Header list of 1rot.pdb file
Complete list - 2 20 Bytes
HEADER ROTAMASE (ISOMERASE) 14-JUN-96 1ROT
TITLE STRUCTURE OF FKBP59-I, THE N-TERMINAL DOMAIN OF A 59 KDA FK506-BINDING
TITLE 2 PROTEIN, NMR, MINIMIZED AVERAGE STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FKBP59-I;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: FKBP52 OR HSP56;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS;
SOURCE 3 ORGANISM_COMMON: RABBIT;
SOURCE 4 ORGANISM_TAXID: 9986;
SOURCE 5 ORGAN: LIVER;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ROTAMASE (ISOMERASE), DOMAIN I (N-TERM) OF A 59 KDA, FK506-BINDING
KEYWDS 2 PROTEIN, PEPTIDYL PROLYL CIS-TRANS ISOMERASE
EXPDTA SOLUTION NMR
AUTHOR C.T.CRAESCU,N.ROUVIERE,A.POPESCU,E.CERPOLINI,M.-C.LEBEAU,E.-
AUTHOR 2 E.BAULIEU,J.MISPELTER
REVDAT 3 02-MAR-22 1ROT 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1ROT 1 VERSN
REVDAT 1 07-DEC-96 1ROT 0
JRNL AUTH C.T.CRAESCU,N.ROUVIERE,A.POPESCU,E.CERPOLINI,M.C.LEBEAU,
JRNL AUTH 2 E.E.BAULIEU,J.MISPELTER
JRNL TITL THREE-DIMENSIONAL STRUCTURE OF THE IMMUNOPHILIN-LIKE DOMAIN
JRNL TITL 2 OF FKBP59 IN SOLUTION.
JRNL REF BIOCHEMISTRY V. 35 11045 1996
JRNL REFN ISSN 0006-2960
JRNL PMID 8780506
JRNL DOI 10.1021/BI960975P
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH N.ROUVIERE-FOURMY,C.T.CRAESCU,J.MISPELTER,M.C.LEBEAU,
REMARK 1 AUTH 2 E.E.BAULIEU
REMARK 1 TITL 1H AND 15N ASSIGNMENT OF NMR SPECTRUM, SECONDARY STRUCTURE
REMARK 1 TITL 2 AND GLOBAL FOLDING OF THE IMMUNOPHILIN-LIKE DOMAIN OF THE
REMARK 1 TITL 3 59-KDA FK506-BINDING PROTEIN
REMARK 1 REF EUR.J.BIOCHEM. V. 231 761 1995
REMARK 1 REFN ISSN 0014-2956
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DISCOVER
REMARK 3 AUTHORS : BIOSYM
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: CVFF OF DISCOVER (BIOSYM)
REMARK 4
REMARK 4 1ROT 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_1000176167.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : 6.7
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 : MINIMIZED AVERAGE
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 RES C SSSEQI
REMARK 465 GLU A 1
REMARK 465 GLU A 2
REMARK 465 MET A 3
REMARK 465 ASP A 4
REMARK 465 ILE A 5
REMARK 465 LYS A 6
REMARK 465 ALA A 7
REMARK 465 ALA A 8
REMARK 465 GLU A 9
REMARK 465 SER A 10
REMARK 465 GLY A 11
REMARK 465 ALA A 12
REMARK 465 GLN A 13
REMARK 465 SER A 14
REMARK 465 ALA A 15
REMARK 465 PRO A 16
REMARK 465 LEU A 17
REMARK 465 PRO A 18
REMARK 465 LEU A 19
REMARK 465 GLU A 20
REMARK 465 GLU A 139
REMARK 465 ASP A 140
REMARK 465 LEU A 141
REMARK 465 THR A 142
REMARK 465 ASP A 143
REMARK 465 ASP A 144
REMARK 465 GLU A 145
REMARK 465 ASP A 146
REMARK 465 GLY A 147
REMARK 465 VAL A 148
REMARK 465 PRO A 149
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O GLN A 28 HD2 ASP A 29 1.56
REMARK 500
REMARK 500 REMARK: NULL
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 GLU A 30 CD GLU A 30 OE2 0.110
REMARK 500 GLU A 39 CD GLU A 39 OE2 0.109
REMARK 500 GLU A 44 CD GLU A 44 OE2 0.121
REMARK 500 GLU A 84 CD GLU A 84 OE2 0.111
REMARK 500 GLU A 100 CD GLU A 100 OE2 0.111
REMARK 500 GLU A 109 CD GLU A 109 OE2 0.110
REMARK 500 GLU A 130 CD GLU A 130 OE2 0.108
REMARK 500 GLU A 132 CD GLU A 132 OE2 0.109
REMARK 500 GLU A 135 CD GLU A 135 OE2 0.108
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 ASP A 23 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP A 23 CB - CG - OD2 ANGL. DEV. = -6.5 DEGREES
REMARK 500 ARG A 38 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 THR A 43 CA - CB - OG1 ANGL. DEV. = 12.9 DEGREES
REMARK 500 ARG A 51 CD - NE - CZ ANGL. DEV. = 9.1 DEGREES
REMARK 500 ARG A 51 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 HIS A 55 ND1 - CE1 - NE2 ANGL. DEV. = 8.5 DEGREES
REMARK 500 TRP A 59 CB - CG - CD2 ANGL. DEV. = 8.8 DEGREES
REMARK 500 TRP A 59 CD1 - NE1 - CE2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 ASP A 62 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP A 62 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 ASP A 67 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 ASP A 71 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP A 71 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 ARG A 72 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ASP A 74 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 ASP A 79 CB - CG - OD2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 GLU A 84 CA - C - N ANGL. DEV. = -13.5 DEGREES
REMARK 500 ASP A 90 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP A 90 CB - CG - OD2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 ARG A 103 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 ARG A 103 NE - CZ - NH2 ANGL. DEV. = -3.0 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 SER A 25 -62.98 -159.72
REMARK 500 PRO A 26 22.87 -70.77
REMARK 500 LYS A 27 -72.46 -132.26
REMARK 500 ASP A 29 27.69 87.00
REMARK 500 GLU A 30 31.51 -90.07
REMARK 500 GLU A 39 -90.69 -42.69
REMARK 500 THR A 41 -32.24 -145.29
REMARK 500 GLU A 44 175.76 73.29
REMARK 500 LYS A 73 -48.11 107.24
REMARK 500 LEU A 80 106.49 -46.01
REMARK 500 LYS A 82 -68.05 -124.84
REMARK 500 GLU A 84 138.02 95.77
REMARK 500 VAL A 85 -122.27 -95.94
REMARK 500 GLU A 100 -154.28 -95.60
REMARK 500 ALA A 111 -120.00 -143.26
REMARK 500 LYS A 120 -20.21 -152.01
REMARK 500 PRO A 123 -0.02 -55.73
REMARK 500 PHE A 136 -90.49 -147.36
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 TYR A 110 0.13 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ROU RELATED DB: PDB
DBREF 1ROT A 1 147 UNP P27124 FKBP4_RABIT 3 147
SEQADV 1ROT ASP A 4 UNP P27124 INSERTION
SEQADV 1ROT ILE A 5 UNP P27124 INSERTION
SEQRES 1 A 149 GLU GLU MET ASP ILE LYS ALA ALA GLU SER GLY ALA GLN
SEQRES 2 A 149 SER ALA PRO LEU PRO LEU GLU GLY VAL ASP ILE SER PRO
SEQRES 3 A 149 LYS GLN ASP GLU GLY VAL LEU LYS VAL ILE LYS ARG GLU
SEQRES 4 A 149 GLY THR GLY THR GLU THR PRO MET ILE GLY ASP ARG VAL
SEQRES 5 A 149 PHE VAL HIS TYR THR GLY TRP LEU LEU ASP GLY THR LYS
SEQRES 6 A 149 PHE ASP SER SER LEU ASP ARG LYS ASP LYS PHE SER PHE
SEQRES 7 A 149 ASP LEU GLY LYS GLY GLU VAL ILE LYS ALA TRP ASP ILE
SEQRES 8 A 149 ALA VAL ALA THR MET LYS VAL GLY GLU LEU CYS ARG ILE
SEQRES 9 A 149 THR CYS LYS PRO GLU TYR ALA TYR GLY SER ALA GLY SER
SEQRES 10 A 149 PRO PRO LYS ILE PRO PRO ASN ALA THR LEU VAL PHE GLU
SEQRES 11 A 149 VAL GLU LEU PHE GLU PHE LYS GLY GLU ASP LEU THR ASP
SEQRES 12 A 149 ASP GLU ASP GLY VAL PRO
HELIX 1 1 LYS A 87 THR A 95 1 9
HELIX 2 2 PRO A 108 TYR A 110 5 3
SHEET 1 A1 6 VAL A 22 ILE A 24 0
SHEET 2 A1 6 VAL A 32 LYS A 37 -1 N VAL A 32 O ILE A 24
SHEET 3 A1 6 LEU A 101 LYS A 107 -1 N ARG A 103 O VAL A 35
SHEET 4 A1 6 LEU A 127 LYS A 137 -1 N LEU A 127 O CYS A 106
SHEET 5 A1 6 ASP A 50 LEU A 60 -1 O TRP A 59 N VAL A 128
SHEET 6 A1 6 THR A 64 SER A 68 -1 O THR A 64 N LEU A 60
SHEET 1 A2 6 VAL A 22 ILE A 24 0
SHEET 2 A2 6 VAL A 32 LYS A 37 -1 N VAL A 32 O ILE A 24
SHEET 3 A2 6 LEU A 101 LYS A 107 -1 N ARG A 103 O VAL A 35
SHEET 4 A2 6 LEU A 127 LYS A 137 -1 N LEU A 127 O CYS A 106
SHEET 5 A2 6 ASP A 50 LEU A 60 -1 O TRP A 59 N VAL A 128
SHEET 6 A2 6 PHE A 76 LEU A 80 -1 O PHE A 76 N VAL A 54
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 - 2 20 Bytes