Header list of 1fkt.pdb file
Complete list - 29 20 Bytes
HEADER CIS-TRANS ISOMERASE 05-MAR-92 1FKT
TITLE SOLUTION STRUCTURE OF FKBP, A ROTAMASE ENZYME AND RECEPTOR FOR FK506
TITLE 2 AND RAPAMYCIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FK506 AND RAPAMYCIN-BINDING PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 CELL_LINE: S2
KEYWDS CIS-TRANS ISOMERASE
EXPDTA SOLUTION NMR
AUTHOR S.W.MICHNICK,M.K.ROSEN,T.J.WANDLESS,M.KARPLUS,S.L.SCHREIBER
REVDAT 3 29-NOV-17 1FKT 1 REMARK HELIX
REVDAT 2 24-FEB-09 1FKT 1 VERSN
REVDAT 1 31-JAN-94 1FKT 0
JRNL AUTH S.W.MICHNICK,M.K.ROSEN,T.J.WANDLESS,M.KARPLUS,S.L.SCHREIBER
JRNL TITL SOLUTION STRUCTURE OF FKBP, A ROTAMASE ENZYME AND RECEPTOR
JRNL TITL 2 FOR FK506 AND RAPAMYCIN.
JRNL REF SCIENCE V. 252 836 1991
JRNL REFN ISSN 0036-8075
JRNL PMID 1709301
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.K.ROSEN,S.W.MICHNICK,M.KARPLUS,S.L.SCHREIBER
REMARK 1 TITL PROTON AND NITROGEN SEQUENTIAL ASSIGNMENTS AND SECONDARY
REMARK 1 TITL 2 STRUCTURE DETERMINATION OF THE HUMAN FK506 AND RAPAMYCIN
REMARK 1 TITL 3 BINDING PROTEIN
REMARK 1 REF BIOCHEMISTRY V. 30 4774 1991
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 2
REMARK 1 AUTH R.F.STANDAERT,A.GALAT,G.L.VERDINE,S.L.SCHREIBER
REMARK 1 TITL MOLECULAR CLONING AND OVEREXPRESSION OF THE HUMAN
REMARK 1 TITL 2 FK506-BINDING PROTEIN FKBP
REMARK 1 REF NATURE V. 346 671 1990
REMARK 1 REFN ISSN 0028-0836
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1FKT 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_1000173323.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: NULL
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
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: MONOMERIC
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 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 A 13 NE - CZ - NH1 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG A 18 NE - CZ - NH1 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG A 40 NE - CZ - NH1 ANGL. DEV. = -5.3 DEGREES
REMARK 500 ARG A 42 NE - CZ - NH1 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG A 57 NE - CZ - NH1 ANGL. DEV. = -3.8 DEGREES
REMARK 500 TRP A 59 CG - CD1 - NE1 ANGL. DEV. = -7.2 DEGREES
REMARK 500 TRP A 59 CD1 - NE1 - CE2 ANGL. DEV. = 8.3 DEGREES
REMARK 500 TRP A 59 NE1 - CE2 - CZ2 ANGL. DEV. = 12.1 DEGREES
REMARK 500 TRP A 59 NE1 - CE2 - CD2 ANGL. DEV. = -7.5 DEGREES
REMARK 500 TRP A 59 CG - CD2 - CE3 ANGL. DEV. = -6.5 DEGREES
REMARK 500 GLU A 61 OE1 - CD - OE2 ANGL. DEV. = 7.5 DEGREES
REMARK 500 ARG A 71 NE - CZ - NH1 ANGL. DEV. = -4.3 DEGREES
REMARK 500 LYS A 73 N - CA - C ANGL. DEV. = -16.9 DEGREES
REMARK 500 GLU A 107 N - CA - C ANGL. DEV. = -18.2 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 GLU A 31 -59.33 -19.01
REMARK 500 ASP A 32 20.51 -140.03
REMARK 500 LYS A 34 -168.26 -160.63
REMARK 500 SER A 39 73.75 -106.10
REMARK 500 ARG A 40 50.61 -101.67
REMARK 500 ARG A 42 -76.87 -17.91
REMARK 500 LYS A 44 79.38 -157.24
REMARK 500 PRO A 45 157.54 -36.64
REMARK 500 GLN A 53 54.96 38.60
REMARK 500 ALA A 81 -115.52 -116.44
REMARK 500 TYR A 82 58.70 -114.16
REMARK 500 PRO A 88 87.84 -57.11
REMARK 500 PRO A 92 170.52 -56.55
REMARK 500 PRO A 93 170.44 -58.56
REMARK 500 HIS A 94 57.72 18.42
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 13 0.29 SIDE CHAIN
REMARK 500 ARG A 18 0.32 SIDE CHAIN
REMARK 500 ARG A 40 0.26 SIDE CHAIN
REMARK 500 ARG A 42 0.24 SIDE CHAIN
REMARK 500 ARG A 57 0.31 SIDE CHAIN
REMARK 500 ARG A 71 0.29 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: BND
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1FKR RELATED DB: PDB
REMARK 900 RELATED ID: 1FKS RELATED DB: PDB
DBREF 1FKT 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
HELIX 1 H1 ARG A 57 GLN A 65 1LAST RESIDUE MAY BE 3/10 9
SHEET 1 S1 5 VAL A 2 SER A 8 0
SHEET 2 S1 5 ARG A 71 SER A 77 -1
SHEET 3 S1 5 LEU A 97 LEU A 106 -1
SHEET 4 S1 5 THR A 21 GLU A 31 -1
SHEET 5 S1 5 LYS A 35 SER A 38 -1
SHEET 1 S2 5 VAL A 2 SER A 8 0
SHEET 2 S2 5 ARG A 71 SER A 77 -1
SHEET 3 S2 5 LEU A 97 LEU A 106 -1
SHEET 4 S2 5 THR A 21 GLU A 31 -1
SHEET 5 S2 5 PHE A 46 MET A 49 -1
SITE 1 BND 8 TYR A 26 PHE A 36 PHE A 46 VAL A 55
SITE 2 BND 8 ILE A 56 TRP A 59 TYR A 82 PHE A 99
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
Complete list - 29 20 Bytes