Header list of 1k3g.pdb file
Complete list - b 23 2 Bytes
HEADER ELECTRON TRANSPORT 03-OCT-01 1K3G
TITLE NMR SOLUTION STRUCTURE OF OXIDIZED CYTOCHROME C-553 FROM BACILLUS
TITLE 2 PASTEURII
CAVEAT 1K3G THERE IS A CHIRALITY ERROR AT THE CA CENTER OF VAL22.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME C-553;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 22-92;
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: DH5ALPHA;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PEC86
KEYWDS C-553, HEME, CYTOCHROME, BACILLUS PASTEURII, ELECTRON TRANSFER,
KEYWDS 2 ELECTRON TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR L.BANCI,I.BERTINI,S.CIURLI,A.DIKIY,J.DITTMER,A.ROSATO,G.SCIARA,
AUTHOR 2 A.R.THOMPSETT
REVDAT 5 23-FEB-22 1K3G 1 REMARK LINK
REVDAT 4 24-FEB-09 1K3G 1 VERSN
REVDAT 3 01-APR-03 1K3G 1 JRNL
REVDAT 2 17-APR-02 1K3G 1 JRNL
REVDAT 1 31-OCT-01 1K3G 0
JRNL AUTH L.BANCI,I.BERTINI,S.CIURLI,A.DIKIY,J.DITTMER,A.ROSATO,
JRNL AUTH 2 G.SCIARA,A.R.THOMPSETT
JRNL TITL NMR SOLUTION STRUCTURE, BACKBONE MOBILITY, AND HOMOLOGY
JRNL TITL 2 MODELING OF C-TYPE CYTOCHROMES FROM GRAM-POSITIVE BACTERIA.
JRNL REF CHEMBIOCHEM V. 3 299 2002
JRNL REFN ISSN 1439-4227
JRNL PMID 11933230
JRNL DOI 10.1002/1439-7633(20020402)3:4<299::AID-CBIC299>3.0.CO;2-0
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.BENINI,A.GONZALEZ,W.R.RYPNIEWSKI,K.S.WILSON,
REMARK 1 AUTH 2 J.J.VAN BEEUMEN,S.CIURLI
REMARK 1 TITL CRYSTAL STRUCTURE OF OXIDIZED BACILLUS PASTEURII CYTOCHROME
REMARK 1 TITL 2 C-553 AT 0.97-A RESOLUTION
REMARK 1 REF BIOCHEMISTRY V. 39 13115 2000
REMARK 1 REFN ISSN 0006-2960
REMARK 1 DOI 10.1021/BI000402J
REMARK 1 REFERENCE 2
REMARK 1 AUTH S.BENINI,M.BORSARI,S.CIURLI,A.DIKIY,M.LAMBORGHINI
REMARK 1 TITL MODULATION OF BACILLUS PASTEURII CYTOCHROME C553 REDUCTION
REMARK 1 TITL 2 POTENTIAL BY STRUCTURAL AND SOLUTION PARAMETERS
REMARK 1 REF J.BIOL.INORG.CHEM. V. 3 371 1998
REMARK 1 REFN ISSN 0949-8257
REMARK 1 DOI 10.1007/S007750050247
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, AMBER 5.0
REMARK 3 AUTHORS : BRUKER (XWINNMR), KOLLMAN (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 PSEUDOCONTACT SHIFTS WERE INCLUDED AS CONSTRAINTS BY
REMARK 3 MEANS OF MODIFIED DYANA AND SANDER MODULES
REMARK 3 (PSEUDODYANA, PSEUDOREM) (BANCI ET AL., 1997)
REMARK 4
REMARK 4 1K3G COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-OCT-01.
REMARK 100 THE DEPOSITION ID IS D_1000014512.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 288
REMARK 210 PH : 7.5
REMARK 210 IONIC STRENGTH : 10 MM PHOSPHATE BUFFER
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1-3 MM OXIDIZED CYTOCHROME C-553
REMARK 210 IN 10 MM PHOSPHATE BUFFER
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; HNHA; 1D NOE
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 700 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY 1.3.13, DYANA 1.5
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS,
REMARK 210 RESTRAINED ENERGY MINIMIZATION
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 400
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
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 1 VAL A 22 CB - CA - C ANGL. DEV. = 11.6 DEGREES
REMARK 500 1 VAL A 22 CA - CB - CG2 ANGL. DEV. = 9.1 DEGREES
REMARK 500 26 VAL A 22 CB - CA - C ANGL. DEV. = 12.1 DEGREES
REMARK 500 26 VAL A 22 CA - CB - CG2 ANGL. DEV. = 10.9 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 GLN A 29 -8.03 -57.34
REMARK 500 1 LYS A 31 -59.44 -138.97
REMARK 500 1 ALA A 43 -77.93 -131.27
REMARK 500 1 GLN A 68 135.64 177.37
REMARK 500 2 GLN A 30 59.23 -142.60
REMARK 500 2 LYS A 31 -36.39 -173.08
REMARK 500 2 ALA A 43 -71.56 -143.79
REMARK 500 2 GLN A 68 133.56 173.83
REMARK 500 3 GLN A 29 -7.20 -58.12
REMARK 500 3 GLN A 30 33.10 -142.82
REMARK 500 3 LYS A 31 -55.66 -153.92
REMARK 500 3 ALA A 43 -75.83 -137.45
REMARK 500 3 GLN A 68 140.58 176.87
REMARK 500 4 LYS A 31 -38.58 -172.04
REMARK 500 4 SER A 34 -36.75 -38.92
REMARK 500 4 ALA A 43 -76.90 -143.52
REMARK 500 4 LYS A 50 40.87 -109.31
REMARK 500 4 GLN A 68 131.38 176.31
REMARK 500 4 GLU A 90 35.65 -84.70
REMARK 500 5 GLN A 30 48.60 -146.43
REMARK 500 5 LYS A 31 -39.70 -162.46
REMARK 500 5 SER A 34 -39.19 -37.38
REMARK 500 5 ALA A 43 -79.77 -143.60
REMARK 500 5 GLN A 68 130.18 173.98
REMARK 500 6 GLN A 30 44.57 -142.56
REMARK 500 6 LYS A 31 -39.98 -157.36
REMARK 500 6 ALA A 43 -73.10 -151.79
REMARK 500 6 GLN A 68 136.28 176.51
REMARK 500 7 LYS A 31 -58.61 -161.28
REMARK 500 7 ALA A 43 -80.34 -152.52
REMARK 500 7 GLN A 68 139.13 170.46
REMARK 500 8 LYS A 31 -38.97 -167.96
REMARK 500 8 SER A 34 -38.55 -37.92
REMARK 500 8 ALA A 43 -78.10 -135.39
REMARK 500 8 GLN A 68 132.87 174.30
REMARK 500 9 GLN A 30 43.67 -141.71
REMARK 500 9 LYS A 31 -39.73 -153.18
REMARK 500 9 SER A 34 -37.01 -37.75
REMARK 500 9 ALA A 43 -72.98 -155.08
REMARK 500 9 GLN A 68 139.63 167.08
REMARK 500 10 LYS A 31 -38.90 -166.43
REMARK 500 10 SER A 34 -39.31 -36.92
REMARK 500 10 ALA A 43 -76.77 -156.24
REMARK 500 10 GLN A 68 140.72 167.03
REMARK 500 11 GLN A 30 55.10 -144.67
REMARK 500 11 LYS A 31 -38.29 -167.25
REMARK 500 11 ALA A 43 -79.55 -135.95
REMARK 500 11 GLN A 68 138.38 166.73
REMARK 500 12 ALA A 24 -64.12 -105.18
REMARK 500 12 LYS A 31 -56.67 -152.37
REMARK 500
REMARK 500 THIS ENTRY HAS 125 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 11 133.18
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 5 TYR A 55 0.08 SIDE CHAIN
REMARK 500 9 TYR A 55 0.07 SIDE CHAIN
REMARK 500 23 TYR A 55 0.09 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 98.0
REMARK 620 3 HEC A 93 NB 89.5 90.6
REMARK 620 4 HEC A 93 NC 86.1 173.8 94.0
REMARK 620 5 HEC A 93 ND 91.1 87.5 178.0 87.9
REMARK 620 6 MET A 71 SD 173.2 82.1 97.3 93.2 82.2
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: 1C75 RELATED DB: PDB
REMARK 900 1C75 IS THE X-RAY STRUCTURE OF THE CYTOCHROME C553 FROM B.
REMARK 900 PASTEURII.
REMARK 900 RELATED ID: 1K3H RELATED DB: PDB
REMARK 900 1K3H IS THE MINIMIZED AVERAGE OF OXIDIZED CYTOCHROME C-553 FROM B.
REMARK 900 PASTEURII.
DBREF 1K3G 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 GLN A 29 1 7
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 1.81
LINK SG CYS A 35 CAC HEC A 93 1555 1555 1.81
LINK NE2 HIS A 36 FE HEC A 93 1555 1555 1.98
LINK SD MET A 71 FE HEC A 93 1555 1555 2.41
SITE 1 AC1 17 LYS A 31 CYS A 32 CYS A 35 HIS A 36
SITE 2 AC1 17 ALA A 45 PRO A 46 ILE A 48 TYR A 55
SITE 3 AC1 17 ILE A 60 ILE A 63 ILE A 64 GLN A 68
SITE 4 AC1 17 GLY A 69 GLY A 70 MET A 71 ILE A 75
SITE 5 AC1 17 VAL A 84
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