Header list of 1n9c.pdb file
Complete list - b 23 2 Bytes
HEADER ELECTRON TRANSPORT 23-NOV-02 1N9C
TITLE STRUCTURE AND DYNAMICS OF REDUCED BACILLUS PASTEURII CYTOCHROME C:
TITLE 2 OXIDATION STATE DEPENDENT PROPERTIES AND IMPLICATIONS FOR ELECTRON
TITLE 3 TRANSFER PROCESSES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME C-553;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SOLUBLE PART OF MEMBRANE-ANCHORED CYTOCHROME C;
COMPND 5 SYNONYM: C553;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SPOROSARCINA PASTEURII;
SOURCE 3 ORGANISM_TAXID: 1474;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: C41(DE3)
KEYWDS CYTOCHROME C, RESPIRATION, ELECTRON TRANSFER, REDOX, ELECTRON
KEYWDS 2 TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR I.BARTALESI,I.BERTINI,A.ROSATO
REVDAT 3 23-FEB-22 1N9C 1 REMARK LINK
REVDAT 2 24-FEB-09 1N9C 1 VERSN
REVDAT 1 04-FEB-03 1N9C 0
JRNL AUTH I.BARTALESI,I.BERTINI,A.ROSATO
JRNL TITL STRUCTURE AND DYNAMICS OF REDUCED BACILLUS PASTEURII
JRNL TITL 2 CYTOCHROME C: OXIDATION STATE DEPENDENT PROPERTIES AND
JRNL TITL 3 IMPLICATIONS FOR ELECTRON TRANSFER PROCESSES
JRNL REF BIOCHEMISTRY V. 42 739 2003
JRNL REFN ISSN 0006-2960
JRNL PMID 12534286
JRNL DOI 10.1021/BI0266028
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH L.BANCI,I.BERTINI,S.CIURLI,A.DIKIY,J.DITTMER,A.ROSATO,
REMARK 1 AUTH 2 G.SCIARA,A.R.THOMPSETT
REMARK 1 TITL NMR SOLUTION STRUCTURE, BACKBONE MOBILITY AND HOMOLOGY
REMARK 1 TITL 2 MODELING OF C-TYPE CYTOCHROMES FROM GRAM-POSITIVE BACTERIA
REMARK 1 REF CHEMBIOCHEM V. 3 299 2002
REMARK 1 REFN ISSN 1439-4227
REMARK 1 DOI 10.1002/1439-7633(20020402)3:4<299::AID-CBIC299>3.0.CO;2-0
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA 1.5, DYANA 1.5
REMARK 3 AUTHORS : GUENTERT (DYANA), GUENTERT (DYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1N9C COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-DEC-02.
REMARK 100 THE DEPOSITION ID IS D_1000017680.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 296
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 100 MM PI
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2 MM CYTOCHROME, 100MM PHOSPHATE
REMARK 210 BUFFER, PH 7.0; 1 MM CYTOCHROME
REMARK 210 U-15N, 100MM PHOSPHATE BUFFER,
REMARK 210 PH 7.0
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; 3D_15N
REMARK 210 -SEPARATED_NOESY; HNHA; HNHB; 3D-
REMARK 210 15N-SEPARATED_TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR
REMARK 210 METHOD USED : RESTRAINED ENERGY MINIMIZATION
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 130
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
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 GLN A 29 1.33 -62.37
REMARK 500 1 GLN A 30 -8.13 -142.73
REMARK 500 1 SER A 34 -38.52 -39.40
REMARK 500 1 ALA A 43 -85.31 -81.49
REMARK 500 1 GLN A 68 122.16 -170.59
REMARK 500 2 GLN A 29 0.76 -61.23
REMARK 500 2 ALA A 43 -78.43 -76.96
REMARK 500 3 GLN A 29 0.19 -61.04
REMARK 500 3 ALA A 43 -84.09 -86.68
REMARK 500 4 GLN A 29 0.40 -61.29
REMARK 500 4 GLN A 30 -13.43 -140.81
REMARK 500 4 ALA A 43 -81.74 -81.57
REMARK 500 4 ASN A 66 -60.17 -102.50
REMARK 500 4 LYS A 91 4.09 -64.51
REMARK 500 5 ASP A 23 97.71 -68.61
REMARK 500 5 LYS A 31 -54.61 -125.01
REMARK 500 5 ALA A 43 -78.92 -82.66
REMARK 500 5 ALA A 79 -6.73 -55.10
REMARK 500 6 GLN A 29 -2.32 -56.02
REMARK 500 6 LYS A 31 -53.06 -129.33
REMARK 500 6 ALA A 43 -72.55 -113.56
REMARK 500 7 GLN A 29 1.05 -60.34
REMARK 500 7 ALA A 43 -80.37 -80.08
REMARK 500 7 ASN A 66 -61.24 -94.81
REMARK 500 7 LYS A 91 9.40 -62.64
REMARK 500 8 GLN A 29 0.86 -63.93
REMARK 500 8 ALA A 43 -76.50 -100.73
REMARK 500 8 ALA A 79 -38.94 -39.84
REMARK 500 8 LYS A 91 7.62 -68.20
REMARK 500 9 GLN A 29 0.46 -57.89
REMARK 500 9 ALA A 43 -78.27 -80.42
REMARK 500 10 GLN A 29 0.89 -60.37
REMARK 500 10 ALA A 43 -80.24 -80.16
REMARK 500 11 GLN A 29 -3.88 -56.63
REMARK 500 11 ALA A 43 -79.25 -101.80
REMARK 500 11 ASN A 66 -62.31 -103.40
REMARK 500 12 GLN A 30 -26.61 -140.27
REMARK 500 12 ALA A 43 -75.81 -79.31
REMARK 500 12 LYS A 91 8.75 -66.93
REMARK 500 13 GLN A 29 0.26 -59.08
REMARK 500 13 ALA A 43 -77.02 -85.24
REMARK 500 13 LYS A 91 7.67 -68.82
REMARK 500 14 ALA A 24 -69.86 -101.51
REMARK 500 14 GLN A 29 0.83 -59.92
REMARK 500 14 GLN A 30 -15.51 -140.47
REMARK 500 14 SER A 34 -39.67 -38.46
REMARK 500 14 ALA A 43 -82.53 -80.59
REMARK 500 14 ASN A 66 -60.77 -105.42
REMARK 500 15 SER A 34 -37.38 -38.64
REMARK 500 15 ALA A 43 -77.11 -108.40
REMARK 500
REMARK 500 THIS ENTRY HAS 88 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 VAL A 22 ASP A 23 2 -138.55
REMARK 500 LYS A 91 LYS A 92 4 -125.59
REMARK 500 LYS A 91 LYS A 92 7 -149.81
REMARK 500 LYS A 91 LYS A 92 8 -143.35
REMARK 500 LYS A 91 LYS A 92 11 -146.19
REMARK 500 LYS A 91 LYS A 92 12 -131.73
REMARK 500 LYS A 91 LYS A 92 13 -128.47
REMARK 500 LYS A 91 LYS A 92 15 -145.45
REMARK 500 LYS A 91 LYS A 92 16 -124.92
REMARK 500 LYS A 91 LYS A 92 17 -126.37
REMARK 500 LYS A 91 LYS A 92 23 -148.44
REMARK 500 VAL A 22 ASP A 23 29 -146.42
REMARK 500 GLU A 90 LYS A 91 29 -149.98
REMARK 500 LYS A 91 LYS A 92 29 -107.28
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 8 TYR A 55 0.08 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 93 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 36 NE2
REMARK 620 2 HEC A 93 NA 94.8
REMARK 620 3 HEC A 93 NB 91.9 90.6
REMARK 620 4 HEC A 93 NC 89.9 174.4 92.3
REMARK 620 5 HEC A 93 ND 88.8 90.3 178.8 86.8
REMARK 620 6 MET A 71 SD 169.6 80.6 97.4 94.2 82.0
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 93
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1K3G RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE OXIDIZED PROTEIN
DBREF 1N9C A 22 92 UNP P82599 CY553_BACPA 22 92
SEQRES 1 A 71 VAL ASP ALA GLU ALA VAL VAL GLN GLN LYS CYS ILE SER
SEQRES 2 A 71 CYS HIS GLY GLY ASP LEU THR GLY ALA SER ALA PRO ALA
SEQRES 3 A 71 ILE ASP LYS ALA GLY ALA ASN TYR SER GLU GLU GLU ILE
SEQRES 4 A 71 LEU ASP ILE ILE LEU ASN GLY GLN GLY GLY MET PRO GLY
SEQRES 5 A 71 GLY ILE ALA LYS GLY ALA GLU ALA GLU ALA VAL ALA ALA
SEQRES 6 A 71 TRP LEU ALA GLU LYS LYS
HET HEC A 93 75
HETNAM HEC HEME C
FORMUL 2 HEC C34 H34 FE N4 O4
HELIX 1 1 ASP A 23 CYS A 32 1 10
HELIX 2 2 CYS A 32 GLY A 37 1 6
HELIX 3 3 LYS A 50 TYR A 55 1 6
HELIX 4 4 SER A 56 GLY A 67 1 12
HELIX 5 5 GLY A 78 LYS A 91 1 14
LINK SG CYS A 32 CAB HEC A 93 1555 1555 1.79
LINK SG CYS A 35 CAC HEC A 93 1555 1555 1.80
LINK NE2 HIS A 36 FE HEC A 93 1555 1555 1.98
LINK SD MET A 71 FE HEC A 93 1555 1555 2.39
SITE 1 AC1 16 LYS A 31 CYS A 32 CYS A 35 HIS A 36
SITE 2 AC1 16 ALA A 45 PRO A 46 ILE A 48 TYR A 55
SITE 3 AC1 16 ILE A 60 ILE A 63 GLN A 68 GLY A 70
SITE 4 AC1 16 MET A 71 PRO A 72 VAL A 84 LEU A 88
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