Header list of 1fdf.pdb file
Complete list - 23 202 Bytes
HEADER SIGNALING PROTEIN 20-JUL-00 1FDF
TITLE HELIX 7 BOVINE RHODOPSIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RHODOPSIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: HELIX 7, RESIDUES 291-315;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: SOLID PHASE PEPTIDE SYNTHESIS
KEYWDS HELIX, SIGNALING PROTEIN
EXPDTA SOLUTION NMR
AUTHOR P.L.YEAGLE,C.DANIS,G.CHOI,J.L.ALDERFER,A.D.ALBERT
REVDAT 5 23-FEB-22 1FDF 1 REMARK
REVDAT 4 24-FEB-09 1FDF 1 VERSN
REVDAT 3 11-APR-01 1FDF 1 REMARK
REVDAT 2 30-AUG-00 1FDF 1 JRNL
REVDAT 1 27-JUL-00 1FDF 0
JRNL AUTH P.L.YEAGLE,C.DANIS,G.CHOI,J.L.ALDERFER,A.D.ALBERT
JRNL TITL THREE DIMENSIONAL STRUCTURE OF THE SEVENTH TRANSMEMBRANE
JRNL TITL 2 HELICAL DOMAIN OF THE G-PROTEIN RECEPTOR, RHODOPSIN.
JRNL REF MOL.VIS. V. 6 125 2000
JRNL REFN ESSN 1090-0535
JRNL PMID 10930473
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DIANA 1, DIANA 1
REMARK 3 AUTHORS : WUTHRICH (DIANA), WUTHRICH (DIANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1FDF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-JUL-00.
REMARK 100 THE DEPOSITION ID IS D_1000011498.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 7
REMARK 210 IONIC STRENGTH : 0
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : PEPTIDE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; DQF-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : DIANA
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 150
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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 TYR A 11 CB - CG - CD1 ANGL. DEV. = -8.2 DEGREES
REMARK 500 TYR A 16 CB - CG - CD1 ANGL. DEV. = -4.8 DEGREES
REMARK 500 PHE A 23 CB - CG - CD2 ANGL. DEV. = -6.4 DEGREES
REMARK 500 PHE A 23 CB - CG - CD1 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 ALA A 5 -77.32 -60.89
REMARK 500 LYS A 6 -65.67 -23.54
REMARK 500 VAL A 10 -37.88 -149.59
REMARK 500 TYR A 11 -37.74 86.53
REMARK 500 ASN A 12 172.91 82.97
REMARK 500 PRO A 13 49.85 -76.16
REMARK 500 VAL A 14 24.36 -148.48
REMARK 500 ASN A 20 -144.26 -80.56
REMARK 500 LYS A 21 35.66 33.18
REMARK 500 GLN A 22 88.74 52.15
REMARK 500 ARG A 24 77.40 35.09
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ALA A 9 VAL A 10 -139.78
REMARK 500 VAL A 14 ILE A 15 108.80
REMARK 500 MET A 19 ASN A 20 143.62
REMARK 500 ASN A 20 LYS A 21 -137.30
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 PHE A 3 0.08 SIDE CHAIN
REMARK 500 PHE A 4 0.06 SIDE CHAIN
REMARK 500 TYR A 11 0.08 SIDE CHAIN
REMARK 500 TYR A 16 0.15 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1EDS RELATED DB: PDB
REMARK 900 INTRADISKAL LOOP 1 OF BOVINE RHODOPSIN
REMARK 900 RELATED ID: 1EDV RELATED DB: PDB
REMARK 900 INTRADISKAL LOOP 2 OF BOVINE RHODOPSIN
REMARK 900 RELATED ID: 1EDW RELATED DB: PDB
REMARK 900 INTRADISKAL LOOP 3 OF BOVINE RHODOPSIN
REMARK 900 RELATED ID: 1EDX RELATED DB: PDB
REMARK 900 AMINO TERMINAL OF BOVINE RHODOPSIN
DBREF 1FDF A 1 25 UNP P02699 OPSD_BOVIN 291 315
SEQRES 1 A 25 PRO ALA PHE PHE ALA LYS THR SER ALA VAL TYR ASN PRO
SEQRES 2 A 25 VAL ILE TYR ILE MET MET ASN LYS GLN PHE ARG ASN
HELIX 1 1 ALA A 5 VAL A 10 1 6
HELIX 2 2 MET A 19 ASN A 25 1 7
CISPEP 1 ALA A 2 PHE A 3 0 5.00
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 - 23 202 Bytes