HEADER ROTAMASE 18-AUG-95 1FKJ
TITLE ATOMIC STRUCTURE OF FKBP12-FK506, AN IMMUNOPHILIN IMMUNOSUPPRESSANT
TITLE 2 COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FK506 BINDING PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: FKBP12;
COMPND 5 EC: 5.2.1.8;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: MR 12,000 DALTONS
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;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS FK506 BINDING PROTEIN, FKBP12, CIS-TRANS PROLYL-ISOMERASE, ROTAMASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.P.WILSON,M.D.SINTCHAK,J.A.THOMSON,M.A.NAVIA
REVDAT 4 07-FEB-24 1FKJ 1 REMARK
REVDAT 3 13-JUL-11 1FKJ 1 VERSN
REVDAT 2 24-FEB-09 1FKJ 1 VERSN
REVDAT 1 07-DEC-95 1FKJ 0
JRNL AUTH K.P.WILSON,M.M.YAMASHITA,M.D.SINTCHAK,S.H.ROTSTEIN,
JRNL AUTH 2 M.A.MURCKO,J.BOGER,J.A.THOMSON,M.J.FITZGIBBON,J.R.BLACK,
JRNL AUTH 3 M.A.NAVIA
JRNL TITL COMPARATIVE X-RAY STRUCTURES OF THE MAJOR BINDING PROTEIN
JRNL TITL 2 FOR THE IMMUNOSUPPRESSANT FK506 (TACROLIMUS) IN UNLIGANDED
JRNL TITL 3 FORM AND IN COMPLEX WITH FK506 AND RAPAMYCIN.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 51 511 1995
JRNL REFN ISSN 0907-4449
JRNL PMID 15299838
JRNL DOI 10.1107/S0907444994014514
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.P.GRIFFITH,J.L.KIM,E.E.KIM,M.D.SINTCHAK,J.A.THOMSON,
REMARK 1 AUTH 2 M.J.FITZGIBBON,M.A.FLEMING,P.R.CARON,K.HSIAO,M.A.NAVIA
REMARK 1 TITL X-RAY STRUCTURE OF CALCINEURIN INHIBITED BY THE
REMARK 1 TITL 2 IMMUNOPHILIN-IMMUNOSUPPRESSANT FKBP12-FK506 COMPLEX
REMARK 1 REF CELL(CAMBRIDGE,MASS.) V. 82 507 1995
REMARK 1 REFN ISSN 0092-8674
REMARK 1 REFERENCE 2
REMARK 1 AUTH J.ROTONDA,J.J.BURBAUM,H.K.CHAN,A.I.MARCY,J.W.BECKER
REMARK 1 TITL IMPROVED CALCINEURIN INHIBITION BY YEAST FKBP12-DRUG
REMARK 1 TITL 2 COMPLEXES. CRYSTALLOGRAPHIC AND FUNCTIONAL ANALYSIS
REMARK 1 REF J.BIOL.CHEM. V. 268 7607 1993
REMARK 1 REFN ISSN 0021-9258
REMARK 1 REFERENCE 3
REMARK 1 AUTH J.W.BECKER,J.ROTONDA,B.M.MCKEEVER,H.K.CHAN,A.I.MARCY,
REMARK 1 AUTH 2 G.WIEDERRECHT,J.D.HERMES,J.P.SPRINGER
REMARK 1 TITL FK-506-BINDING PROTEIN: THREE-DIMENSIONAL STRUCTURE OF THE
REMARK 1 TITL 2 COMPLEX WITH THE ANTAGONIST L-685,818
REMARK 1 REF J.MOL.BIOL. V. 268 11335 1993
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 4
REMARK 1 AUTH G.D.VAN DUYNE,R.F.STANDAERT,P.A.KARPLUS,S.L.SCHREIBER,
REMARK 1 AUTH 2 J.CLARDY
REMARK 1 TITL ATOMIC STRUCTURES OF HUMAN IMMUNOPHILIN FKBP-12 COMPLEXES
REMARK 1 TITL 2 WITH FK506 AND RAPAMYCIN
REMARK 1 REF J.MOL.BIOL. V. 229 105 1993
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 5
REMARK 1 AUTH G.D.VAN DUYNE,R.F.STANDAERT,S.L.SCHREIBER,J.CLARDY
REMARK 1 TITL ATOMIC STRUCTURE OF THE RAPAMYCIN HUMAN IMMUNOPHILIN FKBP-12
REMARK 1 TITL 2 COMPLEX
REMARK 1 REF J.AM.CHEM.SOC. V. 113 7433 1991
REMARK 1 REFN ISSN 0002-7863
REMARK 1 REFERENCE 6
REMARK 1 AUTH G.D.VAN DUYNE,R.F.STANDAERT,P.A.KARPLUS,S.L.SCHREIBER,
REMARK 1 AUTH 2 J.CLARDY
REMARK 1 TITL ATOMIC STRUCTURE OF FKBP-FK506, AN
REMARK 1 TITL 2 IMMUNOPHILIN-IMMUNOSUPPRESSANT COMPLEX
REMARK 1 REF SCIENCE V. 252 839 1991
REMARK 1 REFN ISSN 0036-8075
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 7.00
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) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 8631
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) : 0.162
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 : 832
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 57
REMARK 3 SOLVENT ATOMS : 97
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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) : 0.014
REMARK 3 BOND ANGLES (DEGREES) : 2.870
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1FKJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000173318.
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) : N
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) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MANUFACTURER SUPPLIED (MSC)
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
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.02
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.98
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42 21 2
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 -Y+1/2,X+1/2,Z+1/2
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/2
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 0.000000 -1.000000 0.000000 29.05000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 29.05000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 27.85000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 29.05000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 29.05000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 27.85000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 29.05000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 29.05000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 27.85000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 29.05000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 29.05000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 27.85000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 55.70000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9710 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17910 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -50.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 58.10000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 58.10000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 -1.000000 55.70000
REMARK 350 BIOMT1 4 0.000000 -1.000000 0.000000 58.10000
REMARK 350 BIOMT2 4 -1.000000 0.000000 0.000000 58.10000
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 55.70000
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 HIS A 25 NE2 HIS A 25 CD2 -0.067
REMARK 500
REMARK 500 REMARK: NULL
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 TRP A 59 CD1 - CG - CD2 ANGL. DEV. = 6.7 DEGREES
REMARK 500 TRP A 59 CG - CD1 - NE1 ANGL. DEV. = -6.2 DEGREES
REMARK 500 TRP A 59 CE2 - CD2 - CG ANGL. DEV. = -5.1 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 ARG A 13 -25.18 -147.26
REMARK 500 ALA A 81 -116.13 -141.11
REMARK 500 ILE A 90 -49.98 -131.51
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 RESIDUE FK5 A 108
DBREF 1FKJ A 1 107 UNP P62942 FKB1A_HUMAN 1 107
SEQRES 1 A 107 GLY VAL GLN VAL GLU THR ILE SER PRO GLY ASP GLY ARG
SEQRES 2 A 107 THR PHE PRO LYS ARG GLY GLN THR CYS VAL VAL HIS TYR
SEQRES 3 A 107 THR GLY MET LEU GLU ASP GLY LYS LYS PHE ASP SER SER
SEQRES 4 A 107 ARG ASP ARG ASN LYS PRO PHE LYS PHE MET LEU GLY LYS
SEQRES 5 A 107 GLN GLU VAL ILE ARG GLY TRP GLU GLU GLY VAL ALA GLN
SEQRES 6 A 107 MET SER VAL GLY GLN ARG ALA LYS LEU THR ILE SER PRO
SEQRES 7 A 107 ASP TYR ALA TYR GLY ALA THR GLY HIS PRO GLY ILE ILE
SEQRES 8 A 107 PRO PRO HIS ALA THR LEU VAL PHE ASP VAL GLU LEU LEU
SEQRES 9 A 107 LYS LEU GLU
HET FK5 A 108 57
HETNAM FK5 8-DEETHYL-8-[BUT-3-ENYL]-ASCOMYCIN
HETSYN FK5 K506
FORMUL 2 FK5 C44 H69 N O12
FORMUL 3 HOH *97(H2 O)
HELIX 1 1 ARG A 40 ARG A 42 5 3
HELIX 2 2 ARG A 57 GLN A 65 1 9
HELIX 3 3 PRO A 78 TYR A 80 5 3
SHEET 1 A 5 PHE A 46 MET A 49 0
SHEET 2 A 5 THR A 21 LEU A 30 -1 N VAL A 24 O PHE A 46
SHEET 3 A 5 LEU A 97 LEU A 106 -1 N LYS A 105 O VAL A 23
SHEET 4 A 5 ARG A 71 ILE A 76 -1 N ILE A 76 O LEU A 97
SHEET 5 A 5 VAL A 2 SER A 8 -1 N SER A 8 O ARG A 71
SHEET 1 B 2 THR A 27 MET A 29 0
SHEET 2 B 2 LYS A 35 SER A 38 -1 N ASP A 37 O GLY A 28
SITE 1 AC1 21 TYR A 26 PHE A 36 ASP A 37 ARG A 42
SITE 2 AC1 21 PHE A 46 GLU A 54 VAL A 55 ILE A 56
SITE 3 AC1 21 TRP A 59 ALA A 81 TYR A 82 THR A 85
SITE 4 AC1 21 GLY A 86 HIS A 87 PRO A 88 ILE A 91
SITE 5 AC1 21 PHE A 99 HOH A 119 HOH A 122 HOH A 137
SITE 6 AC1 21 HOH A 199
CRYST1 58.100 58.100 55.700 90.00 90.00 90.00 P 42 21 2 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 0.017212 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017212 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017953 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
