Header list of 1gks.pdb file
Complete list - b 23 2 Bytes
HEADER ELECTRON TRANSPORT 16-JUL-96 1GKS
TITLE ECTOTHIORHODOSPIRA HALOPHILA CYTOCHROME C551 (REDUCED), NMR, 37
TITLE 2 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME C551;
COMPND 3 CHAIN: A
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HALORHODOSPIRA HALOPHILA;
SOURCE 3 ORGANISM_TAXID: 1053;
SOURCE 4 STRAIN: BN9626;
SOURCE 5 CELLULAR_LOCATION: PERIPLASM
KEYWDS BACTERIAL CYTOCHROME C, HALOPHILIC PURPLE PHOTOTROPHIC BACTERIUM,
KEYWDS 2 ELECTRON TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 37
AUTHOR B.BERSCH,M.J.BLACKLEDGE,T.E.MEYER,D.MARION
REVDAT 4 23-FEB-22 1GKS 1 REMARK LINK
REVDAT 3 24-FEB-09 1GKS 1 VERSN
REVDAT 2 01-APR-03 1GKS 1 JRNL
REVDAT 1 27-JAN-97 1GKS 0
JRNL AUTH B.BERSCH,M.J.BLACKLEDGE,T.E.MEYER,D.MARION
JRNL TITL ECTOTHIORHODOSPIRA HALOPHILA FERROCYTOCHROME C551: SOLUTION
JRNL TITL 2 STRUCTURE AND COMPARISON WITH BACTERIAL CYTOCHROMES C.
JRNL REF J.MOL.BIOL. V. 264 567 1996
JRNL REFN ISSN 0022-2836
JRNL PMID 8969306
JRNL DOI 10.1006/JMBI.1996.0662
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH B.BERSCH,B.BRUTSCHER,T.E.MEYER,D.MARION
REMARK 1 TITL 1H AND 13C NMR ASSIGNMENTS AND STRUCTURAL ASPECTS OF A
REMARK 1 TITL 2 FERROCYTOCHROME C-551 FROM THE PURPLE PHOTOTROPHIC BACTERIUM
REMARK 1 TITL 3 ECTOTHIORHODOSPIRA HALOPHILA
REMARK 1 REF EUR.J.BIOCHEM. V. 227 249 1995
REMARK 1 REFN ISSN 0014-2956
REMARK 1 REFERENCE 2
REMARK 1 AUTH R.P.AMBLER,T.E.MEYER,M.D.KAMEN
REMARK 1 TITL AMINO ACID SEQUENCES OF CYTOCHROMES C-551 FROM THE
REMARK 1 TITL 2 HALOPHILIC PURPLE PHOTOTROPHIC BACTERIA, ECTOTHIORHODOSPIRA
REMARK 1 TITL 3 HALOPHILA AND E. HALOCHLORIS
REMARK 1 REF ARCH.BIOCHEM.BIOPHYS. V. 306 83 1993
REMARK 1 REFN ISSN 0003-9861
REMARK 1 REFERENCE 3
REMARK 1 AUTH T.E.MEYER
REMARK 1 TITL ISOLATION AND CHARACTERIZATION OF SOLUBLE CYTOCHROMES,
REMARK 1 TITL 2 FERREDOXINS AND OTHER CHROMOPHORIC PROTEINS FROM THE
REMARK 1 TITL 3 HALOPHILIC PHOTOTROPHIC BACTERIUM ECTOTHIORHODOSPIRA
REMARK 1 TITL 4 HALOPHILA
REMARK 1 REF BIOCHIM.BIOPHYS.ACTA V. 806 175 1985
REMARK 1 REFN ISSN 0006-3002
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DISCOVER
REMARK 3 AUTHORS : BIOSYM
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1GKS 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_1000173594.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
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 : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AMX-600
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 40
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 37
REMARK 210 CONFORMERS, SELECTION CRITERIA : PHYSICAL AND EXPERIMENTAL 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 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 11 LEU A 49 CB - CG - CD2 ANGL. DEV. = 10.6 DEGREES
REMARK 500 23 ARG A 37 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 33 CYS A 14 CA - CB - SG ANGL. DEV. = 8.7 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 29 49.43 36.39
REMARK 500 1 PRO A 38 85.83 -63.08
REMARK 500 1 ASP A 59 100.80 -47.79
REMARK 500 2 ASN A 29 54.11 35.14
REMARK 500 2 ARG A 64 -49.81 -29.32
REMARK 500 3 ASN A 8 -12.74 -145.32
REMARK 500 3 SER A 40 101.81 -53.99
REMARK 500 3 ARG A 64 -62.17 52.05
REMARK 500 4 ASN A 8 40.36 -157.31
REMARK 500 4 ASN A 29 53.60 36.09
REMARK 500 4 PRO A 38 84.33 -68.03
REMARK 500 4 SER A 40 106.82 -46.79
REMARK 500 4 ARG A 64 -59.35 15.32
REMARK 500 4 SER A 76 34.57 -72.07
REMARK 500 5 ASN A 8 33.77 -157.65
REMARK 500 5 PRO A 38 93.67 -59.38
REMARK 500 5 SER A 40 106.93 -48.41
REMARK 500 5 ASP A 59 102.83 -49.41
REMARK 500 5 ARG A 64 -52.47 -28.29
REMARK 500 5 SER A 76 42.49 -74.41
REMARK 500 6 ASN A 8 39.07 -159.69
REMARK 500 6 SER A 40 103.94 -57.00
REMARK 500 6 ASP A 59 84.86 -53.79
REMARK 500 6 SER A 76 41.42 -74.03
REMARK 500 7 GLU A 3 60.51 38.33
REMARK 500 7 SER A 4 -61.52 -156.11
REMARK 500 7 ALA A 30 74.47 -153.15
REMARK 500 7 SER A 40 94.96 -55.22
REMARK 500 7 ARG A 64 -45.86 -29.83
REMARK 500 8 ASN A 29 51.67 35.70
REMARK 500 8 SER A 40 101.86 -56.91
REMARK 500 8 ASP A 59 109.78 -37.30
REMARK 500 8 ARG A 64 -52.25 -27.38
REMARK 500 9 ASN A 8 -9.69 -149.17
REMARK 500 9 ASN A 29 52.19 33.96
REMARK 500 9 SER A 40 104.99 -56.54
REMARK 500 9 LYS A 52 112.54 -160.52
REMARK 500 9 ASP A 59 83.44 -55.87
REMARK 500 9 ARG A 64 -49.99 -29.96
REMARK 500 10 GLU A 3 -40.32 68.49
REMARK 500 10 ASN A 8 -8.24 -146.68
REMARK 500 10 ASN A 29 54.16 35.17
REMARK 500 10 PRO A 38 87.13 -62.23
REMARK 500 10 ARG A 64 -51.57 -26.65
REMARK 500 11 ASN A 8 -15.51 -148.61
REMARK 500 11 ALA A 30 59.44 -141.10
REMARK 500 11 TRP A 34 -40.28 -134.66
REMARK 500 11 SER A 40 102.51 -50.72
REMARK 500 11 SER A 76 37.93 -74.83
REMARK 500 11 THR A 77 24.24 -148.59
REMARK 500
REMARK 500 THIS ENTRY HAS 179 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 6 0.08 SIDE CHAIN
REMARK 500 2 TYR A 58 0.06 SIDE CHAIN
REMARK 500 2 TYR A 73 0.12 SIDE CHAIN
REMARK 500 3 TYR A 6 0.09 SIDE CHAIN
REMARK 500 3 ARG A 20 0.10 SIDE CHAIN
REMARK 500 5 TYR A 6 0.07 SIDE CHAIN
REMARK 500 5 TYR A 73 0.10 SIDE CHAIN
REMARK 500 6 TYR A 58 0.07 SIDE CHAIN
REMARK 500 7 TYR A 6 0.07 SIDE CHAIN
REMARK 500 8 TYR A 58 0.10 SIDE CHAIN
REMARK 500 8 TYR A 73 0.12 SIDE CHAIN
REMARK 500 9 TYR A 6 0.08 SIDE CHAIN
REMARK 500 9 TYR A 58 0.07 SIDE CHAIN
REMARK 500 10 TYR A 58 0.07 SIDE CHAIN
REMARK 500 11 TYR A 6 0.09 SIDE CHAIN
REMARK 500 11 TYR A 58 0.07 SIDE CHAIN
REMARK 500 12 TYR A 6 0.10 SIDE CHAIN
REMARK 500 12 TYR A 58 0.07 SIDE CHAIN
REMARK 500 13 TYR A 6 0.08 SIDE CHAIN
REMARK 500 13 TYR A 73 0.08 SIDE CHAIN
REMARK 500 14 TYR A 6 0.08 SIDE CHAIN
REMARK 500 14 TYR A 73 0.06 SIDE CHAIN
REMARK 500 15 TYR A 6 0.11 SIDE CHAIN
REMARK 500 15 ARG A 20 0.10 SIDE CHAIN
REMARK 500 15 ARG A 37 0.08 SIDE CHAIN
REMARK 500 15 TYR A 73 0.10 SIDE CHAIN
REMARK 500 16 TYR A 6 0.08 SIDE CHAIN
REMARK 500 16 TYR A 73 0.13 SIDE CHAIN
REMARK 500 17 TYR A 6 0.11 SIDE CHAIN
REMARK 500 17 TYR A 73 0.07 SIDE CHAIN
REMARK 500 18 TYR A 6 0.09 SIDE CHAIN
REMARK 500 18 TYR A 73 0.06 SIDE CHAIN
REMARK 500 19 TYR A 73 0.09 SIDE CHAIN
REMARK 500 21 TYR A 6 0.06 SIDE CHAIN
REMARK 500 21 TYR A 73 0.11 SIDE CHAIN
REMARK 500 22 ARG A 61 0.09 SIDE CHAIN
REMARK 500 23 TYR A 6 0.10 SIDE CHAIN
REMARK 500 26 TYR A 6 0.07 SIDE CHAIN
REMARK 500 27 TYR A 73 0.10 SIDE CHAIN
REMARK 500 28 TYR A 6 0.08 SIDE CHAIN
REMARK 500 29 TYR A 6 0.09 SIDE CHAIN
REMARK 500 30 TYR A 6 0.10 SIDE CHAIN
REMARK 500 30 TYR A 73 0.13 SIDE CHAIN
REMARK 500 31 TYR A 73 0.10 SIDE CHAIN
REMARK 500 32 TYR A 6 0.08 SIDE CHAIN
REMARK 500 33 TYR A 6 0.14 SIDE CHAIN
REMARK 500 33 TYR A 73 0.09 SIDE CHAIN
REMARK 500 34 TYR A 6 0.11 SIDE CHAIN
REMARK 500 34 TYR A 73 0.08 SIDE CHAIN
REMARK 500 35 TYR A 6 0.08 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 55 PLANE DEVIATIONS.
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 0 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 18 NE2
REMARK 620 2 HEM A 0 NA 91.7
REMARK 620 3 HEM A 0 NB 88.1 90.2
REMARK 620 4 HEM A 0 NC 90.0 177.9 91.1
REMARK 620 5 HEM A 0 ND 91.4 90.1 179.4 88.6
REMARK 620 6 MET A 55 SD 173.1 84.7 86.1 93.7 94.5
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 0
DBREF 1GKS A 1 78 UNP P00122 CY551_ECTHA 1 78
SEQRES 1 A 78 ASP GLY GLU SER ILE TYR ILE ASN GLY THR ALA PRO THR
SEQRES 2 A 78 CYS SER SER CYS HIS ASP ARG GLY VAL ALA GLY ALA PRO
SEQRES 3 A 78 GLU LEU ASN ALA PRO GLU ASP TRP ALA ASP ARG PRO SER
SEQRES 4 A 78 SER VAL ASP GLU LEU VAL GLU SER THR LEU ALA GLY LYS
SEQRES 5 A 78 GLY ALA MET PRO ALA TYR ASP GLY ARG ALA ASP ARG GLU
SEQRES 6 A 78 ASP LEU VAL LYS ALA ILE GLU TYR MET LEU SER THR LEU
HET HEM A 0 43
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETSYN HEM HEME
FORMUL 2 HEM C34 H32 FE N4 O4
HELIX 1 1 GLY A 2 ILE A 7 1 6
HELIX 2 2 SER A 15 HIS A 18 1 4
HELIX 3 3 VAL A 22 GLY A 24 5 3
HELIX 4 4 PRO A 31 ALA A 35 1 5
HELIX 5 5 VAL A 41 ALA A 50 1 10
HELIX 6 6 ARG A 64 LEU A 75 1 12
LINK CAB HEM A 0 SG CYS A 14 1555 1555 1.82
LINK CAC HEM A 0 SG CYS A 17 1555 1555 1.81
LINK FE HEM A 0 NE2 HIS A 18 1555 1555 1.99
LINK FE HEM A 0 SD MET A 55 1555 1555 2.35
CISPEP 1 ALA A 11 PRO A 12 1 -9.11
CISPEP 2 ALA A 11 PRO A 12 2 -5.63
CISPEP 3 ALA A 11 PRO A 12 3 -12.18
CISPEP 4 ALA A 11 PRO A 12 4 -12.69
CISPEP 5 ALA A 11 PRO A 12 5 -9.92
CISPEP 6 ALA A 11 PRO A 12 6 -9.33
CISPEP 7 ALA A 11 PRO A 12 7 -13.37
CISPEP 8 ALA A 11 PRO A 12 8 -11.09
CISPEP 9 ALA A 11 PRO A 12 9 -3.22
CISPEP 10 ALA A 11 PRO A 12 10 -11.48
CISPEP 11 ALA A 11 PRO A 12 11 -8.46
CISPEP 12 ALA A 11 PRO A 12 12 -7.33
CISPEP 13 ALA A 11 PRO A 12 13 -10.92
CISPEP 14 ALA A 11 PRO A 12 14 -8.52
CISPEP 15 ALA A 11 PRO A 12 15 -11.03
CISPEP 16 ALA A 11 PRO A 12 16 -15.17
CISPEP 17 ALA A 11 PRO A 12 17 -13.74
CISPEP 18 ALA A 11 PRO A 12 18 -15.72
CISPEP 19 ALA A 11 PRO A 12 19 -13.01
CISPEP 20 ALA A 11 PRO A 12 20 -12.89
CISPEP 21 ALA A 11 PRO A 12 21 -12.77
CISPEP 22 ALA A 11 PRO A 12 22 -8.65
CISPEP 23 ALA A 11 PRO A 12 23 -9.76
CISPEP 24 ALA A 11 PRO A 12 24 -11.07
CISPEP 25 ALA A 11 PRO A 12 25 -11.18
CISPEP 26 ALA A 11 PRO A 12 26 -8.62
CISPEP 27 ALA A 11 PRO A 12 27 -9.71
CISPEP 28 ALA A 11 PRO A 12 28 -9.00
CISPEP 29 ALA A 11 PRO A 12 29 -15.41
CISPEP 30 ALA A 11 PRO A 12 30 -14.35
CISPEP 31 ALA A 11 PRO A 12 31 -18.11
CISPEP 32 ALA A 11 PRO A 12 32 -8.95
CISPEP 33 ALA A 11 PRO A 12 33 -8.90
CISPEP 34 ALA A 11 PRO A 12 34 -13.16
CISPEP 35 ALA A 11 PRO A 12 35 -10.60
CISPEP 36 ALA A 11 PRO A 12 36 -10.73
CISPEP 37 ALA A 11 PRO A 12 37 -7.04
SITE 1 AC1 15 THR A 10 CYS A 14 CYS A 17 HIS A 18
SITE 2 AC1 15 ALA A 25 PRO A 26 ARG A 37 LEU A 44
SITE 3 AC1 15 SER A 47 THR A 48 LYS A 52 ALA A 54
SITE 4 AC1 15 MET A 55 TYR A 58 MET A 74
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 23 2 Bytes