Header list of 1pd7.pdb file
Complete list - b 23 2 Bytes
HEADER TRANSCRIPTION 19-MAY-03 1PD7
TITLE EXTENDED SID OF MAD1 BOUND TO THE PAH2 DOMAIN OF MSIN3B
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SIN3B PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PAH2 DOMAIN (RESIDUES 148-232);
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: MAD1;
COMPND 8 CHAIN: B;
COMPND 9 FRAGMENT: EXTENDED SID DOMAIN (RESIDUES 5-28);
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: SIN3;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: PBL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX2T;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN HUMANS.
KEYWDS PAH2, SIN3, MAD1, EUKARYOTIC TRANSCRIPTIONAL REGULATION, PROTEIN-
KEYWDS 2 PROTEIN INTERACTIONS, TRANSCRIPTION
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR H.VAN INGEN,E.LASONDER,J.F.JANSEN,A.M.KAAN,C.A.SPRONK,
AUTHOR 2 H.G.STUNNENBERG,G.W.VUISTER
REVDAT 3 23-FEB-22 1PD7 1 REMARK
REVDAT 2 24-FEB-09 1PD7 1 VERSN
REVDAT 1 20-JAN-04 1PD7 0
JRNL AUTH H.VAN INGEN,E.LASONDER,J.F.JANSEN,A.M.KAAN,C.A.SPRONK,
JRNL AUTH 2 H.G.STUNNENBERG,G.W.VUISTER
JRNL TITL EXTENSION OF THE BINDING MOTIF OF THE SIN3 INTERACTING
JRNL TITL 2 DOMAIN OF THE MAD FAMILY PROTEINS(,).
JRNL REF BIOCHEMISTRY V. 43 46 2004
JRNL REFN ISSN 0006-2960
JRNL PMID 14705930
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 2002, X-PLOR 3.581
REMARK 3 AUTHORS : DELAGLIO (NMRPIPE), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1PD7 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-MAY-03.
REMARK 100 THE DEPOSITION ID IS D_1000019246.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 6.3
REMARK 210 IONIC STRENGTH : 50 MM K2HPO4/KH2PO4
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.3 MM PAH2 U-15,13C; 1.3 MM SID
REMARK 210 50 MM PHOSPHATE BUFFER PH 6.3
REMARK 210 TRACE AMOUNTS OF NAN3 AND
REMARK 210 PEFABLOC
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 2D X-FILTERED
REMARK 210 NOESY; 3D 13C-EDITED-13C-
REMARK 210 FILTERED HMQC-NOESY; 3D 15N-
REMARK 210 EDITED-15N-FILTERED HSQC-NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 750 MHZ; 800
REMARK 210 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY 1.3.9, X-PLOR 3.581
REMARK 210 METHOD USED : SIMULATED ANNEALING, ITERATIVE
REMARK 210 NOE-ASSIGNMENT
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
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: A COLLECTION OF PDB FILES, COMPILED BY NMR_REFINE
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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
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 TYR A 13 CB - CG - CD2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 1 ARG A 20 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 1 ARG A 48 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 1 ARG A 51 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 1 ARG A 67 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 1 ARG B 214 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 2 ARG A 29 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 2 MET A 53 CG - SD - CE ANGL. DEV. = -9.8 DEGREES
REMARK 500 2 ARG A 67 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 3 TYR A 38 CB - CG - CD2 ANGL. DEV. = -5.3 DEGREES
REMARK 500 3 TYR A 38 CB - CG - CD1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 3 ARG A 51 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 3 MET A 53 CG - SD - CE ANGL. DEV. = -14.0 DEGREES
REMARK 500 3 PHE A 66 CB - CG - CD2 ANGL. DEV. = -4.7 DEGREES
REMARK 500 3 PHE A 66 CB - CG - CD1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 4 TYR A 13 CB - CG - CD2 ANGL. DEV. = -4.7 DEGREES
REMARK 500 4 ARG A 20 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 4 MET A 53 CG - SD - CE ANGL. DEV. = -11.1 DEGREES
REMARK 500 4 PHE A 66 CB - CG - CD1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 4 ARG B 214 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 4 ARG B 214 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 5 ARG A 29 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 5 TYR A 38 CB - CG - CD2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 5 PHE A 66 CB - CG - CD1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 6 PHE A 7 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 6 TYR A 38 CB - CG - CD2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 6 ARG A 51 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 6 MET A 53 CG - SD - CE ANGL. DEV. = -10.3 DEGREES
REMARK 500 6 ARG B 199 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 6 ARG B 214 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 6 ARG B 215 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 7 TYR A 13 CB - CG - CD2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 7 ARG A 20 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 7 MET A 53 CG - SD - CE ANGL. DEV. = -9.7 DEGREES
REMARK 500 7 ARG B 214 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 7 ARG B 217 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 8 ARG A 29 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 8 TYR A 38 CB - CG - CD2 ANGL. DEV. = -6.7 DEGREES
REMARK 500 8 TYR A 38 CB - CG - CD1 ANGL. DEV. = 5.2 DEGREES
REMARK 500 8 ARG A 48 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 8 PHE A 50 CB - CG - CD1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 8 MET A 53 CG - SD - CE ANGL. DEV. = -13.3 DEGREES
REMARK 500 8 ARG A 85 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 9 TYR A 13 CB - CG - CD2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 9 MET A 53 CG - SD - CE ANGL. DEV. = -11.8 DEGREES
REMARK 500 9 PHE A 66 CB - CG - CD2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 9 PHE A 66 CB - CG - CD1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 9 PHE A 76 CB - CG - CD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 9 PHE A 76 CB - CG - CD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 9 ARG B 215 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 166 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 SER A 2 123.68 83.10
REMARK 500 1 SER A 4 26.11 -142.42
REMARK 500 1 LYS A 46 56.21 -110.70
REMARK 500 1 MET A 53 -147.65 -141.30
REMARK 500 1 ARG A 67 127.51 -35.34
REMARK 500 1 GLU A 82 -87.28 -100.90
REMARK 500 1 LYS A 84 65.81 72.27
REMARK 500 2 SER A 4 33.20 -76.63
REMARK 500 2 PHE A 21 47.88 -84.34
REMARK 500 2 LEU A 43 35.67 70.67
REMARK 500 2 PHE A 50 -77.25 -99.95
REMARK 500 2 MET A 53 -132.02 20.66
REMARK 500 2 ARG A 67 95.37 25.91
REMARK 500 2 LEU A 80 -82.14 -42.35
REMARK 500 2 ALA A 83 91.50 -165.09
REMARK 500 2 ARG B 199 156.49 72.42
REMARK 500 2 ASN B 201 -178.71 -173.71
REMARK 500 3 ASP A 3 -69.09 -120.04
REMARK 500 3 PHE A 21 44.21 -89.78
REMARK 500 3 LEU A 43 -139.69 53.23
REMARK 500 3 MET A 53 -134.51 44.73
REMARK 500 3 ALA A 83 46.11 -141.39
REMARK 500 4 SER A 2 177.36 75.74
REMARK 500 4 PHE A 21 44.28 -82.07
REMARK 500 4 LEU A 43 -75.42 63.68
REMARK 500 4 HIS A 44 12.65 -146.52
REMARK 500 4 PHE A 50 -132.31 -93.05
REMARK 500 4 ARG A 51 -109.70 -125.04
REMARK 500 4 MET A 53 -156.15 -73.36
REMARK 500 4 ARG A 67 121.90 -38.13
REMARK 500 4 ALA A 83 -78.82 -152.10
REMARK 500 4 LYS A 84 63.33 -150.14
REMARK 500 4 ARG B 199 62.80 -114.27
REMARK 500 5 SER A 2 -173.25 77.49
REMARK 500 5 ASP A 3 -82.98 -77.33
REMARK 500 5 SER A 4 88.22 75.11
REMARK 500 5 PHE A 21 42.07 -89.11
REMARK 500 5 PHE A 50 -86.03 -122.84
REMARK 500 5 MET A 53 -123.97 -92.28
REMARK 500 5 LEU A 80 -82.64 -64.77
REMARK 500 5 GLU A 82 -99.44 -85.91
REMARK 500 5 LYS A 84 61.41 63.10
REMARK 500 5 ARG B 199 137.82 67.34
REMARK 500 5 ASN B 201 -156.15 -104.08
REMARK 500 6 ARG A 48 76.08 23.70
REMARK 500 6 PHE A 50 120.13 63.18
REMARK 500 6 ARG A 51 -77.21 -159.69
REMARK 500 6 MET A 53 -133.14 46.28
REMARK 500 6 ARG A 67 123.90 -39.19
REMARK 500 6 ALA A 83 -51.29 -150.00
REMARK 500
REMARK 500 THIS ENTRY HAS 258 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 PHE A 79 LEU A 80 2 -149.68
REMARK 500 GLY A 52 MET A 53 8 -149.13
REMARK 500 PHE A 79 LEU A 80 9 -148.94
REMARK 500 MET A 53 SER A 54 14 149.18
REMARK 500 PHE A 79 LEU A 80 14 -149.51
REMARK 500 GLY A 52 MET A 53 19 149.93
REMARK 500 MET A 53 SER A 54 20 148.15
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 48 0.14 SIDE CHAIN
REMARK 500 2 TYR B 211 0.06 SIDE CHAIN
REMARK 500 3 TYR A 38 0.07 SIDE CHAIN
REMARK 500 3 ARG B 215 0.08 SIDE CHAIN
REMARK 500 4 ARG A 29 0.11 SIDE CHAIN
REMARK 500 4 ARG A 85 0.10 SIDE CHAIN
REMARK 500 4 ARG B 199 0.09 SIDE CHAIN
REMARK 500 5 ARG A 67 0.09 SIDE CHAIN
REMARK 500 6 ARG A 29 0.10 SIDE CHAIN
REMARK 500 7 ARG A 48 0.08 SIDE CHAIN
REMARK 500 7 ARG B 217 0.11 SIDE CHAIN
REMARK 500 8 TYR A 28 0.07 SIDE CHAIN
REMARK 500 8 ARG A 29 0.08 SIDE CHAIN
REMARK 500 8 ARG A 48 0.08 SIDE CHAIN
REMARK 500 8 ARG A 67 0.18 SIDE CHAIN
REMARK 500 9 ARG A 51 0.18 SIDE CHAIN
REMARK 500 9 ARG A 85 0.08 SIDE CHAIN
REMARK 500 10 ARG B 217 0.10 SIDE CHAIN
REMARK 500 12 TYR A 38 0.08 SIDE CHAIN
REMARK 500 12 ARG B 199 0.15 SIDE CHAIN
REMARK 500 14 ARG B 215 0.08 SIDE CHAIN
REMARK 500 16 ARG A 29 0.15 SIDE CHAIN
REMARK 500 16 TYR A 38 0.08 SIDE CHAIN
REMARK 500 16 ARG A 51 0.11 SIDE CHAIN
REMARK 500 16 ARG A 85 0.11 SIDE CHAIN
REMARK 500 16 ARG B 214 0.15 SIDE CHAIN
REMARK 500 17 ARG A 29 0.07 SIDE CHAIN
REMARK 500 17 ARG B 217 0.10 SIDE CHAIN
REMARK 500 18 TYR A 38 0.08 SIDE CHAIN
REMARK 500 18 ARG A 48 0.14 SIDE CHAIN
REMARK 500 18 ARG A 51 0.09 SIDE CHAIN
REMARK 500 19 ARG A 29 0.09 SIDE CHAIN
REMARK 500 19 ARG A 85 0.09 SIDE CHAIN
REMARK 500 19 ARG B 215 0.09 SIDE CHAIN
REMARK 500 20 ARG A 85 0.08 SIDE CHAIN
REMARK 500 21 TYR A 13 0.08 SIDE CHAIN
REMARK 500 21 TYR A 38 0.12 SIDE CHAIN
REMARK 500 21 ARG A 85 0.14 SIDE CHAIN
REMARK 500 21 ARG B 215 0.10 SIDE CHAIN
REMARK 500 21 ARG B 217 0.08 SIDE CHAIN
REMARK 500 22 ARG A 20 0.10 SIDE CHAIN
REMARK 500 22 ARG B 214 0.14 SIDE CHAIN
REMARK 500 23 ARG A 29 0.09 SIDE CHAIN
REMARK 500 24 ARG A 85 0.12 SIDE CHAIN
REMARK 500 25 ARG A 20 0.08 SIDE CHAIN
REMARK 500 26 TYR A 13 0.11 SIDE CHAIN
REMARK 500 26 ARG B 217 0.12 SIDE CHAIN
REMARK 500 27 ARG A 29 0.18 SIDE CHAIN
REMARK 500 27 ARG A 85 0.08 SIDE CHAIN
REMARK 500 28 ARG A 48 0.08 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 55 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1E91 RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF MINIMAL SID OF MAD1 BOUND TO PAH2 DOMAIN OF MSIN3B
REMARK 900 RELATED ID: 1G1E RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF MINIMAL SID OF MAD1 BOUND TO PAH2 DOMAIN OF MSIN3A
REMARK 900 RELATED ID: 5457 RELATED DB: BMRB
REMARK 900 COMPLETE 1H CHEMICAL SHIFT ASSIGNMENT OF THE EXTENDED SID OF MAD1
REMARK 900 BOUND TO THE PAH2 DOMAIN OF MSIN3B
DBREF 1PD7 A 1 85 UNP Q62141 SIN3B_MOUSE 148 232
DBREF 1PD7 B 198 221 UNP Q05195 MAD_HUMAN 5 28
SEQRES 1 A 85 GLU SER ASP SER VAL GLU PHE ASN ASN ALA ILE SER TYR
SEQRES 2 A 85 VAL ASN LYS ILE LYS THR ARG PHE LEU ASP HIS PRO GLU
SEQRES 3 A 85 ILE TYR ARG SER PHE LEU GLU ILE LEU HIS THR TYR GLN
SEQRES 4 A 85 LYS GLU GLN LEU HIS THR LYS GLY ARG PRO PHE ARG GLY
SEQRES 5 A 85 MET SER GLU GLU GLU VAL PHE THR GLU VAL ALA ASN LEU
SEQRES 6 A 85 PHE ARG GLY GLN GLU ASP LEU LEU SER GLU PHE GLY GLN
SEQRES 7 A 85 PHE LEU PRO GLU ALA LYS ARG
SEQRES 1 B 24 VAL ARG MET ASN ILE GLN MET LEU LEU GLU ALA ALA ASP
SEQRES 2 B 24 TYR LEU GLU ARG ARG GLU ARG GLU ALA GLU HIS
HELIX 1 1 SER A 4 PHE A 21 1 18
HELIX 2 2 GLU A 26 LYS A 40 1 15
HELIX 3 3 LYS A 40 THR A 45 1 6
HELIX 4 4 SER A 54 ARG A 67 1 14
HELIX 5 5 GLN A 69 GLY A 77 1 9
HELIX 6 6 ILE B 202 HIS B 221 1 20
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