Header list of 1ig6.pdb file
Complete list - b 23 2 Bytes
HEADER DNA BINDING PROTEIN 17-APR-01 1IG6
TITLE HUMAN MRF-2 DOMAIN, NMR, 11 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MODULATOR RECOGNITION FACTOR 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: DNA-BINDING DOMAIN;
COMPND 5 SYNONYM: MRF-2;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: MRF-2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 DE3;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PQE30
KEYWDS DNA BINDING PROTEIN, MRF-2, DNA-BINDING MOTIF, PROTEIN-DNA
KEYWDS 2 INTERACTION
EXPDTA SOLUTION NMR
NUMMDL 11
AUTHOR D.LIN,V.TSUI,D.CASE,Y.C.YUAN,Y.CHEN
REVDAT 4 23-FEB-22 1IG6 1 REMARK
REVDAT 3 24-FEB-09 1IG6 1 VERSN
REVDAT 2 02-MAY-01 1IG6 1 SPRSDE
REVDAT 1 25-APR-01 1IG6 0
SPRSDE 02-MAY-01 1IG6 1BMY
JRNL AUTH D.LIN,V.TSUI,D.CASE,Y.C.YUAN,Y.CHEN
JRNL TITL HUMAN MRF-2 DOMAIN, NMR, 11 STRUCTURES
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH Y.C.YUAN,R.H.WHITSON,Q.LIU,K.ITAKURA,Y.CHEN
REMARK 1 TITL A NOVEL DNA-BINDING MOTIF SHARES STRUCTURAL HOMOLOGY TO DNA
REMARK 1 TITL 2 REPLICATION AND REPAIR NUCLEASES AND POLYMERASES
REMARK 1 REF NAT.STRUCT.BIOL. V. 5 959 1998
REMARK 1 REFN ISSN 1072-8368
REMARK 1 DOI 10.1038/2934
REMARK 1 REFERENCE 2
REMARK 1 AUTH Y.C.YUAN,R.H.WHITSON,K.ITAKURA,Y.CHEN
REMARK 1 TITL RESONANCE ASSIGNMENTS OF THE MRF-2 DNA-BINDING DOMAIN
REMARK 1 REF J.BIOMOL.NMR V. 11 459 1998
REMARK 1 REFN ISSN 0925-2738
REMARK 1 DOI 10.1023/A:1008231900431
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : FELIX 98.0, AMBER 7.0
REMARK 3 AUTHORS : BIOSYM/MSI (FELIX), KOLLMAN, CASE, MERZ, CHEATHAM,
REMARK 3 SIMMERLING, PEARLMAN (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 2478 RESTRAINTS, 2290 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 74
REMARK 3 DIHEDRAL ANGLE RESTRAINTS, 42 DISTANCE RESTRAINTS FROM HYDROGEN
REMARK 3 BONDS, 35 RESIDUAL DIPOLAR COUPLING CONSTANTS.
REMARK 4
REMARK 4 1IG6 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-APR-01.
REMARK 100 THE DEPOSITION ID IS D_1000013244.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.00
REMARK 210 IONIC STRENGTH : 100 MM SODIUM PHOSPHATE
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.7 MM MRF-2 U-15N,13C, 100MM
REMARK 210 PHOSPHATE BUFFER NA, 0.02% NAN3,
REMARK 210 5 MM DDT; 0.7 MM MRF-2 U-15N,13C,
REMARK 210 100MM PHOSPHATE BUFFER NA, 0.02%
REMARK 210 NAN3, 5 MM DDT
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 3D HNHB; 3D_
REMARK 210 15N_TOCSY-HSQC; 3D HCCH-TOCSY;
REMARK 210 2D_PFG-SE-IPAP
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA 1.5, VNMR 6.1
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 11
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY,STRUCTURES
REMARK 210 WITH THE LEAST RESTRAINT
REMARK 210 VIOLATIONS,STRUCTURES WITH THE
REMARK 210 LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING THE RESTRAINTS DERIVED
REMARK 210 FROM NMR EXPERIMENTS (NOE, DIHEDRAL ANGLES, HYDROGEN BONDS,
REMARK 210 RESIDUAL DIPOLAR COUPLING CONSTANTS, ETC.)
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 4 ARG A 90 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 5 ARG A 78 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 6 ARG A 83 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 6 ARG A 90 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 7 ARG A 78 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 8 ARG A 90 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 9 ARG A 54 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 9 ARG A 78 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 11 ARG A 83 NE - CZ - NH1 ANGL. DEV. = 3.3 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 LEU A 28 -71.59 -64.35
REMARK 500 1 ASN A 34 51.97 -141.29
REMARK 500 1 SER A 70 48.23 -141.87
REMARK 500 1 ALA A 74 -44.99 64.87
REMARK 500 1 ILE A 85 -21.91 -158.01
REMARK 500 1 GLU A 95 22.86 -142.03
REMARK 500 1 GLU A 96 -46.40 -151.83
REMARK 500 2 ARG A 18 4.55 -68.84
REMARK 500 2 LYS A 19 34.89 73.92
REMARK 500 2 ILE A 22 -34.23 60.23
REMARK 500 2 LEU A 28 48.47 -97.35
REMARK 500 2 ILE A 33 99.30 -63.69
REMARK 500 2 SER A 70 24.33 -78.15
REMARK 500 2 ILE A 85 -21.78 -164.05
REMARK 500 2 LYS A 93 -15.02 -141.73
REMARK 500 2 GLU A 96 82.62 34.17
REMARK 500 2 LYS A 98 -39.07 -131.93
REMARK 500 2 ILE A 103 29.42 45.12
REMARK 500 3 PRO A 21 22.33 -71.96
REMARK 500 3 ILE A 22 -20.11 62.09
REMARK 500 3 ASN A 34 42.80 -141.60
REMARK 500 3 TYR A 48 -45.82 62.08
REMARK 500 3 ILE A 85 -24.13 -150.77
REMARK 500 3 GLU A 96 48.43 31.42
REMARK 500 3 ASP A 97 30.21 -74.56
REMARK 500 3 ILE A 103 38.11 36.97
REMARK 500 3 LYS A 104 63.33 -155.52
REMARK 500 4 ARG A 18 -77.42 -103.37
REMARK 500 4 LYS A 19 15.44 176.06
REMARK 500 4 PRO A 26 -168.86 -75.98
REMARK 500 4 LEU A 28 36.51 -81.88
REMARK 500 4 PHE A 30 -2.88 -143.42
REMARK 500 4 GLN A 32 37.87 -78.33
REMARK 500 4 ILE A 33 71.12 53.44
REMARK 500 4 ASN A 34 64.47 -69.80
REMARK 500 4 SER A 70 41.75 -79.61
REMARK 500 4 ILE A 85 -23.97 -154.92
REMARK 500 4 GLU A 96 64.96 26.78
REMARK 500 4 LYS A 98 53.45 36.35
REMARK 500 4 PRO A 102 -9.53 -50.73
REMARK 500 4 PRO A 105 170.98 -54.36
REMARK 500 5 PRO A 26 -142.97 -77.05
REMARK 500 5 PHE A 30 -2.18 -144.61
REMARK 500 5 GLN A 32 39.40 -78.92
REMARK 500 5 SER A 70 47.41 -84.09
REMARK 500 5 ILE A 85 -25.35 -157.92
REMARK 500 5 GLU A 96 -43.25 -154.64
REMARK 500 5 LYS A 104 -36.01 -132.94
REMARK 500 5 ARG A 106 28.41 45.66
REMARK 500 6 ARG A 18 -71.15 -128.76
REMARK 500
REMARK 500 THIS ENTRY HAS 110 RAMACHANDRAN OUTLIERS.
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 ARG A 78 0.11 SIDE CHAIN
REMARK 500 8 TYR A 88 0.06 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1BMY RELATED DB: PDB
REMARK 900 1BMY IS LOW QUALITY STRUCTURE OF HUMAN MRF-2 DOMAIN
DBREF 1IG6 A 1 107 UNP Q14865 ARI5B_HUMAN 17 123
SEQRES 1 A 107 ARG ALA ASP GLU GLN ALA PHE LEU VAL ALA LEU TYR LYS
SEQRES 2 A 107 TYR MET LYS GLU ARG LYS THR PRO ILE GLU ARG ILE PRO
SEQRES 3 A 107 TYR LEU GLY PHE LYS GLN ILE ASN LEU TRP THR MET PHE
SEQRES 4 A 107 GLN ALA ALA GLN LYS LEU GLY GLY TYR GLU THR ILE THR
SEQRES 5 A 107 ALA ARG ARG GLN TRP LYS HIS ILE TYR ASP GLU LEU GLY
SEQRES 6 A 107 GLY ASN PRO GLY SER THR SER ALA ALA THR CYS THR ARG
SEQRES 7 A 107 ARG HIS TYR GLU ARG LEU ILE LEU PRO TYR GLU ARG PHE
SEQRES 8 A 107 ILE LYS GLY GLU GLU ASP LYS PRO LEU PRO PRO ILE LYS
SEQRES 9 A 107 PRO ARG LYS
HELIX 1 1 ARG A 1 GLU A 17 1 17
HELIX 2 2 PRO A 21 ILE A 25 5 5
HELIX 3 3 ASN A 34 LEU A 45 1 12
HELIX 4 4 GLY A 46 ARG A 55 1 10
HELIX 5 5 GLN A 56 GLY A 65 1 10
HELIX 6 6 CYS A 76 ILE A 85 1 10
HELIX 7 7 TYR A 88 GLU A 96 1 9
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