Header list of 1kx2.pdb file
Complete list - 23 20 Bytes
HEADER OXYGEN STORAGE/TRANSPORT 30-JAN-02 1KX2
TITLE MINIMIZED AVERAGE STRUCTURE OF A MONO-HEME FERROCYTOCHROME C FROM
TITLE 2 SHEWANELLA PUTREFACIENS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MONO-HEME C-TYPE CYTOCHROME SCYA;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: MONO-HEME FERROCYTOCHROME C;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SHEWANELLA PUTREFACIENS;
SOURCE 3 ORGANISM_TAXID: 24;
SOURCE 4 GENE: SCYA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)C41;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PPB10SCYA
KEYWDS HAEM PROTEIN, FERROCYTOCHROME, ELECTRON TRANSPORT, GRAM NEGATIVE,
KEYWDS 2 BACTERIA, SCYA SHEWANELLA PUTREFACIENS, MONO HAEM, ALL-ALPHA, OXYGEN
KEYWDS 3 STORAGE-TRANSPORT COMPLEX
EXPDTA SOLUTION NMR
MDLTYP MINIMIZED AVERAGE
AUTHOR I.BARTALESI,I.BERTINI,P.HAJIEVA,A.ROSATO,P.R.VASOS
REVDAT 4 23-FEB-22 1KX2 1 REMARK SEQADV LINK
REVDAT 3 24-FEB-09 1KX2 1 VERSN
REVDAT 2 19-JUN-02 1KX2 1 JRNL
REVDAT 1 13-FEB-02 1KX2 0
JRNL AUTH I.BARTALESI,I.BERTINI,P.HAJIEVA,A.ROSATO,P.R.VASOS
JRNL TITL SOLUTION STRUCTURE OF A MONOHEME FERROCYTOCHROME C FROM
JRNL TITL 2 SHEWANELLA PUTREFACIENS AND STRUCTURAL ANALYSIS OF
JRNL TITL 3 SEQUENCE-SIMILAR PROTEINS: FUNCTIONAL IMPLICATIONS.
JRNL REF BIOCHEMISTRY V. 41 5112 2002
JRNL REFN ISSN 0006-2960
JRNL PMID 11955059
JRNL DOI 10.1021/BI015984Z
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA 1.5, AMBER 6
REMARK 3 AUTHORS : GUNTERT, P., MUMENTHALER, C., WUTHRICH, K.
REMARK 3 (DYANA), CASE (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1KX2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-JAN-02.
REMARK 100 THE DEPOSITION ID IS D_1000015428.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.5 MM CYTOCHROME C: 100 MM
REMARK 210 PHOSPHATE BUFFER; REDUCED WITH
REMARK 210 DITHYONITE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_TOCSY; 2D_NOESY; 2D_
REMARK 210 TOCSY; HNHA; HNHB; 15N-HSQC
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 : NULL
REMARK 210 METHOD USED : SIMULATED ANNEALING IN THE
REMARK 210 DIHEDRAL ANGLE SPACE IN DYANA IN
REMARK 210 15000 STEPS; 30 STRUCTURES WITH
REMARK 210 THE LOWEST TARGET FUNCTION OUT
REMARK 210 OF A TOTAL NUMBER OF 250
REMARK 210 GENERATED STRUCTURES CONSTITUTE
REMARK 210 THE REM FAMILY - SUBJECT TO
REMARK 210 RESTRAINED ENERGY MINIMIZATION
REMARK 210 IN AMBER; THE MINIMIZED MEAN IS
REMARK 210 REPORTED
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
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 ALA A 10 -65.98 -101.86
REMARK 500 CYS A 11 47.41 -78.27
REMARK 500 PRO A 33 27.56 -76.50
REMARK 500 ARG A 34 -52.97 -127.49
REMARK 500 VAL A 39 -63.92 -126.33
REMARK 500 ASP A 40 17.65 -68.86
REMARK 500 MET A 58 -4.22 85.69
REMARK 500 THR A 60 -78.81 -80.20
REMARK 500 ASP A 61 32.38 -83.32
REMARK 500 MET A 74 -79.06 -71.69
REMARK 500 SER A 75 43.60 -159.67
REMARK 500 LYS A 76 52.77 36.68
REMARK 500 ALA A 77 -67.33 -145.09
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 TYR A 7 0.09 SIDE CHAIN
REMARK 500 ARG A 34 0.12 SIDE CHAIN
REMARK 500 TYR A 67 0.12 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 90 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 15 NE2
REMARK 620 2 HEC A 90 NA 94.9
REMARK 620 3 HEC A 90 NB 90.7 90.4
REMARK 620 4 HEC A 90 NC 86.7 176.8 92.3
REMARK 620 5 HEC A 90 ND 87.5 88.0 177.5 89.4
REMARK 620 6 MET A 53 SD 168.2 84.0 101.0 93.9 80.8
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 90
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1KX7 RELATED DB: PDB
REMARK 900 30 CONFORMERS ENSEMBLE OF S. PUTREFACIENS MONO-HEME C-TYPE
REMARK 900 CYTOCHROME SCYA
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 RECOMBINANT PROTEIN, WITHOUT THE SIGNALING PEPTIDE.
REMARK 999 THE FIRST THREE AMINO-ACIDS (ALA ASP LEU) HAVE
REMARK 999 BEEN ADDED FOR PROTEIN EXPRESSION PURPOSES.
DBREF 1KX2 A 1 78 UNP O52685 O52685_SHEPU 22 99
SEQADV 1KX2 ALA A -3 UNP O52685 CLONING ARTIFACT
SEQADV 1KX2 ASP A -2 UNP O52685 CLONING ARTIFACT
SEQADV 1KX2 LEU A -1 UNP O52685 CLONING ARTIFACT
SEQRES 1 A 81 ALA ASP LEU GLN ASP ALA GLU ALA ILE TYR ASN LYS ALA
SEQRES 2 A 81 CYS THR VAL CYS HIS SER MET GLY VAL ALA GLY ALA PRO
SEQRES 3 A 81 LYS SER HIS ASN THR ALA ASP TRP GLU PRO ARG LEU ALA
SEQRES 4 A 81 LYS GLY VAL ASP ASN LEU VAL LYS SER VAL LYS THR GLY
SEQRES 5 A 81 LEU ASN ALA MET PRO PRO GLY GLY MET CYS THR ASP CYS
SEQRES 6 A 81 THR ASP GLU ASP TYR LYS ALA ALA ILE GLU PHE MET SER
SEQRES 7 A 81 LYS ALA LYS
HET HEC A 90 75
HETNAM HEC HEME C
FORMUL 2 HEC C34 H34 FE N4 O4
HELIX 1 1 ASP A 2 ALA A 10 1 9
HELIX 2 2 GLY A 18 ALA A 22 5 5
HELIX 3 3 TRP A 31 ALA A 36 1 6
HELIX 4 4 ASN A 41 GLY A 49 1 9
HELIX 5 5 PRO A 54 CYS A 59 5 6
HELIX 6 6 THR A 63 SER A 75 1 13
SSBOND 1 CYS A 59 CYS A 62 1555 1555 2.09
LINK SG CYS A 11 CAB HEC A 90 1555 1555 1.81
LINK SG CYS A 14 CAC HEC A 90 1555 1555 1.82
LINK NE2 HIS A 15 FE HEC A 90 1555 1555 1.97
LINK SD MET A 53 FE HEC A 90 1555 1555 2.37
SITE 1 AC1 13 ALA A 10 CYS A 11 CYS A 14 HIS A 15
SITE 2 AC1 13 ALA A 20 ALA A 22 PRO A 23 ARG A 34
SITE 3 AC1 13 LEU A 42 VAL A 46 MET A 53 GLY A 57
SITE 4 AC1 13 LYS A 78
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
Complete list - 23 20 Bytes