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PDBsum entry 1qng

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Top Page protein Protein-protein interface(s) links
Isomerase/immunosuppressant PDB id
1qng
Jmol
Contents
Protein chains
170 a.a. *
11 a.a. *
Waters ×175
* Residue conservation analysis
HEADER    ISOMERASE/IMMUNOSUPPRESSANT             14-OCT-99   1QNG
TITLE     PLASMODIUM FALCIPARUM CYCLOPHILIN COMPLEXED WITH
TITLE    2 CYCLOSPORIN A
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: PPIASE, ROTAMASE, CYCLOPHILIN A;
COMPND   5 EC: 5.2.1.8;
COMPND   6 ENGINEERED: YES;
COMPND   7 MOL_ID: 2;
COMPND   8 MOLECULE: CYCLOSPORIN A;
COMPND   9 CHAIN: D;
COMPND  10 SYNONYM: CYCLOSPORINE, CICLOSPORIN, CICLOSPORINE
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: PLASMODIUM FALCIPARUM;
SOURCE   3 ORGANISM_TAXID: 5833;
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE   7 MOL_ID: 2;
SOURCE   8 ORGANISM_SCIENTIFIC: TOLYPOCLADIUM INFLATUM;
SOURCE   9 ORGANISM_TAXID: 29910
KEYWDS    ISOMERASE-IMMUNOSUPPRESSANT COMPLEX, CYCLOPHILIN-CYCLOSPORIN
KEYWDS   2 COMPLEX, CYCLOSPORIN A, IMMUNOSUPPRESSANT, CYCLOPHILIN
EXPDTA    X-RAY DIFFRACTION
AUTHOR    M.R.PETERSON,D.R.HALL,W.N.HUNTER
REVDAT   5   12-MAR-14 1QNG    1       COMPND SOURCE REMARK
REVDAT   4   13-JUL-11 1QNG    1       VERSN
REVDAT   3   24-FEB-09 1QNG    1       VERSN
REVDAT   2   23-JUL-02 1QNG    1       HEADER
REVDAT   1   13-OCT-00 1QNG    0
JRNL        AUTH   M.R.PETERSON,D.R.HALL,M.BERRIMAN,G.A.LEONARD,A.H.FAIRLAMB,
JRNL        AUTH 2 W.N.HUNTER
JRNL        TITL   THE THREE-DIMENSIONAL STRUCTURE OF A PLASMODIUM FALCIPARUM
JRNL        TITL 2 CYCLOPHILIN IN COMPLEX WITH THE POTENT ANTI-MALARIAL
JRNL        TITL 3 CYCLOSPORIN A
JRNL        REF    J.MOL.BIOL.                   V. 298   123 2000
JRNL        REFN                   ISSN 0022-2836
JRNL        PMID   10756109
JRNL        DOI    10.1006/JMBI.2000.3633
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   M.BERRIMAN,A.H.FAIRLAMB
REMARK   1  TITL   DETAILED CHARACTERIZATION OF A CYCLOPHILIN FROM THE HUMAN
REMARK   1  TITL 2 MALARIA PARASITE PLASMODIUM FALCIPARUM
REMARK   1  REF    BIOCHEM.J.                    V. 334   437 1998
REMARK   1  REFN                   ISSN 0264-6021
REMARK   1  PMID   9716503
REMARK   2
REMARK   2 RESOLUTION.    2.1  ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS 0.5
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) : 2.1
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 32.8
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 92.3
REMARK   3   NUMBER OF REFLECTIONS             : 8101
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) : 0.15
REMARK   3   FREE R VALUE                     : 0.19
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0
REMARK   3   FREE R VALUE TEST SET COUNT      : 388
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 8
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.1
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.2
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 89.5
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 954
REMARK   3   BIN R VALUE           (WORKING SET) : 0.17
REMARK   3   BIN FREE R VALUE                    : 0.21
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 49
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            : 1326
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 73
REMARK   3   SOLVENT ATOMS            : 175
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 26.5
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 21.8
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) : NULL
REMARK   3   ESD FROM SIGMAA              (A) : NULL
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.006
REMARK   3   BOND ANGLES            (DEGREES) : 1.3
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL
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) : 1.124 ; 1.5
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.714 ; 2.0
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.810 ; 2.0
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.510 ; 2.5
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : NULL
REMARK   3   KSOL        : NULL
REMARK   3   BSOL        : NULL
REMARK   3
REMARK   3  NCS MODEL : NULL
REMARK   3
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM
REMARK   3  PARAMETER FILE  3  : NULL
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP
REMARK   3  TOPOLOGY FILE  3   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: REFINEMENT AT EARLY STAGES UTILISED
REMARK   3  REFMAC. THE SIDE CHAIN OF ARG49 IS DISORDERED
REMARK   4
REMARK   4 1QNG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-OCT-99.
REMARK 100 THE PDBE ID CODE IS EBI-4206.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : 100.0
REMARK 200  PH                             : 7.50
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          : RIGAKU/MSC RU-H3R
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : R-AXIS IV
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 8101
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100
REMARK 200  RESOLUTION RANGE LOW       (A) : 32.800
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.3
REMARK 200  DATA REDUNDANCY                : 3.000
REMARK 200  R MERGE                    (I) : 0.03500
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 26.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.15
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.00
REMARK 200  R MERGE FOR SHELL          (I) : 0.06100
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 15.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS 0.5
REMARK 200 STARTING MODEL: PDB ENTRY 1QNH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,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
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 1140 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9710 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.6 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 400
REMARK 400 COMPOUND
REMARK 400 CYCLOSPORIN IS A CYCLIC UNDECAPEPTIDE.
REMARK 400 HERE, CYCLOSPORIN A IS REPRESENTED BY THE SEQUENCE (SEQRES)
REMARK 400
REMARK 400  GROUP: 1
REMARK 400   NAME: CYCLOSPORIN A
REMARK 400   CHAIN: D
REMARK 400   COMPONENT_1: PEPTIDE LIKE SEQUENCE RESIDUES 1 TO 11
REMARK 400   DESCRIPTION: CYCLOSPORIN IS A CYCLIC UNDECAPEPTIDE.
REMARK 400                CYCLIZATION IS ACHIEVED BY LINKING THE N- AND
REMARK 400                THE C- TERMINI.
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     ARG A  49    CG   CD   NE   CZ   NH1  NH2
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    PHE A  67      -76.78   -144.35
REMARK 500    SER A 116     -106.09   -134.45
REMARK 500    MLE D 210     -167.82   -107.97
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN D OF CYCLOSPORIN A
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1BCK   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF HUMAN CYCLOPHILIN A COMPLEXED WITH
REMARK 900  CYCLOSPORIN C
REMARK 900 RELATED ID: 1C5F   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF THE CYCLOPHILIN-LIKE DOMAIN FROM
REMARK 900  BRUGIA MALAYI COMPLEXED WITH CYCLOSPORIN A
REMARK 900 RELATED ID: 1CSA   RELATED DB: PDB
REMARK 900  SOLUTION STRUCTURE OF E.COLI  CYCLOPHILIN (F112W) COMPLEXED WITH
REMARK 900  CYCLOSPORIN A
REMARK 900 RELATED ID: 1CWA   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF HUMAN CYCLOPHILIN A COMPLEXED WITH
REMARK 900  CYCLOSPORIN A
REMARK 900 RELATED ID: 1CWB   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF HUMAN CYCLOPHILIN A COMPLEXED WITH
REMARK 900  MODIFIED CYCLOSPORIN A AT POSITION 5
REMARK 900 RELATED ID: 1CWC   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF HUMAN CYCLOPHILIN A COMPLEXED WITH
REMARK 900  MODIFIED CYCLOSPORIN A AT POSITION 8
REMARK 900 RELATED ID: 1CWF   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF HUMAN CYCLOPHILIN A COMPLEXED WITH
REMARK 900  CYCLOSPORIN D
REMARK 900 RELATED ID: 1CWH   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF HUMAN CYCLOPHILIN A COMPLEXED WITH
REMARK 900  CYCLOSPORIN A MODIFIED AT POSITION 7
REMARK 900 RELATED ID: 1CWI   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF HUMAN CYCLOPHILIN A COMPLEXED WITH
REMARK 900  MODIFIED CYCLOSPORIN D AT POSITION 7
REMARK 900 RELATED ID: 1CWJ   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF HUMAN CYCLOPHILIN A COMPLEXED WITH
REMARK 900  MODIFIED CYCLOSPORIN D AT POSITIONS 5 AND 7.
REMARK 900 RELATED ID: 1CWK   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF HUMAN CYCLOPHILIN A COMPLEXED WITH
REMARK 900  MODIFIED CYCLOSPORIN D AT POSITIONS 5 AND 7.
REMARK 900 RELATED ID: 1CWL   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF HUMAN CYCLOPHILIN A COMPLEXED WITH
REMARK 900  MODIFIED CYCLOSPORIN A AT POSITION 8
REMARK 900 RELATED ID: 1CWM   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF HUMAN CYCLOPHILIN A COMPLEXED WITH
REMARK 900  MODIFIED CYCLOSPORIN A AT POSITION 8
REMARK 900 RELATED ID: 1CWO   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF HUMAN CYCLOPHILIN A COMPLEXED WITH
REMARK 900  NODIFIED CYCLOSPORIN C AT POSITIONS 1,  AND 9
REMARK 900 RELATED ID: 1CYA   RELATED DB: PDB
REMARK 900  SOLUTION STRUCTURE OF HUMAN CYCLOPHILIN COMPLEXED WIYH
REMARK 900  CYCLOSPORIN A
REMARK 900 RELATED ID: 1CYB   RELATED DB: PDB
REMARK 900  SOLUTION STRUCTURE OF HUMAN CYCLOPHILIN COMPLEXED WITH
REMARK 900  CYCLOSPORIN A
REMARK 900 RELATED ID: 1CYN   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF HUMAN CYCLOPHILIN B COMPLEXED WITH
REMARK 900  MODIFIED CYCLOSPORIN A
REMARK 900 RELATED ID: 1IKF   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF CTCLOSPORIN-FAB COMPLEX
REMARK 900 RELATED ID: 1M63   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF CALCINEURIN-CYCLOPHILIN-CYCLOSPORIN
REMARK 900  COMPLEX
REMARK 900 RELATED ID: 1MF8   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF HUMAN CALCINEURIN COMPLEXED WITH
REMARK 900  HUMAN CYCLOPHILIN AND CYCLOSPORIN A
REMARK 900 RELATED ID: 1MIK   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF HUMAN CYCLOPHILIN A COMPLEXED WITH
REMARK 900  MODIFIED CYCLOSPORIN A AT POSITION 6
REMARK 900 RELATED ID: 1QNH   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF PLASMODIUM FALCIPARUM CYCLOPHILIN
REMARK 900  (DOUBLE MUTANT) COMPLEXED WITH CYCLOSPORIN A
REMARK 900 RELATED ID: 1XQ7   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF TRYPANOSOMA CRUZI CYCLOPHILIN
REMARK 900  COMPLEXED WITH CYCLOSPORIN A
REMARK 900 RELATED ID: 2ESL   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF HUMAN CYCLOPHILIN C COMPLEXED WITH
REMARK 900  CYCLOSPORIN A
REMARK 900 RELATED ID: 2OJU   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF HUMAN CYCLOPHILIN J COMPLEXED WITH
REMARK 900  CYCLOSPORIN A
REMARK 900 RELATED ID: 2POY   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF CRYPTOSPORIDIUM PARVUM IOWA II
REMARK 900  CYCLOPHILIN A COMPLEXED WITH CYCLOSPORIN A
REMARK 900 RELATED ID: 2RMA   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF HUMAN CYCLOPHILIN A COMPLEXED WITH
REMARK 900  CYCLOSPORIN A
REMARK 900 RELATED ID: 2RMB   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF HUMAN CYCLOPHILIN A COMPLEXED WITH
REMARK 900  MODIFIED CYCLOSPORIN A AT POSITION 5
REMARK 900 RELATED ID: 2RMC   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF MURINE CYCLOPHILIN C COMPLEXED WITH
REMARK 900  CYCLOSPORIN A
REMARK 900 RELATED ID: 2WFJ   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF THE PPIASE DOMAIN OF
REMARK 900  HUMAN CYCLOPHILIN G COMPLEXED WITH CYCLOSPORIN A
REMARK 900 RELATED ID: 2X2C   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF HUMAN ACETYL-CYPA COMPLEXED WITH
REMARK 900  CYCLOSPORINE A
REMARK 900 RELATED ID: 2X7K   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF PPIL1 COMPLEXED WITH CYCLOSPORINE A
REMARK 900 RELATED ID: 2Z6W   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF HUMAN CYCLOPHILIN D IN COMPLEX WITH
REMARK 900  CYCLOSPORIN A
REMARK 900 RELATED ID: 3BO7   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF CYCLOSPHILIN A FROM TOXOPLASMA
REMARK 900  GONDII COMPLEXED WIT CYCLOSPORIN A
REMARK 900 RELATED ID: 3CYS   RELATED DB: PDB
REMARK 900  SOLUTION STRUCTURE OF THE HUMAN CYCLOSPORIN A COMPLEXED
REMARK 900  WITH CYCLOSPORIN A
REMARK 900 RELATED ID: 3EOV   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF CYCLOPHILIN FROM LEISHMANIA DONOVANI
REMARK 900  COMPLEXED WITH CYCLOSPORIN A
DBREF  1QNG A    2   171  UNP    Q25756   Q25756           2    171
DBREF  1QNG D  201   211  NOR    NOR00033 NOR00033         1     11
SEQRES   1 A  170  SER LYS ARG SER LYS VAL PHE PHE ASP ILE SER ILE ASP
SEQRES   2 A  170  ASN SER ASN ALA GLY ARG ILE ILE PHE GLU LEU PHE SER
SEQRES   3 A  170  ASP ILE THR PRO ARG THR CYS GLU ASN PHE ARG ALA LEU
SEQRES   4 A  170  CYS THR GLY GLU LYS ILE GLY SER ARG GLY LYS ASN LEU
SEQRES   5 A  170  HIS TYR LYS ASN SER ILE PHE HIS ARG ILE ILE PRO GLN
SEQRES   6 A  170  PHE MET CYS GLN GLY GLY ASP ILE THR ASN GLY ASN GLY
SEQRES   7 A  170  SER GLY GLY GLU SER ILE TYR GLY ARG SER PHE THR ASP
SEQRES   8 A  170  GLU ASN PHE ASN MET LYS HIS ASP GLN PRO GLY LEU LEU
SEQRES   9 A  170  SER MET ALA ASN ALA GLY PRO ASN THR ASN SER SER GLN
SEQRES  10 A  170  PHE PHE ILE THR LEU VAL PRO CYS PRO TRP LEU ASP GLY
SEQRES  11 A  170  LYS HIS VAL VAL PHE GLY LYS VAL ILE GLU GLY MET ASN
SEQRES  12 A  170  VAL VAL ARG GLU MET GLU LYS GLU GLY ALA LYS SER GLY
SEQRES  13 A  170  TYR VAL LYS ARG SER VAL VAL ILE THR ASP CYS GLY GLU
SEQRES  14 A  170  LEU
SEQRES   1 D   11  DAL MLE MLE MVA BMT ABA SAR MLE VAL MLE ALA
HET    DAL  D 201       5
HET    MLE  D 202       9
HET    MLE  D 203       9
HET    MVA  D 204       8
HET    BMT  D 205      13
HET    ABA  D 206       6
HET    SAR  D 207       5
HET    MLE  D 208       9
HET    MLE  D 210       9
HETNAM     DAL D-ALANINE
HETNAM     MVA N-METHYLVALINE
HETNAM     BMT 4-METHYL-4-[(E)-2-BUTENYL]-4,N-METHYL-
HETNAM   2 BMT  THREONINE
HETNAM     ABA ALPHA-AMINOBUTYRIC ACID
HETNAM     SAR SARCOSINE
HETNAM     MLE N-METHYLLEUCINE
FORMUL   2  BMT    C10 H19 N O3
FORMUL   2  ABA    C4 H9 N O2
FORMUL   2  SAR    C3 H7 N O2
FORMUL   2  MLE    4(C7 H15 N O2)
FORMUL   2  DAL    C3 H7 N O2
FORMUL   2  MVA    C6 H13 N O2
FORMUL   3  HOH   *175(H2 O)
HELIX    1   1 THR A   30  GLY A   43  1                                  14
HELIX    2   2 CYS A  126  ASP A  130  5                                   5
HELIX    3   3 GLY A  142  LYS A  151  1                                  10
SHEET    1  AA 8 ARG A  62  ILE A  64  0
SHEET    2  AA 8 MET A  68  GLY A  71 -1  O  MET A  68   N  ILE A  64
SHEET    3  AA 8 PHE A 119  THR A 122 -1  O  PHE A 119   N  GLY A  71
SHEET    4  AA 8 LEU A 104  MET A 107 -1  O  LEU A 104   N  THR A 122
SHEET    5  AA 8 VAL A 135  GLU A 141 -1  N  PHE A 136   O  LEU A 105
SHEET    6  AA 8 ASN A  17  LEU A  25 -1  O  ILE A  22   N  ILE A 140
SHEET    7  AA 8 LYS A   6  ILE A  13 -1  O  VAL A   7   N  PHE A  23
SHEET    8  AA 8 VAL A 163  LEU A 171 -1  O  VAL A 164   N  SER A  12
SHEET    1  AB 2 LYS A  45  ILE A  46  0
SHEET    2  AB 2 ASN A  52  LEU A  53 -1  O  LEU A  53   N  LYS A  45
LINK         N   DAL D 201                 C   ALA D 211     1555   1555  1.34
LINK         C   DAL D 201                 N   MLE D 202     1555   1555  1.37
LINK         C   MLE D 202                 N   MLE D 203     1555   1555  1.35
LINK         C   MLE D 203                 N   MVA D 204     1555   1555  1.36
LINK         C   MVA D 204                 N   BMT D 205     1555   1555  1.38
LINK         C   BMT D 205                 N   ABA D 206     1555   1555  1.35
LINK         C   ABA D 206                 N   SAR D 207     1555   1555  1.36
LINK         C   SAR D 207                 N   MLE D 208     1555   1555  1.36
LINK         C   MLE D 208                 N   VAL D 209     1555   1555  1.32
LINK         C   VAL D 209                 N   MLE D 210     1555   1555  1.35
LINK         C   MLE D 210                 N   ALA D 211     1555   1555  1.33
SITE     1 AC1 19 ILE A  22  ASN A  52  ARG A  62  PHE A  67
SITE     2 AC1 19 MET A  68  GLN A  70  GLY A  79  ALA A 108
SITE     3 AC1 19 ASN A 109  ALA A 110  GLN A 118  PHE A 120
SITE     4 AC1 19 TRP A 128  LEU A 129  HIS A 133  GLU A 141
SITE     5 AC1 19 HOH D2001  HOH D2002  HOH D2003
CRYST1   35.460   37.690   37.990  61.08  62.70  85.08 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      0.028201 -0.002428 -0.015419        0.00000
SCALE2      0.000000  0.026630 -0.015448        0.00000
SCALE3      0.000000  0.000000  0.034246        0.00000
      
PROCHECK
Go to PROCHECK summary
 References