Header list of 3phy.pdb file
Complete list - r 16 2 Bytes
HEADER PHOTORECEPTOR 06-FEB-98 3PHY
TITLE PHOTOACTIVE YELLOW PROTEIN, DARK STATE (UNBLEACHED), SOLUTION
TITLE 2 STRUCTURE, NMR, 26 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOTOACTIVE YELLOW PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PYP
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HALORHODOSPIRA HALOPHILA;
SOURCE 3 ORGANISM_TAXID: 1053;
SOURCE 4 STRAIN: BN9626
KEYWDS PHOTORECEPTOR, LIGHT SENSOR FOR NEGATIVE PHOTOTAXIS
EXPDTA SOLUTION NMR
NUMMDL 26
AUTHOR P.DUX,G.RUBINSTENN,G.W.VUISTER,R.BOELENS,F.A.A.MULDER,K.HARD,
AUTHOR 2 W.D.HOFF,A.KROON,W.CRIELAARD,K.J.HELLINGWERF,R.KAPTEIN
REVDAT 3 16-MAR-22 3PHY 1 REMARK LINK
REVDAT 2 24-FEB-09 3PHY 1 VERSN
REVDAT 1 27-MAY-98 3PHY 0
JRNL AUTH P.DUX,G.RUBINSTENN,G.W.VUISTER,R.BOELENS,F.A.MULDER,K.HARD,
JRNL AUTH 2 W.D.HOFF,A.R.KROON,W.CRIELAARD,K.J.HELLINGWERF,R.KAPTEIN
JRNL TITL SOLUTION STRUCTURE AND BACKBONE DYNAMICS OF THE PHOTOACTIVE
JRNL TITL 2 YELLOW PROTEIN.
JRNL REF BIOCHEMISTRY V. 37 12689 1998
JRNL REFN ISSN 0006-2960
JRNL PMID 9737845
JRNL DOI 10.1021/BI9806652
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH W.D.HOFF,P.DUX,K.HARD,B.DEVREESE,I.M.NUGTEREN-ROODZANT,
REMARK 1 AUTH 2 W.CRIELAARD,R.BOELENS,R.KAPTEIN,J.VAN BEEUMEN,
REMARK 1 AUTH 3 K.J.HELLINGWERF
REMARK 1 TITL THIOL ESTER-LINKED P-COUMARIC ACID AS A NEW PHOTOACTIVE
REMARK 1 TITL 2 PROSTHETIC GROUP IN A PROTEIN WITH RHODOPSIN-LIKE
REMARK 1 TITL 3 PHOTOCHEMISTRY
REMARK 1 REF BIOCHEMISTRY V. 33 13959 1994
REMARK 1 REFN ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: TWO CONSTRAINT REFINEMENT STEPS OF 0.47
REMARK 3 AND 0.58 PS, RESPECTIVELY, WITH AN INITIAL TEMPERATURE OF 2000K,
REMARK 3 EXCLUDING ELECTROSTATIC INTERACTIONS, WERE DONE.
REMARK 4
REMARK 4 3PHY COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000179108.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 311
REMARK 210 PH : 5.8
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; TOCSY; COSY; HSQC-NOESY;
REMARK 210 HSQC-TOCSY; HNHA; HNHB
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : AMX600; AMX500; UNITY-PLUS500;
REMARK 210 UNITY-PLUS750
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR
REMARK 210 METHOD USED : DISTANCE GEOMETRY
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 40
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 26
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOW ENERGY
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 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HC4 A 126
DBREF 3PHY A 1 125 UNP P16113 PYP_ECTHA 1 125
SEQRES 1 A 125 MET GLU HIS VAL ALA PHE GLY SER GLU ASP ILE GLU ASN
SEQRES 2 A 125 THR LEU ALA LYS MET ASP ASP GLY GLN LEU ASP GLY LEU
SEQRES 3 A 125 ALA PHE GLY ALA ILE GLN LEU ASP GLY ASP GLY ASN ILE
SEQRES 4 A 125 LEU GLN TYR ASN ALA ALA GLU GLY ASP ILE THR GLY ARG
SEQRES 5 A 125 ASP PRO LYS GLN VAL ILE GLY LYS ASN PHE PHE LYS ASP
SEQRES 6 A 125 VAL ALA PRO CYS THR ASP SER PRO GLU PHE TYR GLY LYS
SEQRES 7 A 125 PHE LYS GLU GLY VAL ALA SER GLY ASN LEU ASN THR MET
SEQRES 8 A 125 PHE GLU TYR THR PHE ASP TYR GLN MET THR PRO THR LYS
SEQRES 9 A 125 VAL LYS VAL HIS MET LYS LYS ALA LEU SER GLY ASP SER
SEQRES 10 A 125 TYR TRP VAL PHE VAL LYS ARG VAL
HET HC4 A 126 17
HETNAM HC4 4'-HYDROXYCINNAMIC ACID
HETSYN HC4 PARA-COUMARIC ACID
FORMUL 2 HC4 C9 H8 O3
HELIX 1 A-1 ILE A 11 LEU A 15 1 5
HELIX 2 A-3 ASN A 43 THR A 50 1 8
HELIX 3 A-4 ASP A 53 ILE A 58 1 6
HELIX 4 A-5 PHE A 75 GLY A 86 1 12
SHEET 1 B-1 6 LYS A 60 PHE A 62 0
SHEET 2 B-1 6 ASN A 38 LEU A 40 -1
SHEET 3 B-1 6 ALA A 27 ASP A 34 -1
SHEET 4 B-1 6 TRP A 119 VAL A 125 -1
SHEET 5 B-1 6 THR A 103 LYS A 111 -1
SHEET 6 B-1 6 LEU A 88 PHE A 96 -1
LINK SG CYS A 69 C1 HC4 A 126 1555 1555 1.80
SITE 1 AC1 7 TYR A 42 THR A 50 ARG A 52 ALA A 67
SITE 2 AC1 7 CYS A 69 PHE A 96 TYR A 98
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
MODEL 1
Complete list - r 16 2 Bytes