Header list of 1sq8.pdb file
Complete list - r 2 2 Bytes
HEADER DNA BINDING PROTEIN 18-MAR-04 1SQ8
TITLE A VARIANT 434 REPRESSOR DNA BINDING DOMAIN DEVOID OF HYDROXYL GROUPS,
TITLE 2 NMR, 20 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DH434;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: VARIANT 434 REPRESSOR DNA-BINDING DOMAIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PHAGE 434;
SOURCE 3 ORGANISM_TAXID: 10712;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PT7-7GFC
KEYWDS HELIX-TURN-HELIX, DNA BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR H.IWAI,G.WIDER,K.WUTHRICH
REVDAT 3 02-MAR-22 1SQ8 1 REMARK
REVDAT 2 24-FEB-09 1SQ8 1 VERSN
REVDAT 1 20-JUL-04 1SQ8 0
JRNL AUTH H.IWAI,G.WIDER,K.WUTHRICH
JRNL TITL NMR STRUCTURE OF A VARIANT 434 REPRESSOR DNA-BINDING DOMAIN
JRNL TITL 2 DEVOID OF HYDROXYL GROUPS
JRNL REF J.BIOMOL.NMR V. 29 395 2004
JRNL REFN ISSN 0925-2738
JRNL PMID 15213439
JRNL DOI 10.1023/B:JNMR.0000032609.72759.41
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA 1.2, OPAL
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1SQ8 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-MAR-04.
REMARK 100 THE DEPOSITION ID IS D_1000021910.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 286
REMARK 210 PH : 4.8
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 5MM DH434, UNLABELED; 25MM
REMARK 210 POTASSIUM PHOSPHATE BUFFER
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 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 1 ARG A 10 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 1 ARG A 10 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 2 ARG A 10 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 3 ARG A 10 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 4 ARG A 10 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 5 ARG A 10 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 5 ARG A 10 NE - CZ - NH2 ANGL. DEV. = -4.9 DEGREES
REMARK 500 6 ARG A 5 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 7 ARG A 10 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 7 ARG A 10 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 8 ARG A 10 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 9 ARG A 10 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 11 ARG A 10 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 12 ARG A 10 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 12 ARG A 10 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 14 ARG A 10 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 17 ARG A 10 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 18 ARG A 10 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 19 ARG A 10 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 19 ARG A 10 NE - CZ - NH2 ANGL. DEV. = -3.0 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 LYS A 40 -76.18 -76.62
REMARK 500 2 LEU A 1 -176.26 85.94
REMARK 500 2 LYS A 40 -66.67 -125.38
REMARK 500 4 LYS A 40 -76.36 -76.38
REMARK 500 5 ARG A 43 4.21 -60.77
REMARK 500 6 PHE A 44 7.05 -69.07
REMARK 500 7 LYS A 40 -72.35 -77.50
REMARK 500 10 LYS A 40 -70.71 -95.83
REMARK 500 10 ASN A 61 -72.89 -98.96
REMARK 500 11 LYS A 40 -72.51 -73.06
REMARK 500 13 LEU A 1 -163.42 83.04
REMARK 500 14 LEU A 1 -172.92 86.73
REMARK 500 15 LYS A 40 -70.43 -122.89
REMARK 500 15 ASN A 61 -73.36 -102.52
REMARK 500 16 LYS A 40 -63.22 -131.33
REMARK 500 17 LYS A 40 -72.19 -122.58
REMARK 500 19 ASN A 61 -76.67 -85.56
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 ARG A 7 0.08 SIDE CHAIN
REMARK 500 4 ARG A 5 0.08 SIDE CHAIN
REMARK 500 4 ARG A 9 0.08 SIDE CHAIN
REMARK 500 6 ARG A 9 0.08 SIDE CHAIN
REMARK 500 8 ARG A 9 0.10 SIDE CHAIN
REMARK 500 9 ARG A 41 0.08 SIDE CHAIN
REMARK 500 11 ARG A 7 0.15 SIDE CHAIN
REMARK 500 12 ARG A 43 0.08 SIDE CHAIN
REMARK 500 15 ARG A 41 0.07 SIDE CHAIN
REMARK 500 17 ARG A 5 0.12 SIDE CHAIN
REMARK 500 18 ARG A 5 0.13 SIDE CHAIN
REMARK 500 18 ARG A 50 0.08 SIDE CHAIN
REMARK 500 20 ARG A 9 0.08 SIDE CHAIN
REMARK 500 20 ARG A 10 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1SQ8 A 10 62 UNP P16117 RPC1_BP434 10 62
SEQRES 1 A 64 MET LEU MET GLY GLU ARG ILE ARG ALA ARG ARG ILE GLN
SEQRES 2 A 64 LEU GLY LEU ASN GLN ALA GLU LEU ALA GLN LYS VAL GLY
SEQRES 3 A 64 VAL ASP GLN GLN ALA ILE GLU GLN LEU GLU ASN GLY LYS
SEQRES 4 A 64 ALA LYS ARG PRO ARG PHE LEU PRO GLU LEU ALA ARG ALA
SEQRES 5 A 64 LEU GLY VAL ALA VAL ASP TRP LEU LEU ASN GLY ALA
HELIX 1 1 LEU A 1 LEU A 13 1 13
HELIX 2 2 ASN A 16 GLY A 25 1 10
HELIX 3 3 ASP A 27 ASN A 36 1 10
HELIX 4 4 PHE A 44 GLY A 53 1 10
HELIX 5 5 ALA A 55 ASN A 61 1 7
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 - r 2 2 Bytes