HEADER ELECTRON TRANSPORT (HEME PROTEIN) 06-MAR-96 1CED
TITLE THE STRUCTURE OF CYTOCHROME C6 FROM MONORAPHIDIUM BRAUNII, NMR,
TITLE 2 MINIMIZED AVERAGE STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME C6;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CYTOCHROME C552;
COMPND 5 OTHER_DETAILS: REDUCED
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MONORAPHIDIUM BRAUNII;
SOURCE 3 ORGANISM_TAXID: 34112
KEYWDS ELECTRON TRANSPORT, HEME PROTEIN, CHLOROPLAST, THYLAKOID MEMBRANE,
KEYWDS 2 ELECTRON TRANSPORT (HEME PROTEIN)
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR L.BANCI,I.BERTINI,G.QUACQUARINI,O.WALTER,A.DIAZ,M.HERVAS,M.A.DE LA
AUTHOR 2 ROSA
REVDAT 3 16-FEB-22 1CED 1 REMARK LINK
REVDAT 2 24-FEB-09 1CED 1 VERSN
REVDAT 1 17-AUG-96 1CED 0
JRNL AUTH L.BANCI,I.BERTINI,G.QUACQUARINI,O.WALTER,A.DIAZ,M.HERVAS,
JRNL AUTH 2 M.A.DE LA ROSA
JRNL TITL THE SOLUTION STRUCTURE OF CYTOCHROME C6 FROM THE GREEN ALGA
JRNL TITL 2 MONORAPHIDIUM BRAUNII
JRNL REF J.BIOL.INORG.CHEM. V. 1 330 1996
JRNL REFN ISSN 0949-8257
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.FRAZAO,C.M.SOARES,M.A.CARRONDO,E.POHL,Z.DAUTER,K.S.WILSON,
REMARK 1 AUTH 2 M.HERVAS,J.A.NAVARRO,M.A.DE LA ROSA,G.M.SHELDRICK
REMARK 1 TITL AB INITIO DETERMINATION OF THE CRYSTAL STRUCTURE OF
REMARK 1 TITL 2 CYTOCHROME C6 AND COMPARISON WITH PLASTOCYANIN
REMARK 1 REF STRUCTURE V. 3 1159 1995
REMARK 1 REFN ISSN 0969-2126
REMARK 1 REFERENCE 2
REMARK 1 AUTH A.P.CAMPOS,A.P.AGUIAR,M.HERVAS,M.REGALLA,J.A.NAVARRO,
REMARK 1 AUTH 2 J.M.ORTEGA,A.V.XAVIER,M.A.DE LA ROSA,M.TEIXEIRA
REMARK 1 TITL CYTOCHROME C6 FROM MONORAPHIDIUM BRAUNII. A CYTOCHROME WITH
REMARK 1 TITL 2 AN UNUSUAL HEME AXIAL COORDINATION
REMARK 1 REF EUR.J.BIOCHEM. V. 216 329 1993
REMARK 1 REFN ISSN 0014-2956
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : AMBER 4.0
REMARK 3 AUTHORS : PEARLMAN,CASE,CALDWELL,SIEBEL,SINGH,
REMARK 3 WEINER,KOLLMAN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1CED 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_1000172273.
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 : 20
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: 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 2 ARG A 67 CD - NE - CZ ANGL. DEV. = 8.4 DEGREES
REMARK 500 16 ARG A 67 CD - NE - CZ ANGL. DEV. = 8.4 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 1 ALA A 20 -82.25 3.98
REMARK 500 1 LEU A 32 35.58 -77.79
REMARK 500 1 LEU A 41 97.75 -63.27
REMARK 500 1 ASP A 42 -70.93 -7.24
REMARK 500 2 ALA A 20 125.90 -39.83
REMARK 500 2 LEU A 32 37.16 -76.44
REMARK 500 2 ASP A 42 -61.59 -29.64
REMARK 500 2 ASN A 46 153.06 175.46
REMARK 500 2 ASN A 56 60.47 -108.74
REMARK 500 2 ALA A 63 159.27 63.74
REMARK 500 2 LYS A 88 33.56 -98.49
REMARK 500 3 VAL A 26 -63.12 -104.48
REMARK 500 3 LEU A 32 44.16 -79.08
REMARK 500 3 GLU A 55 -74.32 -54.86
REMARK 500 3 ALA A 60 38.70 36.09
REMARK 500 4 ALA A 20 -118.69 44.61
REMARK 500 4 LEU A 41 105.27 -58.50
REMARK 500 4 ASP A 42 -70.59 -9.69
REMARK 500 4 GLU A 55 -70.72 -57.72
REMARK 500 4 LYS A 58 -151.40 -125.01
REMARK 500 4 ALA A 60 38.88 38.82
REMARK 500 4 ASN A 87 71.92 29.46
REMARK 500 5 ASN A 24 109.21 -43.54
REMARK 500 5 HIS A 30 41.96 -84.31
REMARK 500 5 LEU A 32 28.17 -78.13
REMARK 500 5 LEU A 41 88.63 -69.92
REMARK 500 5 ASP A 42 -68.37 -9.28
REMARK 500 6 ALA A 2 -137.77 -70.12
REMARK 500 6 ALA A 20 120.92 -28.24
REMARK 500 6 ASN A 24 101.55 -47.05
REMARK 500 6 HIS A 30 43.25 -85.08
REMARK 500 6 LEU A 32 28.82 -77.90
REMARK 500 6 ASP A 42 -68.10 -24.95
REMARK 500 6 ASN A 87 54.31 24.88
REMARK 500 7 ALA A 20 -84.58 6.49
REMARK 500 7 ASN A 24 92.78 -52.25
REMARK 500 7 LEU A 32 37.93 -76.72
REMARK 500 7 LYS A 34 -68.58 -29.04
REMARK 500 7 ALA A 60 46.48 33.14
REMARK 500 7 ASN A 87 56.74 38.16
REMARK 500 8 ALA A 20 -82.86 5.32
REMARK 500 8 ASN A 24 107.37 -48.40
REMARK 500 8 LEU A 32 44.83 -79.19
REMARK 500 8 ASP A 42 65.79 -66.83
REMARK 500 8 GLU A 55 -75.79 -56.41
REMARK 500 9 ASN A 24 105.35 -40.33
REMARK 500 9 GLU A 55 -74.53 -54.74
REMARK 500 9 ALA A 63 141.29 70.30
REMARK 500 9 LYS A 88 38.68 -91.59
REMARK 500 10 ASN A 24 103.52 -43.07
REMARK 500
REMARK 500 THIS ENTRY HAS 112 RAMACHANDRAN OUTLIERS.
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 LEU A 41 ASP A 42 1 147.75
REMARK 500 GLY A 86 ASN A 87 4 -147.06
REMARK 500 LEU A 41 ASP A 42 15 147.75
REMARK 500 GLY A 86 ASN A 87 18 -147.06
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 ARG A 67 0.17 SIDE CHAIN
REMARK 500 2 TYR A 79 0.07 SIDE CHAIN
REMARK 500 4 ARG A 67 0.18 SIDE CHAIN
REMARK 500 5 TYR A 79 0.07 SIDE CHAIN
REMARK 500 5 TYR A 81 0.06 SIDE CHAIN
REMARK 500 6 PHE A 45 0.10 SIDE CHAIN
REMARK 500 6 ARG A 67 0.18 SIDE CHAIN
REMARK 500 6 TYR A 79 0.09 SIDE CHAIN
REMARK 500 7 ARG A 67 0.18 SIDE CHAIN
REMARK 500 9 TYR A 52 0.11 SIDE CHAIN
REMARK 500 9 ARG A 67 0.21 SIDE CHAIN
REMARK 500 10 TYR A 79 0.07 SIDE CHAIN
REMARK 500 13 ARG A 67 0.19 SIDE CHAIN
REMARK 500 13 TYR A 79 0.08 SIDE CHAIN
REMARK 500 14 ARG A 67 0.19 SIDE CHAIN
REMARK 500 15 ARG A 67 0.17 SIDE CHAIN
REMARK 500 16 TYR A 79 0.07 SIDE CHAIN
REMARK 500 18 ARG A 67 0.18 SIDE CHAIN
REMARK 500 19 TYR A 52 0.06 SIDE CHAIN
REMARK 500 19 TYR A 79 0.07 SIDE CHAIN
REMARK 500 20 TYR A 79 0.07 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 HEM A 90 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 19 NE2
REMARK 620 2 HEM A 90 NA 95.6
REMARK 620 3 HEM A 90 NB 91.6 91.5
REMARK 620 4 HEM A 90 NC 87.9 176.0 90.3
REMARK 620 5 HEM A 90 ND 89.7 89.5 178.2 88.6
REMARK 620 6 MET A 61 SD 170.1 81.7 98.0 94.5 80.7
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 90
DBREF 1CED A 1 89 UNP Q09099 CYC6_MONBR 1 89
SEQRES 1 A 89 GLU ALA ASP LEU ALA LEU GLY LYS ALA VAL PHE ASP GLY
SEQRES 2 A 89 ASN CYS ALA ALA CYS HIS ALA GLY GLY GLY ASN ASN VAL
SEQRES 3 A 89 ILE PRO ASP HIS THR LEU GLN LYS ALA ALA ILE GLU GLN
SEQRES 4 A 89 PHE LEU ASP GLY GLY PHE ASN ILE GLU ALA ILE VAL TYR
SEQRES 5 A 89 GLN ILE GLU ASN GLY LYS GLY ALA MET PRO ALA TRP ASP
SEQRES 6 A 89 GLY ARG LEU ASP GLU ASP GLU ILE ALA GLY VAL ALA ALA
SEQRES 7 A 89 TYR VAL TYR ASP GLN ALA ALA GLY ASN LYS TRP
HET HEM A 90 43
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETSYN HEM HEME
FORMUL 2 HEM C34 H32 FE N4 O4
HELIX 1 1 LEU A 4 ASN A 14 1 11
HELIX 2 2 ALA A 16 HIS A 19 1 4
HELIX 3 3 LYS A 34 PHE A 40 1 7
HELIX 4 4 ILE A 47 ASN A 56 1 10
HELIX 5 5 GLU A 70 GLY A 86 1 17
LINK SG CYS A 15 CAB HEM A 90 1555 1555 1.81
LINK SG CYS A 18 CAC HEM A 90 1555 1555 1.82
LINK NE2 HIS A 19 FE HEM A 90 1555 1555 1.95
LINK SD MET A 61 FE HEM A 90 1555 1555 2.37
SITE 1 AC1 17 CYS A 15 CYS A 18 HIS A 19 ASN A 24
SITE 2 AC1 17 HIS A 30 THR A 31 LEU A 32 ALA A 36
SITE 3 AC1 17 ILE A 37 LEU A 41 ILE A 50 GLN A 53
SITE 4 AC1 17 ILE A 54 LYS A 58 MET A 61 PRO A 62
SITE 5 AC1 17 TRP A 64
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
(ATOM LINES ARE NOT SHOWN.)
END
