MIRRORS
REMARK 200  OPTICS                         : MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : MAC SCIENCE DIP-2030
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38677
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.790
REMARK 200  RESOLUTION RANGE LOW       (A) : 57.740
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.6
REMARK 200  DATA REDUNDANCY                : 6.300
REMARK 200  R MERGE                    (I) : 0.05800
REMARK 200  R SYM                      (I) : 0.05800
REMARK 200   FOR THE DATA SET  : 18.5300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: 1K0M
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 49.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG MME 5000, PH 4.5, VAPOR
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 277K
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       29.93050
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       53.75300
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       34.59450
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       53.75300
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       29.93050
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       34.59450
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 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: 2180 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21190 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 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 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 A    -1
REMARK 465     SER A     0
REMARK 465     MET A     1
REMARK 465     ALA A     2
REMARK 465     GLU A     3
REMARK 465     GLU A     4
REMARK 465     GLN A     5
REMARK 465     PRO A     6
REMARK 465     GLN A     7
REMARK 465     VAL A     8
REMARK 465     GLU A     9
REMARK 465     LEU A    10
REMARK 465     PHE A    11
REMARK 465     VAL A    12
REMARK 465     LYS A    13
REMARK 465     ALA A    14
REMARK 465     GLY A    15
REMARK 465     SER A    16
REMARK 465     ASP A    17
REMARK 465     GLY A    18
REMARK 465     ALA A    19
REMARK 465     LYS A    20
REMARK 465     ILE A    21
REMARK 465     GLN A   235
REMARK 465     VAL A   236
REMARK 465     ALA A   237
REMARK 465     LYS A   238
REMARK 465     ALA A   239
REMARK 465     LEU A   240
REMARK 465     LYS A   241
REMARK 465     GLY B    -1
REMARK 465     SER B     0
REMARK 465     MET B     1
REMARK 465     ALA B     2
REMARK 465     GLU B     3
REMARK 465     GLU B     4
REMARK 465     GLN B     5
REMARK 465     PRO B     6
REMARK 465     GLN B     7
REMARK 465     VAL B     8
REMARK 465     GLU B     9
REMARK 465     LEU B    10
REMARK 465     PHE B    11
REMARK 465     VAL B    12
REMARK 465     LYS B    13
REMARK 465     ALA B    14
REMARK 465     GLY B    15
REMARK 465     SER B    16
REMARK 465     ASP B    17
REMARK 465     GLY B    18
REMARK 465     ALA B    19
REMARK 465     LYS B    20
REMARK 465     ILE B    21
REMARK 465     GLU B   154
REMARK 465     THR B   155
REMARK 465     SER B   156
REMARK 465     ALA B   157
REMARK 465     GLU B   158
REMARK 465     ASP B   159
REMARK 465     GLU B   160
REMARK 465     GLN B   235
REMARK 465     VAL B   236
REMARK 465     ALA B   237
REMARK 465     LYS B   238
REMARK 465     ALA B   239
REMARK 465     LEU B   240
REMARK 465     LYS B   241
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    ARG B  51   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 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    VAL A  39       79.04   -109.38
REMARK 500    GLU A 158      -36.49   -130.22
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1K0M   RELATED DB: PDB
REMARK 900 THE NATIVE MONOMERIC FORM OF CLIC1
DBREF  1RK4 A    1   241  UNP    O00299   CLIC1_HUMAN      1    241
DBREF  1RK4 B    1   241  UNP    O00299   CLIC1_HUMAN      1    241
SEQADV 1RK4 GLY A   -1  UNP  O00299              CLONING ARTIFACT
SEQADV 1RK4 SER A    0  UNP  O00299              CLONING ARTIFACT
SEQADV 1RK4 GLY B   -1  UNP  O00299              CLONING ARTIFACT
SEQADV 1RK4 SER B    0  UNP  O00299              CLONING ARTIFACT
SEQRES   1 A  243  GLY SER MET ALA GLU GLU GLN PRO GLN VAL GLU LEU PHE
SEQRES   2 A  243  VAL LYS ALA GLY SER ASP GLY ALA LYS ILE GLY ASN CYS
SEQRES   3 A  243  PRO PHE SER GLN ARG LEU PHE MET VAL LEU TRP LEU LYS
SEQRES   4 A  243  GLY VAL THR PHE ASN VAL THR THR VAL ASP THR LYS ARG
SEQRES   5 A  243  ARG THR GLU THR VAL GLN LYS LEU CYS PRO GLY GLY GLN
SEQRES   6 A  243  LEU PRO PHE LEU LEU TYR GLY THR GLU VAL HIS THR ASP
SEQRES   7 A  243  THR ASN LYS ILE GLU GLU PHE LEU GLU ALA VAL LEU CYS
SEQRES   8 A  243  PRO PRO ARG TYR PRO LYS LEU ALA ALA LEU ASN PRO GLU
SEQRES   9 A  243  SER ASN THR ALA GLY LEU ASP ILE PHE ALA LYS PHE SER
SEQRES  10 A  243  ALA TYR ILE LYS ASN SER ASN PRO ALA LEU ASN ASP ASN
SEQRES  11 A  243  LEU GLU LYS GLY LEU LEU LYS ALA LEU LYS VAL LEU ASP
SEQRES  12 A  243  ASN TYR LEU THR SER PRO LEU PRO GLU GLU VAL ASP GLU
SEQRES  13 A  243  THR SER ALA GLU ASP GLU GLY VAL SER GLN ARG LYS PHE
SEQRES  14 A  243  LEU ASP GLY ASN GLU LEU THR LEU ALA ASP CYS ASN LEU
SEQRES  15 A  243  LEU PRO LYS LEU HIS ILE VAL GLN VAL VAL CYS LYS LYS
SEQRES  16 A  243  TYR ARG GLY PHE THR ILE PRO GLU ALA PHE ARG GLY VAL
SEQRES  17 A  243  HIS ARG TYR LEU SER ASN ALA TYR ALA ARG GLU GLU PHE
SEQRES  18 A  243  ALA SER THR CYS PRO ASP ASP GLU GLU ILE GLU LEU ALA
SEQRES  19 A  243  TYR GLU GLN VAL ALA LYS ALA LEU LYS
SEQRES   1 B  243  GLY SER MET ALA GLU GLU GLN PRO GLN VAL GLU LEU PHE
SEQRES   2 B  243  VAL LYS ALA GLY SER ASP GLY ALA LYS ILE GLY ASN CYS
SEQRES   3 B  243  PRO PHE SER GLN ARG LEU PHE MET VAL LEU TRP LEU LYS
SEQRES   4 B  243  GLY VAL THR PHE ASN VAL THR THR VAL ASP THR LYS ARG
SEQRES   5 B  243  ARG THR GLU THR VAL GLN LYS LEU CYS PRO GLY GLY GLN
SEQRES   6 B  243  LEU PRO PHE LEU LEU TYR GLY THR GLU VAL HIS THR ASP
SEQRES   7 B  243  THR ASN LYS ILE GLU GLU PHE LEU GLU ALA VAL LEU CYS
SEQRES   8 B  243  PRO PRO ARG TYR PRO LYS LEU ALA ALA LEU ASN PRO GLU
SEQRES   9 B  243  SER ASN THR ALA GLY LEU ASP ILE PHE ALA LYS PHE SER
SEQRES  10 B  243  ALA TYR ILE LYS ASN SER ASN PRO ALA LEU ASN ASP ASN
SEQRES  11 B  243  LEU GLU LYS GLY LEU LEU LYS ALA LEU LYS VAL LEU ASP
SEQRES  12 B  243  ASN TYR LEU THR SER PRO LEU PRO GLU GLU VAL ASP GLU
SEQRES  13 B  243  THR SER ALA GLU ASP GLU GLY VAL SER GLN ARG LYS PHE
SEQRES  14 B  243  LEU ASP GLY ASN GLU LEU THR LEU ALA ASP CYS ASN LEU
SEQRES  15 B  243  LEU PRO LYS LEU HIS ILE VAL GLN VAL VAL CYS LYS LYS
SEQRES  16 B  243  TYR ARG GLY PHE THR ILE PRO GLU ALA PHE ARG GLY VAL
SEQRES  17 B  243  HIS ARG TYR LEU SER ASN ALA TYR ALA ARG GLU GLU PHE
SEQRES  18 B  243  ALA SER THR CYS PRO ASP ASP GLU GLU ILE GLU LEU ALA
SEQRES  19 B  243  TYR GLU GLN VAL ALA LYS ALA LEU LYS
FORMUL   3  HOH   *342(H2 O)
HELIX    1   1 SER A   27  GLY A   38  1                                  12
HELIX    2   2 THR A   44  CYS A   59  1                                  16
HELIX    3   3 ASN A   78  LEU A   88  1                                  11
HELIX    4   4 ASN A  100  THR A  105  5                                   6
HELIX    5   5 ASP A  109  ASN A  120  1                                  12
HELIX    6   6 ASN A  122  ALA A  124  5                                   3
HELIX    7   7 LEU A  125  SER A  146  1                                  22
HELIX    8   8 LEU A  148  VAL A  152  5                                   5
HELIX    9   9 THR A  174  GLY A  196  1                                  23
HELIX   10  10 PHE A  203  ALA A  215  1                                  13
HELIX   11  11 ARG A  216  SER A  221  1                                   6
HELIX   12  12 ASP A  225  TYR A  233  1                                   9
HELIX   13  13 SER B   27  LYS B   37  1                                  11
HELIX   14  14 THR B   44  CYS B   59  1                                  16
HELIX   15  15 ASN B   78  LEU B   88  1                                  11
HELIX   16  16 ASN B  100  THR B  105  5                                   6
HELIX   17  17 ASP B  109  ASN B  120  1                                  12
HELIX   18  18 ASN B  122  ALA B  124  5                                   3
HELIX   19  19 LEU B  125  SER B  146  1                                  22
HELIX   20  20 LEU B  148  VAL B  152  5                                   5
HELIX   21  21 THR B  174  GLY B  196  1                                  23
HELIX   22  22 PHE B  203  ALA B  215  1                                  13
HELIX   23  23 ARG B  216  SER B  221  1                                   6
HELIX   24  24 ASP B  225  GLU B  234  1                                  10
SSBOND   1 CYS A   24    CYS A   59                          1555   1555  2.04
SSBOND   2 CYS B   24    CYS B   59                          1555   1555  2.01
CISPEP   1 PRO A   90    PRO A   91          0        -3.44
CISPEP   2 PRO B   90    PRO B   91          0         2.44
CRYST1   59.861   69.189  107.506  90.00  90.00  90.00 P 21 21 21    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      0.016705  0.000000  0.000000        0.00000
SCALE2      0.000000  0.014453  0.000000        0.00000
SCALE3      0.000000  0.000000  0.009302        0.00000
      
PROCHECK
Go to PROCHECK summary
 References