Header list of 9pcy.pdb file
Complete list - r 16 2 Bytes
HEADER ELECTRON TRANSPORT 18-MAR-91 9PCY
TITLE HIGH-RESOLUTION SOLUTION STRUCTURE OF REDUCED FRENCH BEAN PLASTOCYANIN
TITLE 2 AND COMPARISON WITH THE CRYSTAL STRUCTURE OF POPLAR PLASTOCYANIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PLASTOCYANIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PHASEOLUS VULGARIS;
SOURCE 3 ORGANISM_TAXID: 3885
KEYWDS ELECTRON TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 16
AUTHOR J.M.MOORE,C.A.LEPRE,G.P.GIPPERT,W.J.CHAZIN,D.A.CASE,P.E.WRIGHT
REVDAT 3 16-MAR-22 9PCY 1 REMARK LINK
REVDAT 2 24-FEB-09 9PCY 1 VERSN
REVDAT 1 31-OCT-93 9PCY 0
JRNL AUTH J.M.MOORE,C.A.LEPRE,G.P.GIPPERT,W.J.CHAZIN,D.A.CASE,
JRNL AUTH 2 P.E.WRIGHT
JRNL TITL HIGH-RESOLUTION SOLUTION STRUCTURE OF REDUCED FRENCH BEAN
JRNL TITL 2 PLASTOCYANIN AND COMPARISON WITH THE CRYSTAL STRUCTURE OF
JRNL TITL 3 POPLAR PLASTOCYANIN.
JRNL REF J.MOL.BIOL. V. 221 533 1991
JRNL REFN ISSN 0022-2836
JRNL PMID 1920431
JRNL DOI 10.1016/0022-2836(91)80071-2
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH G.P.GIPPERT,P.F.YIP,P.E.WRIGHT,D.A.CASE
REMARK 1 TITL COMPUTATIONAL METHODS FOR DETERMINING PROTEIN STRUCTURES
REMARK 1 TITL 2 FROM NMR DATA
REMARK 1 REF BIOCHEM.PHARM. V. 40 15 1990
REMARK 1 REFN ISSN 0006-2952
REMARK 1 REFERENCE 2
REMARK 1 AUTH J.M.MOORE,D.A.CASE,W.J.CHAZIN,G.P.GIPPERT,T.F.HAVEL,R.POWLS,
REMARK 1 AUTH 2 P.E.WRIGHT
REMARK 1 TITL THREE-DIMENSIONAL SOLUTION STRUCTURE OF PLASTOCYANIN FROM
REMARK 1 TITL 2 THE GREEN ALGA SCENEDESMUS OBLIQUUS
REMARK 1 REF SCIENCE V. 240 314 1988
REMARK 1 REFN ISSN 0036-8075
REMARK 1 REFERENCE 3
REMARK 1 AUTH W.J.CHAZIN,M.RANCE,P.E.WRIGHT
REMARK 1 TITL COMPLETE ASSIGNMENT OF THE 1H NUCLEAR MAGNETIC RESONANCE
REMARK 1 TITL 2 SPECTRUM OF FRENCH BEAN PLASTOCYANIN. APPLICATION OF AN
REMARK 1 TITL 3 INTEGRATED APPROACH TO SPIN SYSTEM IDENTIFICATION IN
REMARK 1 TITL 4 PROTEINS
REMARK 1 REF J.MOL.BIOL. V. 202 603 1988
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 4
REMARK 1 AUTH W.J.CHAZIN,P.E.WRIGHT
REMARK 1 TITL COMPLETE ASSIGNMENT OF THE 1H NUCLEAR MAGNETIC RESONANCE
REMARK 1 TITL 2 SPECTRUM OF FRENCH BEAN PLASTOCYANIN. SEQUENTIAL RESONANCE
REMARK 1 TITL 3 ASSIGNMENTS, SECONDARY STRUCTURE AND GLOBAL FOLD
REMARK 1 REF J.MOL.BIOL. V. 202 623 1988
REMARK 1 REFN ISSN 0022-2836
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : AMBER
REMARK 3 AUTHORS : HAVEL,WUTHRICH (DISGEO),
REMARK 3 PEARLMAN,CASE,CALDWELL,SIEBEL,SINGH,WEINER,KOLLMAN
REMARK 3 (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 9PCY 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_1000180070.
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 : 16
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: 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 1 SER A 7 42.86 -82.87
REMARK 500 1 ASP A 9 36.27 -73.10
REMARK 500 1 SER A 17 -60.42 -103.14
REMARK 500 1 ASN A 31 99.60 -67.72
REMARK 500 2 ASN A 32 -72.96 -87.34
REMARK 500 2 PRO A 47 109.50 -53.62
REMARK 500 2 ALA A 48 106.42 -52.28
REMARK 500 2 ASP A 51 109.11 -59.11
REMARK 500 3 ALA A 48 108.37 -51.50
REMARK 500 4 ASN A 32 -69.72 -97.44
REMARK 500 4 GLU A 43 -36.68 -37.61
REMARK 500 4 GLU A 45 57.58 -93.32
REMARK 500 4 PRO A 47 108.15 -57.85
REMARK 500 4 PRO A 58 107.31 -48.97
REMARK 500 4 PRO A 86 -19.49 -46.29
REMARK 500 5 ASN A 32 -72.08 -84.33
REMARK 500 5 ALA A 33 -53.54 -146.24
REMARK 500 5 PRO A 58 99.28 -33.54
REMARK 500 5 GLU A 68 122.82 -38.33
REMARK 500 6 ASP A 9 34.37 -73.72
REMARK 500 6 ASN A 31 93.51 -67.70
REMARK 500 6 ALA A 48 107.88 -52.88
REMARK 500 6 GLU A 68 111.07 -18.53
REMARK 500 7 ASP A 9 42.97 -78.31
REMARK 500 7 SER A 11 106.27 -40.44
REMARK 500 7 ASN A 32 -69.93 -94.05
REMARK 500 7 PRO A 47 108.98 -58.67
REMARK 500 7 PRO A 58 107.37 -38.47
REMARK 500 8 PRO A 47 104.81 -58.88
REMARK 500 8 GLU A 59 -37.05 -38.86
REMARK 500 8 GLU A 68 118.41 -26.24
REMARK 500 8 ASP A 75 -63.22 -92.35
REMARK 500 9 SER A 7 43.88 -83.00
REMARK 500 9 ASP A 9 34.47 -72.85
REMARK 500 9 ASN A 32 -64.74 -102.59
REMARK 500 9 GLU A 59 68.86 -69.06
REMARK 500 9 GLU A 60 -47.96 -167.08
REMARK 500 9 ASN A 64 -46.12 -138.77
REMARK 500 10 ASN A 31 93.82 -67.01
REMARK 500 10 ASN A 32 -75.77 -85.39
REMARK 500 10 GLU A 45 59.36 -118.91
REMARK 500 10 GLU A 68 123.91 -39.86
REMARK 500 11 ASN A 32 -61.84 -92.38
REMARK 500 11 ASP A 44 -64.79 -161.70
REMARK 500 12 SER A 7 47.87 -82.78
REMARK 500 12 ASP A 9 38.07 -72.10
REMARK 500 12 SER A 17 -62.86 -92.61
REMARK 500 12 ALA A 48 107.33 -54.34
REMARK 500 12 ASP A 51 108.15 -57.99
REMARK 500 12 GLU A 59 -48.89 -28.76
REMARK 500
REMARK 500 THIS ENTRY HAS 70 RAMACHANDRAN OUTLIERS.
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 1 TYR A 80 0.10 SIDE CHAIN
REMARK 500 2 TYR A 70 0.07 SIDE CHAIN
REMARK 500 2 TYR A 80 0.09 SIDE CHAIN
REMARK 500 3 TYR A 80 0.07 SIDE CHAIN
REMARK 500 4 TYR A 80 0.11 SIDE CHAIN
REMARK 500 5 TYR A 80 0.11 SIDE CHAIN
REMARK 500 6 TYR A 80 0.10 SIDE CHAIN
REMARK 500 7 TYR A 70 0.08 SIDE CHAIN
REMARK 500 7 TYR A 80 0.10 SIDE CHAIN
REMARK 500 8 TYR A 80 0.14 SIDE CHAIN
REMARK 500 9 TYR A 80 0.11 SIDE CHAIN
REMARK 500 10 TYR A 80 0.09 SIDE CHAIN
REMARK 500 11 TYR A 70 0.07 SIDE CHAIN
REMARK 500 11 TYR A 80 0.11 SIDE CHAIN
REMARK 500 12 TYR A 70 0.08 SIDE CHAIN
REMARK 500 12 TYR A 80 0.11 SIDE CHAIN
REMARK 500 13 TYR A 80 0.12 SIDE CHAIN
REMARK 500 14 PHE A 14 0.08 SIDE CHAIN
REMARK 500 14 TYR A 80 0.12 SIDE CHAIN
REMARK 500 15 TYR A 80 0.09 SIDE CHAIN
REMARK 500 16 TYR A 80 0.11 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 CU A 100 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 37 ND1
REMARK 620 2 CYS A 84 SG 121.0
REMARK 620 3 HIS A 87 ND1 119.2 114.1
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 CU A 100
DBREF 9PCY A 1 99 UNP P00287 PLAS_PHAVU 1 99
SEQRES 1 A 99 LEU GLU VAL LEU LEU GLY SER GLY ASP GLY SER LEU VAL
SEQRES 2 A 99 PHE VAL PRO SER GLU PHE SER VAL PRO SER GLY GLU LYS
SEQRES 3 A 99 ILE VAL PHE LYS ASN ASN ALA GLY PHE PRO HIS ASN VAL
SEQRES 4 A 99 VAL PHE ASP GLU ASP GLU ILE PRO ALA GLY VAL ASP ALA
SEQRES 5 A 99 VAL LYS ILE SER MET PRO GLU GLU GLU LEU LEU ASN ALA
SEQRES 6 A 99 PRO GLY GLU THR TYR VAL VAL THR LEU ASP THR LYS GLY
SEQRES 7 A 99 THR TYR SER PHE TYR CYS SER PRO HIS GLN GLY ALA GLY
SEQRES 8 A 99 MET VAL GLY LYS VAL THR VAL ASN
HET CU A 100 1
HETNAM CU COPPER (II) ION
FORMUL 2 CU CU 2+
HELIX 1 1 ASP A 51 ILE A 55 5 5
HELIX 2 2 SER A 85 GLN A 88 5 4
SHEET 1 A 4 PHE A 14 VAL A 15 0
SHEET 2 A 4 GLU A 2 LEU A 5 -1 N LEU A 4 O VAL A 15
SHEET 3 A 4 GLU A 25 ASN A 31 1 O VAL A 28 N VAL A 3
SHEET 4 A 4 THR A 69 LEU A 74 -1 O TYR A 70 N PHE A 29
SHEET 1 B 4 GLU A 18 PRO A 22 0
SHEET 2 B 4 VAL A 93 ASN A 99 1 O LYS A 95 N PHE A 19
SHEET 3 B 4 GLY A 78 TYR A 83 -1 O GLY A 78 N VAL A 98
SHEET 4 B 4 VAL A 40 PHE A 41 -1 N VAL A 40 O TYR A 83
LINK ND1 HIS A 37 CU CU A 100 1555 1555 2.03
LINK SG CYS A 84 CU CU A 100 1555 1555 2.13
LINK ND1 HIS A 87 CU CU A 100 1555 1555 2.06
CISPEP 1 VAL A 15 PRO A 16 1 -1.37
CISPEP 2 PHE A 35 PRO A 36 1 4.21
CISPEP 3 VAL A 15 PRO A 16 2 -1.48
CISPEP 4 PHE A 35 PRO A 36 2 3.73
CISPEP 5 VAL A 15 PRO A 16 3 -1.57
CISPEP 6 PHE A 35 PRO A 36 3 4.72
CISPEP 7 VAL A 15 PRO A 16 4 -0.81
CISPEP 8 PHE A 35 PRO A 36 4 4.34
CISPEP 9 VAL A 15 PRO A 16 5 -1.36
CISPEP 10 PHE A 35 PRO A 36 5 2.45
CISPEP 11 VAL A 15 PRO A 16 6 -1.37
CISPEP 12 PHE A 35 PRO A 36 6 4.85
CISPEP 13 VAL A 15 PRO A 16 7 -0.45
CISPEP 14 PHE A 35 PRO A 36 7 3.71
CISPEP 15 VAL A 15 PRO A 16 8 -1.45
CISPEP 16 PHE A 35 PRO A 36 8 1.57
CISPEP 17 VAL A 15 PRO A 16 9 -0.77
CISPEP 18 PHE A 35 PRO A 36 9 2.88
CISPEP 19 VAL A 15 PRO A 16 10 -0.79
CISPEP 20 PHE A 35 PRO A 36 10 4.25
CISPEP 21 VAL A 15 PRO A 16 11 -1.02
CISPEP 22 PHE A 35 PRO A 36 11 2.64
CISPEP 23 VAL A 15 PRO A 16 12 -1.62
CISPEP 24 PHE A 35 PRO A 36 12 5.16
CISPEP 25 VAL A 15 PRO A 16 13 -1.33
CISPEP 26 PHE A 35 PRO A 36 13 2.19
CISPEP 27 VAL A 15 PRO A 16 14 -1.07
CISPEP 28 PHE A 35 PRO A 36 14 1.07
CISPEP 29 VAL A 15 PRO A 16 15 -1.41
CISPEP 30 PHE A 35 PRO A 36 15 1.60
CISPEP 31 VAL A 15 PRO A 16 16 -1.30
CISPEP 32 PHE A 35 PRO A 36 16 3.95
SITE 1 AC1 5 PRO A 36 HIS A 37 CYS A 84 HIS A 87
SITE 2 AC1 5 MET A 92
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