Header list of 1c6s.pdb file
Complete list - b 16 2 Bytes
HEADER ELECTRON TRANSPORT 31-MAR-97 1C6S
TITLE THE SOLUTION STRUCTURE OF CYTOCHROME C6 FROM THE THERMOPHILIC
TITLE 2 CYANOBACTERIUM SYNECHOCOCCUS ELONGATUS, NMR, 20 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME C6;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CYTOCHROME C553;
COMPND 5 OTHER_DETAILS: REDUCED
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SYNECHOCOCCUS ELONGATUS;
SOURCE 3 ORGANISM_TAXID: 32046
KEYWDS CYTOCHROME C6, ELECTRON TRANSPORT, PHOTOSYNTHESIS, SYNECHOCOCCUS
KEYWDS 2 ELONGATUS
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR P.ROESCH,M.BEISSINGER,H.STICHT,M.SUTTER,A.EJCHART,W.HAEHNEL
REVDAT 3 16-FEB-22 1C6S 1 REMARK LINK
REVDAT 2 24-FEB-09 1C6S 1 VERSN
REVDAT 1 08-APR-98 1C6S 0
JRNL AUTH M.BEISSINGER,H.STICHT,M.SUTTER,A.EJCHART,W.HAEHNEL,P.ROSCH
JRNL TITL SOLUTION STRUCTURE OF CYTOCHROME C6 FROM THE THERMOPHILIC
JRNL TITL 2 CYANOBACTERIUM SYNECHOCOCCUS ELONGATUS.
JRNL REF EMBO J. V. 17 27 1998
JRNL REFN ISSN 0261-4189
JRNL PMID 9427738
JRNL DOI 10.1093/EMBOJ/17.1.27
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.SUTTER,H.STICHT,R.SCHMID,P.HOERTH,P.ROESCH,W.HAEHNEL
REMARK 1 TITL CYTOCHROME C6 FROM THE THERMOPHILIC SYNECHOCOCCUS ELONGATUS
REMARK 1 EDIT P.MATHIS
REMARK 1 REF PHOTOSYNTHESIS : FROM LIGHT V. 2 563 1995
REMARK 1 REF 2 TO BIOSPHERE : PROCEEDINGS
REMARK 1 REF 3 OF THE XTH INTERNATIONAL
REMARK 1 REF 4 PHOTOSYNTHESIS CONGRESS,
REMARK 1 REF 5 MONTPELLIER, FRANCE, 20-25
REMARK 1 REF 6 AUGUST 1995
REMARK 1 PUBL DORDRECHT : KLUWER ACADEMIC PUBLISHERS
REMARK 1 REFN ISSN 0-7923-3862-6
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: NULL
REMARK 4
REMARK 4 1C6S 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_1000172173.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.5
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 : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AMX600
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NDEE, X-PLOR
REMARK 210 METHOD USED : SIMULATED ANNEALING, RESTRAINED
REMARK 210 MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : ENERGY, AGREEMENT WITH
REMARK 210 EXPERIMENTAL DATA
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 7 TYR A 76 CB - CG - CD2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 18 TYR A 76 CB - CG - CD2 ANGL. DEV. = -3.8 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 ASN A 13 -57.83 -154.82
REMARK 500 1 HIS A 18 -69.63 -157.07
REMARK 500 1 MET A 19 102.59 36.24
REMARK 500 1 ASN A 28 -62.95 -176.58
REMARK 500 1 LYS A 29 97.00 -55.18
REMARK 500 1 THR A 30 -167.40 -111.10
REMARK 500 1 LYS A 32 -89.75 -45.22
REMARK 500 1 LYS A 33 -26.02 -178.74
REMARK 500 1 MET A 41 29.95 158.57
REMARK 500 1 ALA A 46 -76.61 -66.06
REMARK 500 1 HIS A 53 26.77 -161.99
REMARK 500 1 LYS A 55 126.67 160.86
REMARK 500 1 ASN A 56 -81.66 68.98
REMARK 500 1 ALA A 60 165.50 -40.23
REMARK 500 1 PHE A 61 15.59 -146.76
REMARK 500 1 LEU A 65 -140.71 -82.00
REMARK 500 1 ASP A 67 -54.92 153.34
REMARK 500 1 GLN A 71 -65.76 -97.48
REMARK 500 1 LYS A 83 39.51 -170.59
REMARK 500 1 TRP A 85 83.78 -40.30
REMARK 500 1 ALA A 86 24.30 46.43
REMARK 500 2 CYS A 17 19.04 -140.64
REMARK 500 2 HIS A 18 -53.30 -158.31
REMARK 500 2 MET A 19 98.67 35.58
REMARK 500 2 ASN A 23 157.53 -40.72
REMARK 500 2 VAL A 25 -68.61 -109.73
REMARK 500 2 ASN A 28 -46.55 178.09
REMARK 500 2 LYS A 32 179.65 -59.72
REMARK 500 2 ALA A 46 -71.63 -57.65
REMARK 500 2 HIS A 53 32.42 -164.38
REMARK 500 2 LYS A 55 128.93 157.90
REMARK 500 2 ASN A 56 -86.97 62.95
REMARK 500 2 ALA A 62 39.01 27.53
REMARK 500 2 THR A 66 179.28 -43.70
REMARK 500 2 GLN A 71 -69.87 -97.31
REMARK 500 2 LYS A 83 30.56 -150.03
REMARK 500 2 TRP A 85 84.34 -40.79
REMARK 500 2 ALA A 86 23.57 47.38
REMARK 500 3 ASN A 13 -53.16 -153.97
REMARK 500 3 HIS A 18 -66.50 -158.67
REMARK 500 3 MET A 19 98.91 39.48
REMARK 500 3 LYS A 32 173.53 -46.01
REMARK 500 3 MET A 41 25.12 -159.16
REMARK 500 3 ALA A 46 -73.94 -69.65
REMARK 500 3 HIS A 53 13.60 -147.35
REMARK 500 3 LYS A 55 127.48 155.17
REMARK 500 3 ASN A 56 -88.31 61.00
REMARK 500 3 ALA A 60 158.50 -37.54
REMARK 500 3 LEU A 65 -157.42 -66.52
REMARK 500 3 ASP A 67 -53.88 153.72
REMARK 500
REMARK 500 THIS ENTRY HAS 395 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 ARG A 64 0.32 SIDE CHAIN
REMARK 500 2 ARG A 64 0.28 SIDE CHAIN
REMARK 500 3 ARG A 64 0.30 SIDE CHAIN
REMARK 500 4 ARG A 64 0.28 SIDE CHAIN
REMARK 500 5 ARG A 64 0.28 SIDE CHAIN
REMARK 500 6 ARG A 64 0.20 SIDE CHAIN
REMARK 500 7 ARG A 64 0.29 SIDE CHAIN
REMARK 500 8 ARG A 64 0.30 SIDE CHAIN
REMARK 500 9 ARG A 64 0.23 SIDE CHAIN
REMARK 500 10 ARG A 64 0.29 SIDE CHAIN
REMARK 500 11 ARG A 64 0.16 SIDE CHAIN
REMARK 500 12 ARG A 64 0.24 SIDE CHAIN
REMARK 500 13 ARG A 64 0.31 SIDE CHAIN
REMARK 500 14 ARG A 64 0.32 SIDE CHAIN
REMARK 500 15 ARG A 64 0.23 SIDE CHAIN
REMARK 500 16 ARG A 64 0.12 SIDE CHAIN
REMARK 500 17 ARG A 64 0.19 SIDE CHAIN
REMARK 500 19 ARG A 64 0.32 SIDE CHAIN
REMARK 500 20 ARG A 64 0.32 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 HEC A 88 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 18 NE2
REMARK 620 2 HEC A 88 NA 87.4
REMARK 620 3 HEC A 88 NB 76.5 90.2
REMARK 620 4 HEC A 88 NC 92.0 179.3 90.0
REMARK 620 5 HEC A 88 ND 103.0 90.1 179.4 89.7
REMARK 620 6 MET A 58 SD 154.7 89.4 78.4 91.3 102.1
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 HEC A 88
DBREF 1C6S A 1 87 UNP P0A3Y0 CYC6_SYNEN 1 87
SEQRES 1 A 87 ALA ASP LEU ALA ASN GLY ALA LYS VAL PHE SER GLY ASN
SEQRES 2 A 87 CYS ALA ALA CYS HIS MET GLY GLY GLY ASN VAL VAL MET
SEQRES 3 A 87 ALA ASN LYS THR LEU LYS LYS GLU ALA LEU GLU GLN PHE
SEQRES 4 A 87 GLY MET TYR SER GLU ASP ALA ILE ILE TYR GLN VAL GLN
SEQRES 5 A 87 HIS GLY LYS ASN ALA MET PRO ALA PHE ALA GLY ARG LEU
SEQRES 6 A 87 THR ASP GLU GLN ILE GLN ASP VAL ALA ALA TYR VAL LEU
SEQRES 7 A 87 ASP GLN ALA ALA LYS GLY TRP ALA GLY
HET HEC A 88 75
HETNAM HEC HEME C
FORMUL 2 HEC C34 H34 FE N4 O4
HELIX 1 1 LEU A 3 PHE A 10 1 8
HELIX 2 2 CYS A 14 CYS A 17 5 4
HELIX 3 3 GLU A 44 VAL A 51 1 8
HELIX 4 4 GLU A 68 GLN A 80 1 13
LINK SG CYS A 14 CAB HEC A 88 1555 1555 1.80
LINK SG CYS A 17 CAC HEC A 88 1555 1555 1.81
LINK NE2 HIS A 18 FE HEC A 88 1555 1555 2.29
LINK SD MET A 58 FE HEC A 88 1555 1555 2.78
SITE 1 AC1 19 CYS A 14 CYS A 17 HIS A 18 ASN A 23
SITE 2 AC1 19 VAL A 25 LYS A 29 LEU A 31 PHE A 39
SITE 3 AC1 19 MET A 41 ILE A 47 GLN A 50 VAL A 51
SITE 4 AC1 19 LYS A 55 ASN A 56 ALA A 57 MET A 58
SITE 5 AC1 19 PRO A 59 PHE A 61 LEU A 65
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 - b 16 2 Bytes