Header list of 1ylb.pdb file
Complete list - 2 20 Bytes
HEADER ELECTRON TRANSPORT 19-JAN-05 1YLB
TITLE NMR SOLUTION STRUCTURE OF THE REDUCED SPINACH PLASTOCYANIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PLASTOCYANIN, CHLOROPLAST;
COMPND 3 CHAIN: B;
COMPND 4 FRAGMENT: REDUCED SPINACH PLASTOCYANIN (RESIDUES 70-168)
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SPINACIA OLERACEA;
SOURCE 3 ORGANISM_COMMON: SPINACH;
SOURCE 4 ORGANISM_TAXID: 3562
KEYWDS PLASTOCYANIN, COPPER(+)-CONTAINING, ELECTRON-TRANSFER, SPINACH,
KEYWDS 2 PHOTOSYNTHESIS, BLUE-COPPER PROTEIN, ELECTRON TRANSPORT
EXPDTA SOLUTION NMR
AUTHOR F.MUSIANI,A.DIKIY,A.Y.SEMENOV,S.CIURLI
REVDAT 4 02-MAR-22 1YLB 1 REMARK LINK
REVDAT 3 24-FEB-09 1YLB 1 VERSN
REVDAT 2 17-MAY-05 1YLB 1 JRNL
REVDAT 1 05-APR-05 1YLB 0
JRNL AUTH F.MUSIANI,A.DIKIY,A.Y.SEMENOV,S.CIURLI
JRNL TITL STRUCTURE OF THE INTERMOLECULAR COMPLEX BETWEEN PLASTOCYANIN
JRNL TITL 2 AND CYTOCHROME F FROM SPINACH.
JRNL REF J.BIOL.CHEM. V. 280 18833 2005
JRNL REFN ISSN 0021-9258
JRNL PMID 15691836
JRNL DOI 10.1074/JBC.M412760200
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH Y.XUE,M.OKVIST,O.HANSSON,S.YOUNG
REMARK 1 TITL CRYSTAL STRUCTURE OF SPINACH PLASTOCYANIN AT 1.7A RESOLUTION
REMARK 1 REF PROTEIN SCI. V. 7 2099 1998
REMARK 1 REFN ISSN 0961-8368
REMARK 1 PMID 9792096
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 1.3, AMBER 6.0
REMARK 3 AUTHORS : BRUKER (XWINNMR), CASE, D. A., PEARLMAN, D. A.,
REMARK 3 CALDWELL, J. W., CHEATHAM III, T. E., ROSS, W. S.,
REMARK 3 SIMMERLING, C. L., DARDEN, T. A., MERZ, K. M.,
REMARK 3 STANTON, R. V., CHENG, A. L., VINCENT, J. J.,
REMARK 3 CROWLEY, M., TSUI, V., RADMER, R. J., DUAN, Y.,
REMARK 3 PITERA, J., MASSOVA, I., SEIBEL, G. L., SINGH, U.
REMARK 3 C., WEINER, P. K., AND KOLLMAN, P. A. (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURE WAS CALCULATED USING
REMARK 3 DIPOLAR (NOESY) DERIVED CONSTRAINTS SUPPLEMENTED WITH PHI AND
REMARK 3 PSI DIHEDRAL ANGLE CONSTRAINTS AS WELL AS WITH HYDROGEN BOND
REMARK 3 CONSTRAINTS. THE MEAN STRUCTURE OF THE DYANA FAMILY WAS
REMARK 3 INITIALLY SUBJECTED TO RESTRAINED ENERGY MINIMIZATION IN VACUO
REMARK 3 AND SUBSEQUENTLY TO RESTRAINED MOLECULAR DYNAMICS IN EXPLICIT
REMARK 3 WATER MEDIUM. FOR FURTHER EXPERIMENTAL DETAILS PLEASE REFER TO
REMARK 3 THE PUBLICATION.
REMARK 4
REMARK 4 1YLB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-JAN-05.
REMARK 100 THE DEPOSITION ID IS D_1000031647.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 7.5
REMARK 210 IONIC STRENGTH : 50 MM SODIUM PHOSPHATE
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1-2 MM WILD TYPE REDUCED SPINACH
REMARK 210 PLASTOCYANIN, 50MM SODIUM
REMARK 210 PHOSPHATE BUFFER
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA 1.5, XEASY 1.3
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS +
REMARK 210 RESTRAINED ENERGY MINIMIZATION +
REMARK 210 RESTRAINED MOLECULAR DYNAMICS
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 : 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: B
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 PHE B 82 CG - CD1 - CE1 ANGL. DEV. = -7.4 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 ASP B 9 -39.91 69.17
REMARK 500 ASN B 32 -43.25 -138.34
REMARK 500 GLU B 76 115.53 78.28
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 B 14 0.08 SIDE CHAIN
REMARK 500 PHE B 19 0.09 SIDE CHAIN
REMARK 500 TYR B 80 0.13 SIDE CHAIN
REMARK 500 PHE B 82 0.24 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU1 B 100 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 37 ND1
REMARK 620 2 CYS B 84 SG 124.6
REMARK 620 3 HIS B 87 ND1 100.7 119.2
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 B 100
DBREF 1YLB B 1 99 UNP P00289 PLAS_SPIOL 70 168
SEQRES 1 B 99 VAL GLU VAL LEU LEU GLY GLY GLY ASP GLY SER LEU ALA
SEQRES 2 B 99 PHE LEU PRO GLY ASP PHE SER VAL ALA SER GLY GLU GLU
SEQRES 3 B 99 ILE VAL PHE LYS ASN ASN ALA GLY PHE PRO HIS ASN VAL
SEQRES 4 B 99 VAL PHE ASP GLU ASP GLU ILE PRO SER GLY VAL ASP ALA
SEQRES 5 B 99 ALA LYS ILE SER MET SER GLU GLU ASP LEU LEU ASN ALA
SEQRES 6 B 99 PRO GLY GLU THR TYR LYS VAL THR LEU THR GLU LYS GLY
SEQRES 7 B 99 THR TYR LYS PHE TYR CYS SER PRO HIS GLN GLY ALA GLY
SEQRES 8 B 99 MET VAL GLY LYS VAL THR VAL ASN
HET CU1 B 100 1
HETNAM CU1 COPPER (I) ION
FORMUL 2 CU1 CU 1+
HELIX 1 1 ASP B 51 ILE B 55 5 5
SHEET 1 A 4 PHE B 14 LEU B 15 0
SHEET 2 A 4 GLU B 2 LEU B 5 -1 N LEU B 4 O LEU B 15
SHEET 3 A 4 GLU B 26 ASN B 31 1 O LYS B 30 N LEU B 5
SHEET 4 A 4 THR B 69 THR B 73 -1 O VAL B 72 N ILE B 27
SHEET 1 B 3 VAL B 40 PHE B 41 0
SHEET 2 B 3 THR B 79 TYR B 83 -1 O TYR B 83 N VAL B 40
SHEET 3 B 3 VAL B 93 THR B 97 -1 O VAL B 96 N TYR B 80
LINK ND1 HIS B 37 CU CU1 B 100 1555 1555 2.07
LINK SG CYS B 84 CU CU1 B 100 1555 1555 2.12
LINK ND1 HIS B 87 CU CU1 B 100 1555 1555 2.09
CISPEP 1 LEU B 15 PRO B 16 0 -3.88
CISPEP 2 PHE B 35 PRO B 36 0 -3.61
SITE 1 AC1 3 HIS B 37 CYS B 84 HIS B 87
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