HEADER ISOMERASE/IMMUNOSUPPRESSANT 30-APR-98 1CWF
TITLE HUMAN CYCLOPHILIN A COMPLEXED WITH 2-VAL CYCLOSPORIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE A;
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 D;
COMPND 9 CHAIN: C;
COMPND 10 SYNONYM: CYCLOSPORINE, CICLOSPORIN, CICLOSPORINE;
COMPND 11 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: CYCLOPHILIN;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_GENE: CYCLOPHILIN;
SOURCE 9 MOL_ID: 2;
SOURCE 10 SYNTHETIC: YES;
SOURCE 11 ORGANISM_SCIENTIFIC: TOLYPOCLADIUM INFLATUM;
SOURCE 12 ORGANISM_TAXID: 29910
KEYWDS ISOMERASE-IMMUNOSUPPRESSANT COMPLEX, CYCLOPHILIN-CYCLOSPORIN COMPLEX,
KEYWDS 2 CYCLOSPORIN D, IMMUNOSUPPRESSANT, CYCLOPHILIN
EXPDTA X-RAY DIFFRACTION
AUTHOR V.MIKOL,J.KALLEN,P.TAYLOR,M.D.WALKINSHAW
REVDAT 4 27-JUL-11 1CWF 1 REMARK
REVDAT 3 13-JUL-11 1CWF 1 VERSN
REVDAT 2 24-FEB-09 1CWF 1 VERSN
REVDAT 1 15-JUL-98 1CWF 0
JRNL AUTH J.KALLEN,V.MIKOL,P.TAYLOR,M.D.WALKINSHAW
JRNL TITL X-RAY STRUCTURES AND ANALYSIS OF 11 CYCLOSPORIN DERIVATIVES
JRNL TITL 2 COMPLEXED WITH CYCLOPHILIN A.
JRNL REF J.MOL.BIOL. V. 283 435 1998
JRNL REFN ISSN 0022-2836
JRNL PMID 9769216
JRNL DOI 10.1006/JMBI.1998.2108
REMARK 2
REMARK 2 RESOLUTION. 1.86 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.86
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 30000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.1000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.7
REMARK 3 NUMBER OF REFLECTIONS : 12089
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.177
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
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 : 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 : 1352
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 177
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.10
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) : 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) : 0.012
REMARK 3 BOND ANGLES (DEGREES) : 1.59
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
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 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 : PARAM19X.PRO
REMARK 3 PARAMETER FILE 2 : PARAM19.SOL
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1CWF 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 : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
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 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR 3.1
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.42
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 18.20000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 36.21000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.71000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 36.21000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 18.20000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 30.71000
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: 1030 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 7830 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
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 D IS REPRESENTED BY THE SEQUENCE (SEQRES)
REMARK 400
REMARK 400 GROUP: 1
REMARK 400 NAME: CYCLOSPORIN D
REMARK 400 CHAIN: C
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 400 CYCLOSPORIN D IS A NATURAL ANALOG OF CYCLOSPORIN A,
REMARK 400 OBTAINED FROM A DIFFERENT NUTRIENT BROTH AND
REMARK 400 DIFFERS FROM CYCLOSPORIN IN RESIDUE 6 (ABA6VAL).
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 60 -75.05 -120.84
REMARK 500 THR A 68 -79.57 -98.61
REMARK 500 ASN A 71 10.18 -144.94
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 MLE C 10 11.94
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 C OF CYCLOSPORIN D
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
REMARK 900 WITH 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: 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 HUMAN
REMARK 900 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: 1QNG RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PLASMODIUM FALCIPARUM CYCLOPHILIN
REMARK 900 COMPLEXED WITH CYCLOSPORIN A
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 HUMAN CYCLOPHILIN
REMARK 900 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 GONDII
REMARK 900 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 1CWF A 2 165 UNP P62937 PPIA_HUMAN 1 164
DBREF 1CWF C 1 11 NOR NOR00036 NOR00036 1 11
SEQRES 1 A 165 MET VAL ASN PRO THR VAL PHE PHE ASP ILE ALA VAL ASP
SEQRES 2 A 165 GLY GLU PRO LEU GLY ARG VAL SER PHE GLU LEU PHE ALA
SEQRES 3 A 165 ASP LYS VAL PRO LYS THR ALA GLU ASN PHE ARG ALA LEU
SEQRES 4 A 165 SER THR GLY GLU LYS GLY PHE GLY TYR LYS GLY SER CYS
SEQRES 5 A 165 PHE HIS ARG ILE ILE PRO GLY PHE MET CYS GLN GLY GLY
SEQRES 6 A 165 ASP PHE THR ARG HIS ASN GLY THR GLY GLY LYS SER ILE
SEQRES 7 A 165 TYR GLY GLU LYS PHE GLU ASP GLU ASN PHE ILE LEU LYS
SEQRES 8 A 165 HIS THR GLY PRO GLY ILE LEU SER MET ALA ASN ALA GLY
SEQRES 9 A 165 PRO ASN THR ASN GLY SER GLN PHE PHE ILE CYS THR ALA
SEQRES 10 A 165 LYS THR GLU TRP LEU ASP GLY LYS HIS VAL VAL PHE GLY
SEQRES 11 A 165 LYS VAL LYS GLU GLY MET ASN ILE VAL GLU ALA MET GLU
SEQRES 12 A 165 ARG PHE GLY SER ARG ASN GLY LYS THR SER LYS LYS ILE
SEQRES 13 A 165 THR ILE ALA ASP CYS GLY GLN LEU GLU
SEQRES 1 C 11 DAL MLE MLE MVA BMT VAL SAR MLE VAL MLE ALA
HET DAL C 1 5
HET MLE C 2 9
HET MLE C 3 9
HET MVA C 4 8
HET BMT C 5 13
HET SAR C 7 5
HET MLE C 8 9
HET MLE C 10 9
HETNAM DAL D-ALANINE
HETNAM MLE N-METHYLLEUCINE
HETNAM MVA N-METHYLVALINE
HETNAM BMT 4-METHYL-4-[(E)-2-BUTENYL]-4,N-METHYL-THREONINE
HETNAM SAR SARCOSINE
FORMUL 2 DAL C3 H7 N O2
FORMUL 2 MLE 4(C7 H15 N O2)
FORMUL 2 MVA C6 H13 N O2
FORMUL 2 BMT C10 H19 N O3
FORMUL 2 SAR C3 H7 N O2
FORMUL 3 HOH *177(H2 O)
HELIX 1 1 VAL A 29 GLY A 42 1 14
HELIX 2 2 THR A 119 ASP A 123 5 5
HELIX 3 3 GLY A 135 ARG A 144 1 10
SHEET 1 AA 8 ARG A 55 ILE A 57 0
SHEET 2 AA 8 MET A 61 GLY A 64 -1 O MET A 61 N ILE A 57
SHEET 3 AA 8 PHE A 112 CYS A 115 -1 O PHE A 112 N GLY A 64
SHEET 4 AA 8 ILE A 97 MET A 100 -1 O ILE A 97 N CYS A 115
SHEET 5 AA 8 VAL A 128 GLU A 134 -1 N PHE A 129 O LEU A 98
SHEET 6 AA 8 GLU A 15 LEU A 24 -1 O SER A 21 N LYS A 133
SHEET 7 AA 8 THR A 5 VAL A 12 -1 O VAL A 6 N PHE A 22
SHEET 8 AA 8 ILE A 156 GLN A 163 -1 O THR A 157 N ALA A 11
LINK C DAL C 1 N MLE C 2 1555 1555 1.32
LINK N DAL C 1 C ALA C 11 1555 1555 1.32
LINK C MLE C 2 N MLE C 3 1555 1555 1.34
LINK C MLE C 3 N MVA C 4 1555 1555 1.33
LINK C MVA C 4 N BMT C 5 1555 1555 1.33
LINK C BMT C 5 N VAL C 6 1555 1555 1.34
LINK C VAL C 6 N SAR C 7 1555 1555 1.33
LINK C SAR C 7 N MLE C 8 1555 1555 1.34
LINK C MLE C 8 N VAL C 9 1555 1555 1.33
LINK C VAL C 9 N MLE C 10 1555 1555 1.33
LINK C MLE C 10 N ALA C 11 1555 1555 1.32
SITE 1 AC1 18 ARG A 19 ARG A 55 PHE A 60 GLN A 63
SITE 2 AC1 18 GLY A 72 THR A 73 ALA A 101 ASN A 102
SITE 3 AC1 18 ALA A 103 GLN A 111 PHE A 113 TRP A 121
SITE 4 AC1 18 HIS A 126 LEU A 164 HOH A2066 HOH A2129
SITE 5 AC1 18 HOH C2001 HOH C2004
CRYST1 36.400 61.420 72.420 90.00 90.00 90.00 P 21 21 21 4
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 0.027473 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016281 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013808 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
