Header list of 1ig4.pdb file
Complete list - b 23 2 Bytes
HEADER TRANSCRIPTION/DNA 17-APR-01 1IG4
TITLE SOLUTION STRUCTURE OF THE METHYL-CPG-BINDING DOMAIN OF HUMAN MBD1 IN
TITLE 2 COMPLEX WITH METHYLATED DNA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 5'-D(*GP*TP*AP*TP*CP*(5CM)P*GP*GP*AP*TP*AP*C)-3';
COMPND 3 CHAIN: B, C;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: METHYL-CPG BINDING PROTEIN;
COMPND 7 CHAIN: A;
COMPND 8 FRAGMENT: METHYL-CPG-BINDING DOMAIN;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 MOL_ID: 2;
SOURCE 4 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 5 ORGANISM_COMMON: HUMAN;
SOURCE 6 ORGANISM_TAXID: 9606;
SOURCE 7 GENE: MBD1;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 10 EXPRESSION_SYSTEM_STRAIN: DH5A;
SOURCE 11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PGEX-2T
KEYWDS PROTEIN-DNA COMPLEX, ALPHA-BETA, DOUBLE HELIX, RECOGNITION VIA BETA-
KEYWDS 2 SHEET, TRANSCRIPTION-DNA COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR I.OHKI,N.SHIMOTAKE,N.FUJITA,J.-G.JEE,T.IKEGAMI,M.NAKAO,M.SHIRAKAWA
REVDAT 4 23-FEB-22 1IG4 1 REMARK LINK
REVDAT 3 24-FEB-09 1IG4 1 VERSN
REVDAT 2 01-APR-03 1IG4 1 JRNL
REVDAT 1 30-MAY-01 1IG4 0
JRNL AUTH I.OHKI,N.SHIMOTAKE,N.FUJITA,J.JEE,T.IKEGAMI,M.NAKAO,
JRNL AUTH 2 M.SHIRAKAWA
JRNL TITL SOLUTION STRUCTURE OF THE METHYL-CPG BINDING DOMAIN OF HUMAN
JRNL TITL 2 MBD1 IN COMPLEX WITH METHYLATED DNA.
JRNL REF CELL(CAMBRIDGE,MASS.) V. 105 487 2001
JRNL REFN ISSN 0092-8674
JRNL PMID 11371345
JRNL DOI 10.1016/S0092-8674(01)00324-5
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH I.OHKI,N.SHIMOTAKE,N.FUJITA,M.NAKAO,M.SHIRAKAWA
REMARK 1 TITL SOLUTION STRUCTURE OF THE METHYL-CPG-BINDING DOMAIN OF THE
REMARK 1 TITL 2 METHYLATION-DEPENDENT TRANSCRIPTIONAL REPRESSOR MBD1
REMARK 1 REF EMBO J. V. 18 6653 1999
REMARK 1 REFN ISSN 0261-4189
REMARK 1 DOI 10.1093/EMBOJ/18.23.6653
REMARK 1 REFERENCE 2
REMARK 1 AUTH S.H.CROSS,R.R.MEEHAN,X.NAN,A.BIRD
REMARK 1 TITL A COMPONENT OF THE TRANSCRIPTIONAL REPRESSOR MECP1 SHARES A
REMARK 1 TITL 2 MOTIF WITH DNA METHYLTRANSFERASE AND HRX PROTEINS
REMARK 1 REF NAT.GENET. V. 16 256 1997
REMARK 1 REFN ISSN 1061-4036
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 1.8, X-PLOR 3.8
REMARK 3 AUTHORS : DELAGLIO (NMRPIPE), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURE WAS DETERMINED FROM A
REMARK 3 TOTAL OF 2,022 DISTANCE AND DIHEDRAL ANGLE RESTRAINTS, INCLUDING
REMARK 3 91 INTERMOLECULAR NOE RESTRAINTS.
REMARK 4
REMARK 4 1IG4 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-APR-01.
REMARK 100 THE DEPOSITION ID IS D_1000013242.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : 1.3MM MBD1(U-15N,13C)-DNA
REMARK 210 COMPLEX; 20MM PHOSPHATE BUFFER;
REMARK 210 1.3MM MBD1(U-15N,13C)-DNA
REMARK 210 COMPLEX; 20MM PHOSPHATE BUFFER;
REMARK 210 1MM MBD1(U-15N)-DNA COMPLEX;
REMARK 210 20MM PHOSPHATE BUFFER
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 4D_13C/15N-SEPARATED_NOESY;
REMARK 210 4D_13C-SEPARATED_NOESY; 3D_15N-SEPARATED_NOESY; 3D_13C-FILTERED_
REMARK 210 13C-SEPARATED_NOESY; HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : PIPP 4.0.4, NMRVIEW 4
REMARK 210 METHOD USED : STRUCTURE CALCULATIONS WERE
REMARK 210 PERFORMED FOLLOWING SIMULATED
REMARK 210 ANNEALING PROTOCOLS USING X-PLOR.
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
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 : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING MULTI-DIMENSIONAL
REMARK 210 HETERONUCLEAR TECHNIQUES.
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: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C, 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: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OP2 DG B 107 H THR A 27 1.33
REMARK 500 H3' DC C 117 OG SER A 45 1.48
REMARK 500 H SER A 37 O ASP A 41 1.55
REMARK 500
REMARK 500 REMARK: NULL
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 DG B 101 O4' - C1' - N9 ANGL. DEV. = 2.6 DEGREES
REMARK 500 1 DG B 101 N7 - C8 - N9 ANGL. DEV. = 4.7 DEGREES
REMARK 500 1 DG B 101 C8 - N9 - C4 ANGL. DEV. = -2.6 DEGREES
REMARK 500 1 DT B 102 O4' - C1' - N1 ANGL. DEV. = 2.2 DEGREES
REMARK 500 1 DA B 103 O4' - C1' - N9 ANGL. DEV. = 2.6 DEGREES
REMARK 500 1 DA B 103 N7 - C8 - N9 ANGL. DEV. = 3.9 DEGREES
REMARK 500 1 DT B 104 O4' - C1' - N1 ANGL. DEV. = 2.4 DEGREES
REMARK 500 1 DC B 105 O4' - C1' - N1 ANGL. DEV. = 2.7 DEGREES
REMARK 500 1 DG B 107 O4' - C1' - N9 ANGL. DEV. = 2.9 DEGREES
REMARK 500 1 DG B 107 N7 - C8 - N9 ANGL. DEV. = 4.7 DEGREES
REMARK 500 1 DG B 107 C8 - N9 - C4 ANGL. DEV. = -2.5 DEGREES
REMARK 500 1 DG B 108 O4' - C1' - N9 ANGL. DEV. = 2.8 DEGREES
REMARK 500 1 DG B 108 N7 - C8 - N9 ANGL. DEV. = 4.6 DEGREES
REMARK 500 1 DG B 108 C8 - N9 - C4 ANGL. DEV. = -2.5 DEGREES
REMARK 500 1 DA B 109 O4' - C1' - N9 ANGL. DEV. = 2.4 DEGREES
REMARK 500 1 DA B 109 N7 - C8 - N9 ANGL. DEV. = 4.0 DEGREES
REMARK 500 1 DT B 110 O4' - C1' - N1 ANGL. DEV. = 2.4 DEGREES
REMARK 500 1 DA B 111 O4' - C1' - N9 ANGL. DEV. = 2.8 DEGREES
REMARK 500 1 DA B 111 N7 - C8 - N9 ANGL. DEV. = 3.8 DEGREES
REMARK 500 1 DC B 112 O4' - C1' - N1 ANGL. DEV. = 2.6 DEGREES
REMARK 500 1 DG C 113 O4' - C1' - N9 ANGL. DEV. = 2.5 DEGREES
REMARK 500 1 DG C 113 N7 - C8 - N9 ANGL. DEV. = 4.6 DEGREES
REMARK 500 1 DG C 113 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500 1 DT C 114 O4' - C1' - N1 ANGL. DEV. = 2.2 DEGREES
REMARK 500 1 DA C 115 O4' - C1' - N9 ANGL. DEV. = 2.6 DEGREES
REMARK 500 1 DA C 115 N7 - C8 - N9 ANGL. DEV. = 3.9 DEGREES
REMARK 500 1 DT C 116 O4' - C1' - N1 ANGL. DEV. = 2.6 DEGREES
REMARK 500 1 DC C 117 O4' - C1' - N1 ANGL. DEV. = 2.8 DEGREES
REMARK 500 1 DG C 119 O4' - C1' - N9 ANGL. DEV. = 2.8 DEGREES
REMARK 500 1 DG C 119 N7 - C8 - N9 ANGL. DEV. = 4.7 DEGREES
REMARK 500 1 DG C 119 C8 - N9 - C4 ANGL. DEV. = -2.5 DEGREES
REMARK 500 1 DG C 120 O4' - C1' - N9 ANGL. DEV. = 2.6 DEGREES
REMARK 500 1 DG C 120 N7 - C8 - N9 ANGL. DEV. = 4.7 DEGREES
REMARK 500 1 DG C 120 C8 - N9 - C4 ANGL. DEV. = -2.5 DEGREES
REMARK 500 1 DA C 121 O4' - C1' - N9 ANGL. DEV. = 2.5 DEGREES
REMARK 500 1 DA C 121 N7 - C8 - N9 ANGL. DEV. = 4.0 DEGREES
REMARK 500 1 DT C 122 O4' - C1' - N1 ANGL. DEV. = 2.5 DEGREES
REMARK 500 1 DA C 123 O4' - C1' - N9 ANGL. DEV. = 2.7 DEGREES
REMARK 500 1 DA C 123 N7 - C8 - N9 ANGL. DEV. = 4.0 DEGREES
REMARK 500 1 DC C 124 O4' - C1' - N1 ANGL. DEV. = 2.7 DEGREES
REMARK 500 2 DG B 101 O4' - C1' - N9 ANGL. DEV. = 2.5 DEGREES
REMARK 500 2 DG B 101 N7 - C8 - N9 ANGL. DEV. = 4.6 DEGREES
REMARK 500 2 DG B 101 C8 - N9 - C4 ANGL. DEV. = -2.6 DEGREES
REMARK 500 2 DT B 102 O4' - C1' - N1 ANGL. DEV. = 2.3 DEGREES
REMARK 500 2 DA B 103 O4' - C1' - N9 ANGL. DEV. = 2.7 DEGREES
REMARK 500 2 DA B 103 N7 - C8 - N9 ANGL. DEV. = 4.0 DEGREES
REMARK 500 2 DT B 104 O4' - C1' - N1 ANGL. DEV. = 2.3 DEGREES
REMARK 500 2 DC B 105 O4' - C1' - N1 ANGL. DEV. = 2.7 DEGREES
REMARK 500 2 DG B 107 O4' - C1' - N9 ANGL. DEV. = 2.9 DEGREES
REMARK 500 2 DG B 107 N7 - C8 - N9 ANGL. DEV. = 4.6 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 796 ANGLE DEVIATIONS.
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 ALA A 2 80.06 52.68
REMARK 500 1 ASP A 4 92.10 -169.39
REMARK 500 1 ASP A 7 170.54 -58.07
REMARK 500 1 CYS A 8 87.75 -150.15
REMARK 500 1 LEU A 11 -68.95 -127.32
REMARK 500 1 ARG A 22 -179.94 48.59
REMARK 500 1 LYS A 23 -38.40 -139.17
REMARK 500 1 SER A 24 -166.06 167.70
REMARK 500 1 ALA A 26 -41.92 -147.81
REMARK 500 1 SER A 37 -177.87 -54.15
REMARK 500 1 THR A 39 14.90 -161.09
REMARK 500 1 ASP A 41 128.79 172.74
REMARK 500 1 PRO A 72 -83.79 -73.33
REMARK 500 1 PRO A 74 -78.64 -73.22
REMARK 500 2 ASP A 4 120.64 62.38
REMARK 500 2 PHE A 21 45.32 -83.05
REMARK 500 2 ARG A 22 168.31 51.75
REMARK 500 2 LYS A 23 -30.81 -134.79
REMARK 500 2 SER A 24 -165.86 164.28
REMARK 500 2 ALA A 26 -40.23 -176.38
REMARK 500 2 CYS A 28 131.32 -39.64
REMARK 500 2 SER A 37 -175.58 -53.47
REMARK 500 2 THR A 39 44.59 -179.20
REMARK 500 2 ASP A 41 -153.32 -116.69
REMARK 500 2 ASP A 58 174.30 -51.32
REMARK 500 2 LEU A 59 62.77 -151.78
REMARK 500 2 PHE A 64 -76.91 57.43
REMARK 500 2 CYS A 70 82.30 -57.83
REMARK 500 2 PRO A 72 -80.66 -71.35
REMARK 500 3 ALA A 2 55.50 -146.44
REMARK 500 3 ASP A 4 92.82 62.03
REMARK 500 3 LEU A 11 -66.84 -126.53
REMARK 500 3 PHE A 21 37.90 -86.09
REMARK 500 3 ARG A 22 162.34 51.54
REMARK 500 3 SER A 24 -170.29 166.39
REMARK 500 3 ALA A 26 -38.76 177.94
REMARK 500 3 SER A 37 -175.47 -54.99
REMARK 500 3 THR A 39 47.19 -168.20
REMARK 500 3 ASP A 41 108.73 165.09
REMARK 500 3 SER A 45 -162.70 -163.34
REMARK 500 3 TYR A 71 88.79 51.49
REMARK 500 4 GLU A 3 -61.00 63.39
REMARK 500 4 ASP A 4 128.01 62.86
REMARK 500 4 ARG A 22 175.08 50.22
REMARK 500 4 LYS A 23 -41.36 -140.48
REMARK 500 4 SER A 24 -166.96 174.48
REMARK 500 4 ALA A 26 -43.88 -166.35
REMARK 500 4 SER A 37 -177.75 -54.60
REMARK 500 4 THR A 39 46.76 -165.91
REMARK 500 4 ASP A 41 113.73 165.69
REMARK 500
REMARK 500 THIS ENTRY HAS 279 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 1 ARG A 17 0.23 SIDE CHAIN
REMARK 500 1 ARG A 18 0.21 SIDE CHAIN
REMARK 500 1 ARG A 22 0.30 SIDE CHAIN
REMARK 500 1 ARG A 30 0.27 SIDE CHAIN
REMARK 500 1 ARG A 42 0.32 SIDE CHAIN
REMARK 500 1 ARG A 44 0.23 SIDE CHAIN
REMARK 500 1 ARG A 51 0.30 SIDE CHAIN
REMARK 500 2 ARG A 17 0.32 SIDE CHAIN
REMARK 500 2 ARG A 18 0.21 SIDE CHAIN
REMARK 500 2 ARG A 22 0.31 SIDE CHAIN
REMARK 500 2 ARG A 30 0.28 SIDE CHAIN
REMARK 500 2 ARG A 42 0.23 SIDE CHAIN
REMARK 500 2 ARG A 44 0.26 SIDE CHAIN
REMARK 500 2 ARG A 51 0.23 SIDE CHAIN
REMARK 500 3 ARG A 17 0.23 SIDE CHAIN
REMARK 500 3 ARG A 18 0.23 SIDE CHAIN
REMARK 500 3 ARG A 22 0.32 SIDE CHAIN
REMARK 500 3 ARG A 30 0.29 SIDE CHAIN
REMARK 500 3 ARG A 42 0.32 SIDE CHAIN
REMARK 500 3 ARG A 44 0.30 SIDE CHAIN
REMARK 500 3 ARG A 51 0.19 SIDE CHAIN
REMARK 500 4 ARG A 17 0.29 SIDE CHAIN
REMARK 500 4 ARG A 18 0.22 SIDE CHAIN
REMARK 500 4 ARG A 22 0.31 SIDE CHAIN
REMARK 500 4 ARG A 30 0.27 SIDE CHAIN
REMARK 500 4 ARG A 42 0.31 SIDE CHAIN
REMARK 500 4 ARG A 44 0.22 SIDE CHAIN
REMARK 500 4 ARG A 51 0.26 SIDE CHAIN
REMARK 500 5 ARG A 17 0.22 SIDE CHAIN
REMARK 500 5 ARG A 18 0.17 SIDE CHAIN
REMARK 500 5 ARG A 22 0.31 SIDE CHAIN
REMARK 500 5 ARG A 30 0.21 SIDE CHAIN
REMARK 500 5 ARG A 42 0.27 SIDE CHAIN
REMARK 500 5 ARG A 44 0.26 SIDE CHAIN
REMARK 500 5 ARG A 51 0.23 SIDE CHAIN
REMARK 500 6 ARG A 17 0.22 SIDE CHAIN
REMARK 500 6 ARG A 22 0.31 SIDE CHAIN
REMARK 500 6 ARG A 30 0.27 SIDE CHAIN
REMARK 500 6 ARG A 42 0.23 SIDE CHAIN
REMARK 500 6 ARG A 44 0.23 SIDE CHAIN
REMARK 500 6 ARG A 51 0.28 SIDE CHAIN
REMARK 500 7 ARG A 17 0.21 SIDE CHAIN
REMARK 500 7 ARG A 18 0.25 SIDE CHAIN
REMARK 500 7 ARG A 22 0.31 SIDE CHAIN
REMARK 500 7 ARG A 30 0.23 SIDE CHAIN
REMARK 500 7 ARG A 42 0.25 SIDE CHAIN
REMARK 500 7 ARG A 44 0.26 SIDE CHAIN
REMARK 500 7 ARG A 51 0.28 SIDE CHAIN
REMARK 500 8 ARG A 17 0.30 SIDE CHAIN
REMARK 500 8 ARG A 18 0.20 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 138 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1IG4 A 1 75 UNP Q9UIS9 MBD1_HUMAN 1 75
DBREF 1IG4 B 101 112 PDB 1IG4 1IG4 101 112
DBREF 1IG4 C 113 124 PDB 1IG4 1IG4 113 124
SEQRES 1 B 12 DG DT DA DT DC 5CM DG DG DA DT DA DC
SEQRES 1 C 12 DG DT DA DT DC 5CM DG DG DA DT DA DC
SEQRES 1 A 75 MET ALA GLU ASP TRP LEU ASP CYS PRO ALA LEU GLY PRO
SEQRES 2 A 75 GLY TRP LYS ARG ARG GLU VAL PHE ARG LYS SER GLY ALA
SEQRES 3 A 75 THR CYS GLY ARG SER ASP THR TYR TYR GLN SER PRO THR
SEQRES 4 A 75 GLY ASP ARG ILE ARG SER LYS VAL GLU LEU THR ARG TYR
SEQRES 5 A 75 LEU GLY PRO ALA CYS ASP LEU THR LEU PHE ASP PHE LYS
SEQRES 6 A 75 GLN GLY ILE LEU CYS TYR PRO ALA PRO LYS
MODRES 1IG4 5CM B 106 DC
MODRES 1IG4 5CM C 118 DC
HET 5CM B 106 33
HET 5CM C 118 33
HETNAM 5CM 5-METHYL-2'-DEOXY-CYTIDINE-5'-MONOPHOSPHATE
FORMUL 1 5CM 2(C10 H16 N3 O7 P)
HELIX 1 1 SER A 45 GLY A 54 1 10
SHEET 1 A 4 TRP A 5 ASP A 7 0
SHEET 2 A 4 LYS A 16 VAL A 20 -1 N ARG A 17 O LEU A 6
SHEET 3 A 4 ASP A 32 GLN A 36 -1 N ASP A 32 O VAL A 20
SHEET 4 A 4 ARG A 42 ILE A 43 -1 O ILE A 43 N TYR A 35
LINK O3' DC B 105 P 5CM B 106 1555 1555 1.61
LINK O3' 5CM B 106 P DG B 107 1555 1555 1.61
LINK O3' DC C 117 P 5CM C 118 1555 1555 1.61
LINK O3' 5CM C 118 P DG C 119 1555 1555 1.61
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