Header list of 1i6d.pdb file
Complete list - b 23 2 Bytes
HEADER ELECTRON TRANSPORT 02-MAR-01 1I6D
TITLE SOLUTION STRUCTURE OF THE FUNCTIONAL DOMAIN OF PARACOCCUS
TITLE 2 DENITRIFICANS CYTOCHROME C552 IN THE REDUCED STATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME C552;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SOLUBLE FUNCTIONAL DOMAIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: COVALENT THIOETHER LINKAGES FROM HEME COFACTOR TO BOTH
COMPND 7 CYS14 AND CYS17
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PARACOCCUS DENITRIFICANS;
SOURCE 3 ORGANISM_TAXID: 266;
SOURCE 4 STRAIN: PD1235;
SOURCE 5 CELLULAR_LOCATION: PERIPLASM;
SOURCE 6 GENE: CYCM;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 10 EXPRESSION_SYSTEM_CELLULAR_LOCATION: PERIPLASM;
SOURCE 11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PET22B+;
SOURCE 13 OTHER_DETAILS: HETEROLOGOUS EXPRESSION
KEYWDS ELECTRON TRANSPORT, CYTOCHROME C552, HEME, REDOX STATES, ISOTOPE
KEYWDS 2 ENRICHMENT {13C/15N}, NMR SPECTROSCOPY, SOLUTION STRUCTURE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR B.REINCKE,C.PEREZ,P.PRISTOVSEK,C.LUECKE,C.LUDWIG,F.LOEHR,V.V.ROGOV,
AUTHOR 2 B.LUDWIG,H.RUETERJANS
REVDAT 4 23-FEB-22 1I6D 1 REMARK LINK
REVDAT 3 24-FEB-09 1I6D 1 VERSN
REVDAT 2 01-APR-03 1I6D 1 JRNL
REVDAT 1 17-OCT-01 1I6D 0
JRNL AUTH B.REINCKE,C.PEREZ,P.PRISTOVSEK,C.LUCKE,C.LUDWIG,F.LOHR,
JRNL AUTH 2 V.V.ROGOV,B.LUDWIG,H.RUTERJANS
JRNL TITL SOLUTION STRUCTURE AND DYNAMICS OF THE FUNCTIONAL DOMAIN OF
JRNL TITL 2 PARACOCCUS DENITRIFICANS CYTOCHROME C(552) IN BOTH REDOX
JRNL TITL 3 STATES.
JRNL REF BIOCHEMISTRY V. 40 12312 2001
JRNL REFN ISSN 0006-2960
JRNL PMID 11591150
JRNL DOI 10.1021/BI010615O
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH P.PRISTOVSEK,C.LUECKE,B.REINCKE,B.LUDWIG,H.RUETERJANS
REMARK 1 TITL SOLUTION STRUCTURE OF THE FUNCTIONAL DOMAIN OF PARACOCCUS
REMARK 1 TITL 2 DENITRIFICANS CYTOCHROME C552 IN THE REDUCED STATE
REMARK 1 REF EUR.J.BIOCHEM. V. 267 4205 2000
REMARK 1 REFN ISSN 0014-2956
REMARK 1 DOI 10.1046/J.1432-1327.2000.01456.X
REMARK 1 REFERENCE 2
REMARK 1 AUTH A.HARRENGA,B.REINCKE,H.RUETERJANS,B.LUDWIG,H.MICHEL
REMARK 1 TITL STRUCTURE OF THE SOLUBLE DOMAIN OF CYTOCHROME C552 FROM
REMARK 1 TITL 2 PARACOCCUS DENITRIFICANS IN THE OXIDIZED AND REDUCED STATES
REMARK 1 REF J.MOL.BIOL. V. 295 667 2000
REMARK 1 REFN ISSN 0022-2836
REMARK 1 DOI 10.1006/JMBI.1999.3382
REMARK 1 REFERENCE 3
REMARK 1 AUTH B.REINCKE,L.THOENY-MEYER,C.DANNEHL,A.ODENWALD,M.AIDIM,
REMARK 1 AUTH 2 H.WITT,H.RUETERJANS,B.LUDWIG
REMARK 1 TITL HETEROLOGOUS EXPRESSION OF SOLUBLE FRAGMENTS OF CYTOCHROME
REMARK 1 TITL 2 C552 ACTING AS ELECTRON DONOR TO THE PARACOCCUS
REMARK 1 TITL 3 DENITRIFICANS CYTOCHROME C OXIDASE
REMARK 1 REF BIOCHIM.BIOPHYS.ACTA V.1441 114 1999
REMARK 1 REFN ISSN 0006-3002
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DISCOVER 97
REMARK 3 AUTHORS : MSI
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: ENERGY MINIMIZATION.
REMARK 4
REMARK 4 1I6D COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-MAR-01.
REMARK 100 THE DEPOSITION ID IS D_1000012960.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298.00
REMARK 210 PH : 5.50
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : 20 MM PHOSPHATE, 90% H2O/ 10%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 1H-1H TOCSY; 1H-1H NOESY; 1H-15N
REMARK 210 HSQC; 1H-15N TOCSY-HSQC; 1H-15N
REMARK 210 NOESY-HSQC; HNCACB; CC(CO)NH-
REMARK 210 TOCSY; 1H-13C HSQC; 1H-13C NOESY-
REMARK 210 HSQC; (HCA)CO(CA)NH
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA 1.5, DISCOVER 97
REMARK 210 METHOD USED : DISTANCE GEOMETRY, ENERGY
REMARK 210 MINIMIZATION
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE EXPERIMENTS WERE PERFORMED WITH REDUCED UNLABELED, 15N
REMARK 210 -LABELED OR 13C-LABELED CYTOCHROME C552.
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: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O GLN A 63 HG1 THR A 67 1.57
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 1 GLU A 8 CD GLU A 8 OE1 0.114
REMARK 500 1 GLU A 60 CD GLU A 60 OE2 0.114
REMARK 500 1 GLU A 64 CD GLU A 64 OE1 0.114
REMARK 500 1 GLU A 87 CD GLU A 87 OE1 0.111
REMARK 500 1 GLU A 97 CD GLU A 97 OE1 0.111
REMARK 500 2 GLU A 8 CD GLU A 8 OE2 0.109
REMARK 500 2 GLU A 60 CD GLU A 60 OE1 0.114
REMARK 500 2 GLU A 64 CD GLU A 64 OE1 0.116
REMARK 500 2 GLU A 87 CD GLU A 87 OE2 0.111
REMARK 500 2 GLU A 97 CD GLU A 97 OE1 0.113
REMARK 500 3 GLU A 8 CD GLU A 8 OE1 0.109
REMARK 500 3 GLU A 60 CD GLU A 60 OE1 0.114
REMARK 500 3 GLU A 64 CD GLU A 64 OE1 0.113
REMARK 500 3 GLU A 87 CD GLU A 87 OE1 0.114
REMARK 500 3 GLU A 97 CD GLU A 97 OE1 0.113
REMARK 500 4 GLU A 8 CD GLU A 8 OE1 0.114
REMARK 500 4 GLU A 60 CD GLU A 60 OE2 0.110
REMARK 500 4 GLU A 64 CD GLU A 64 OE1 0.113
REMARK 500 4 GLU A 87 CD GLU A 87 OE2 0.109
REMARK 500 4 GLU A 97 CD GLU A 97 OE1 0.109
REMARK 500 5 GLU A 8 CD GLU A 8 OE2 0.112
REMARK 500 5 GLU A 60 CD GLU A 60 OE1 0.110
REMARK 500 5 GLU A 64 CD GLU A 64 OE1 0.114
REMARK 500 5 GLU A 87 CD GLU A 87 OE2 0.114
REMARK 500 5 GLU A 97 CD GLU A 97 OE1 0.114
REMARK 500 6 GLU A 8 CD GLU A 8 OE1 0.116
REMARK 500 6 GLU A 60 CD GLU A 60 OE1 0.114
REMARK 500 6 GLU A 64 CD GLU A 64 OE1 0.110
REMARK 500 6 GLU A 87 CD GLU A 87 OE2 0.114
REMARK 500 6 GLU A 97 CD GLU A 97 OE1 0.113
REMARK 500 7 GLU A 8 CD GLU A 8 OE2 0.112
REMARK 500 7 GLU A 60 CD GLU A 60 OE2 0.110
REMARK 500 7 GLU A 64 CD GLU A 64 OE2 0.110
REMARK 500 7 GLU A 87 CD GLU A 87 OE2 0.110
REMARK 500 7 GLU A 97 CD GLU A 97 OE1 0.110
REMARK 500 8 GLU A 8 CD GLU A 8 OE1 0.116
REMARK 500 8 GLU A 60 CD GLU A 60 OE1 0.114
REMARK 500 8 GLU A 64 CD GLU A 64 OE2 0.110
REMARK 500 8 GLU A 87 CD GLU A 87 OE1 0.114
REMARK 500 8 GLU A 97 CD GLU A 97 OE1 0.114
REMARK 500 9 GLU A 8 CD GLU A 8 OE1 0.118
REMARK 500 9 GLU A 60 CD GLU A 60 OE1 0.119
REMARK 500 9 GLU A 64 CD GLU A 64 OE1 0.112
REMARK 500 9 GLU A 87 CD GLU A 87 OE1 0.110
REMARK 500 9 GLU A 97 CD GLU A 97 OE1 0.115
REMARK 500 10 GLU A 8 CD GLU A 8 OE2 0.110
REMARK 500 10 GLU A 60 CD GLU A 60 OE1 0.114
REMARK 500 10 GLU A 64 CD GLU A 64 OE1 0.111
REMARK 500 10 GLU A 87 CD GLU A 87 OE2 0.110
REMARK 500 10 GLU A 97 CD GLU A 97 OE1 0.110
REMARK 500
REMARK 500 THIS ENTRY HAS 100 BOND DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
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 1 ASP A 21 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 1 HIS A 29 ND1 - CE1 - NE2 ANGL. DEV. = 8.6 DEGREES
REMARK 500 1 ARG A 36 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 1 ASP A 42 CB - CG - OD1 ANGL. DEV. = -5.8 DEGREES
REMARK 500 1 ASP A 48 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 1 HIS A 53 ND1 - CE1 - NE2 ANGL. DEV. = 8.4 DEGREES
REMARK 500 1 ASP A 56 CB - CG - OD1 ANGL. DEV. = 6.2 DEGREES
REMARK 500 1 ASP A 56 CB - CG - OD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 1 ASP A 88 CB - CG - OD1 ANGL. DEV. = -5.7 DEGREES
REMARK 500 1 ASP A 88 CB - CG - OD2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 1 ARG A 89 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 2 ASP A 3 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 2 HIS A 18 ND1 - CE1 - NE2 ANGL. DEV. = 7.8 DEGREES
REMARK 500 2 ASP A 21 CB - CG - OD1 ANGL. DEV. = -5.9 DEGREES
REMARK 500 2 HIS A 29 ND1 - CE1 - NE2 ANGL. DEV. = 8.6 DEGREES
REMARK 500 2 ARG A 36 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 2 ASP A 42 CB - CG - OD1 ANGL. DEV. = -6.0 DEGREES
REMARK 500 2 ASP A 42 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 2 HIS A 53 ND1 - CE1 - NE2 ANGL. DEV. = 8.6 DEGREES
REMARK 500 2 ASP A 56 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 2 ASP A 56 CB - CG - OD2 ANGL. DEV. = -6.5 DEGREES
REMARK 500 2 ASP A 88 CB - CG - OD1 ANGL. DEV. = -6.0 DEGREES
REMARK 500 2 ASP A 88 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 2 ARG A 89 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 3 ASP A 3 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 3 HIS A 18 ND1 - CE1 - NE2 ANGL. DEV. = 7.9 DEGREES
REMARK 500 3 ASP A 21 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 3 ASP A 21 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 3 ASP A 24 CB - CG - OD1 ANGL. DEV. = -5.4 DEGREES
REMARK 500 3 HIS A 29 ND1 - CE1 - NE2 ANGL. DEV. = 8.6 DEGREES
REMARK 500 3 ARG A 36 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 3 ASP A 42 CB - CG - OD1 ANGL. DEV. = -5.9 DEGREES
REMARK 500 3 ASP A 48 CB - CG - OD1 ANGL. DEV. = -5.9 DEGREES
REMARK 500 3 HIS A 53 ND1 - CE1 - NE2 ANGL. DEV. = 8.5 DEGREES
REMARK 500 3 ASP A 56 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 3 ARG A 89 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 4 ASP A 3 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 4 HIS A 18 ND1 - CE1 - NE2 ANGL. DEV. = 7.8 DEGREES
REMARK 500 4 ASP A 21 CB - CG - OD1 ANGL. DEV. = -5.8 DEGREES
REMARK 500 4 ASP A 24 CB - CG - OD1 ANGL. DEV. = -5.7 DEGREES
REMARK 500 4 ASP A 24 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 4 HIS A 29 ND1 - CE1 - NE2 ANGL. DEV. = 8.6 DEGREES
REMARK 500 4 ARG A 36 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 4 ASP A 42 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 4 ASP A 42 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 4 ASP A 48 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 4 ASP A 48 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 4 HIS A 53 ND1 - CE1 - NE2 ANGL. DEV. = 8.6 DEGREES
REMARK 500 4 ASP A 56 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 4 ASP A 56 CB - CG - OD2 ANGL. DEV. = -6.4 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 297 ANGLE DEVIATIONS.
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 2 GLN A 99 46.81 -89.50
REMARK 500 3 PRO A 28 -179.42 -69.99
REMARK 500 4 ALA A 52 39.39 -90.53
REMARK 500 4 LYS A 77 5.05 -69.89
REMARK 500 5 ASP A 21 56.03 -96.18
REMARK 500 6 ALA A 2 78.30 -113.81
REMARK 500 8 ALA A 2 71.17 -115.34
REMARK 500 8 ASP A 21 52.10 -110.95
REMARK 500 8 LYS A 77 22.94 -77.49
REMARK 500 9 ALA A 2 71.98 -118.32
REMARK 500 9 HIS A 29 124.33 -25.61
REMARK 500 9 ALA A 52 30.76 -86.44
REMARK 500 10 ALA A 2 72.34 -114.29
REMARK 500 10 LYS A 77 24.91 -74.45
REMARK 500 11 ALA A 39 69.05 70.64
REMARK 500 11 LYS A 77 5.76 -69.45
REMARK 500 12 ASP A 21 56.40 -90.30
REMARK 500 12 ALA A 52 32.76 -88.57
REMARK 500 12 LYS A 77 25.59 -74.72
REMARK 500 13 ALA A 39 61.60 67.00
REMARK 500 14 ALA A 2 105.21 -166.13
REMARK 500 14 ASP A 21 58.12 -94.48
REMARK 500 15 ALA A 2 78.42 -101.95
REMARK 500 15 LYS A 77 1.72 -69.86
REMARK 500 16 ALA A 2 78.06 -116.21
REMARK 500 17 ALA A 2 71.82 -116.67
REMARK 500 17 ASP A 21 52.80 -94.12
REMARK 500 17 HIS A 29 125.05 -36.60
REMARK 500 17 GLN A 99 56.81 -90.13
REMARK 500 18 LEU A 20 -31.19 64.73
REMARK 500 19 ALA A 39 60.77 65.35
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 6 HIS A 18 0.11 SIDE CHAIN
REMARK 500 9 ARG A 36 0.08 SIDE CHAIN
REMARK 500 15 HIS A 18 0.11 SIDE CHAIN
REMARK 500 18 HIS A 18 0.11 SIDE CHAIN
REMARK 500 20 HIS A 18 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 HEC A 101 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 18 NE2
REMARK 620 2 HEC A 101 NA 89.4
REMARK 620 3 HEC A 101 NB 97.4 84.1
REMARK 620 4 HEC A 101 NC 105.7 164.9 93.3
REMARK 620 5 HEC A 101 ND 76.8 86.5 169.0 97.2
REMARK 620 6 MET A 78 SD 150.3 70.8 102.1 95.3 80.0
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 101
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1I6E RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE FUNCTIONAL DOMAIN OF PARACOCCUS
REMARK 900 DENITRIFICANS CYTOCHROME C552 IN THE OXIDIZED STATE
REMARK 900 RELATED ID: 1QL3 RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF THE SOLUBLE DOMAIN OF CYTOCHROME C552 FROM
REMARK 900 PARACOCCUS DENITRIFICANS IN THE REDUCED STATE
REMARK 900 RELATED ID: 1QL4 RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF THE SOLUBLE DOMAIN OF CYTOCHROME C552 FROM
REMARK 900 PARACOCCUS DENITRIFICANS IN THE OXIDIZED STATE
REMARK 900 RELATED ID: 1C7M RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE FUNCTIONAL DOMAIN OF PARACOCCUS
REMARK 900 DENITRIFICANS CYTOCHROME C552 IN THE REDUCED STATE
DBREF 1I6D A 2 100 UNP P54820 CY552_PARDE 78 176
SEQADV 1I6D MET A 1 UNP P54820 SEE REMARK 999
SEQRES 1 A 100 MET ALA ASP PRO ALA ALA GLY GLU LYS VAL PHE GLY LYS
SEQRES 2 A 100 CYS LYS ALA CYS HIS LYS LEU ASP GLY ASN ASP GLY VAL
SEQRES 3 A 100 GLY PRO HIS LEU ASN GLY VAL VAL GLY ARG THR VAL ALA
SEQRES 4 A 100 GLY VAL ASP GLY PHE ASN TYR SER ASP PRO MET LYS ALA
SEQRES 5 A 100 HIS GLY GLY ASP TRP THR PRO GLU ALA LEU GLN GLU PHE
SEQRES 6 A 100 LEU THR ASN PRO LYS ALA VAL VAL LYS GLY THR LYS MET
SEQRES 7 A 100 ALA PHE ALA GLY LEU PRO LYS ILE GLU ASP ARG ALA ASN
SEQRES 8 A 100 LEU ILE ALA TYR LEU GLU GLY GLN GLN
HET HEC A 101 75
HETNAM HEC HEME C
FORMUL 2 HEC C34 H34 FE N4 O4
HELIX 1 H1 PRO A 4 LYS A 13 1 10
HELIX 2 H2 ASP A 48 HIS A 53 1 6
HELIX 3 H3 PRO A 59 THR A 67 1 9
HELIX 4 H4 PRO A 69 VAL A 72 1 4
HELIX 5 H5 ILE A 86 GLY A 98 1 13
LINK SG CYS A 14 CAB HEC A 101 1555 1555 1.81
LINK SG CYS A 17 CAC HEC A 101 1555 1555 1.82
LINK NE2 HIS A 18 FE HEC A 101 1555 1555 1.79
LINK SD MET A 78 FE HEC A 101 1555 1555 2.11
SITE 1 AC1 19 LYS A 13 CYS A 14 CYS A 17 HIS A 18
SITE 2 AC1 19 VAL A 26 ARG A 36 TYR A 46 SER A 47
SITE 3 AC1 19 MET A 50 TRP A 57 LEU A 62 PHE A 65
SITE 4 AC1 19 LEU A 66 THR A 76 LYS A 77 MET A 78
SITE 5 AC1 19 ALA A 79 PHE A 80 LEU 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 - b 23 2 Bytes