Header list of 1g1e.pdb file
Complete list - b 23 2 Bytes
HEADER TRANSCRIPTION 11-OCT-00 1G1E
TITLE NMR STRUCTURE OF THE HUMAN MAD1 TRANSREPRESSION DOMAIN SID IN COMPLEX
TITLE 2 WITH MAMMALIAN SIN3A PAH2 DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MAD1 PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SIN3 INTERACTION DOMAIN (SID) TRANSREPRESSION DOMAIN;
COMPND 5 SYNONYM: MAX DIMERIZATION PROTEIN;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: SIN3A;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: PAIRED AMPHIPATHIC HELIX 2 (PAH2 REPEAT);
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THE PEPTIDE SEQUENCE WAS SYNTHESIZED VIA AUTOMATED
SOURCE 4 METHODS. THE SEQUENCE IS NATURALLY FOUND IN HOMO SAPIENS (HUMAN).;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 7 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 8 ORGANISM_TAXID: 10090;
SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET24
KEYWDS FOUR-HELIX BUNDLE, PROTEIN-PEPTIDE COMPLEX, TRANSCRIPTION
EXPDTA SOLUTION NMR
NUMMDL 15
MDLTYP MINIMIZED AVERAGE
AUTHOR K.BRUBAKER,S.M.COWLEY,K.HUANG,R.N.EISENMAN,I.RADHAKRISHNAN
REVDAT 3 23-FEB-22 1G1E 1 REMARK
REVDAT 2 24-FEB-09 1G1E 1 VERSN
REVDAT 1 06-DEC-00 1G1E 0
JRNL AUTH K.BRUBAKER,S.M.COWLEY,K.HUANG,L.LOO,G.S.YOCHUM,D.E.AYER,
JRNL AUTH 2 R.N.EISENMAN,I.RADHAKRISHNAN
JRNL TITL SOLUTION STRUCTURE OF THE INTERACTING DOMAINS OF THE
JRNL TITL 2 MAD-SIN3 COMPLEX: IMPLICATIONS FOR RECRUITMENT OF A
JRNL TITL 3 CHROMATIN-MODIFYING COMPLEX.
JRNL REF CELL(CAMBRIDGE,MASS.) V. 103 655 2000
JRNL REFN ISSN 0092-8674
JRNL PMID 11106735
JRNL DOI 10.1016/S0092-8674(00)00168-9
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : FELIX 98, CNS 1.0
REMARK 3 AUTHORS : MOLECULAR SIMULATIONS (FELIX), BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON 1612 UNIQUE
REMARK 3 DISTANCE CONSTRAINTS, 198 TORSION ANGLE CONSTRAINTS AND 72 JHNHA
REMARK 3 COUPLING CONSTANT CONSTRAINTS.
REMARK 4
REMARK 4 1G1E COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-OCT-00.
REMARK 100 THE DEPOSITION ID IS D_1000012112.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 20 MM PHOSPHATE
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.0 MM 1:1 SID UNLABELED, PAH2 U
REMARK 210 -15N; 1.6 MM 1:1 SID UNLABELED,
REMARK 210 PAH2 U-15N, U-13C.; 1.6 MM 1:1
REMARK 210 SID UNLABELED, PAH2 U-15N,13C;
REMARK 210 20 MM PHOSPHATE BUFFER PH 6.0,
REMARK 210 0.2% NAN3; 1.6 MM 1:1 SID
REMARK 210 UNLABELED, PAH2 U-15N,13C; 20 MM
REMARK 210 PHOSPHATE BUFFER PH 6.0, 0.2%
REMARK 210 NAN3
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D 15N-SEPARATED_NOESY; HNHA; 2D
REMARK 210 13C,15N-DOUBLE-HALF-FILTERED
REMARK 210 NOESY; 2D 13C-DOUBLE-HALF-
REMARK 210 FILTERED NOESY; 3D 13C-SEPARATED_
REMARK 210 NOESY; 3D HACAHB; 2D SPIN-ECHO
REMARK 210 DIFFERENCE FOR JNCGAMMA, JC'
REMARK 210 CGAMMA; 3D HNHB
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX 98, DYANA 1.5
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 25
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH FAVORABLE NON
REMARK 210 -BOND ENERGY,STRUCTURES WITH THE
REMARK 210 LEAST RESTRAINT VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 15
REMARK 210
REMARK 210 REMARK: INTERPROTON NOES WERE ASSIGNED ITERATIVELY BUT MANUALLY
REMARK 210 DURING STRUCTURE REFINEMENT.
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 O MET A 7 H MET A 11 1.57
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 2 TYR A 18 CB - CG - CD2 ANGL. DEV. = -3.8 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 ASN A 8 -97.36 -7.09
REMARK 500 1 GLN B 300 85.71 57.06
REMARK 500 1 PHE B 318 39.85 -98.93
REMARK 500 1 PHE B 366 43.98 -90.38
REMARK 500 1 LYS B 367 -74.32 -51.70
REMARK 500 1 GLN B 369 49.40 -142.44
REMARK 500 1 ASP B 382 48.61 -87.73
REMARK 500 2 MET A 7 -179.82 65.37
REMARK 500 2 ASN A 8 -73.10 -84.33
REMARK 500 2 LEU B 296 89.53 65.18
REMARK 500 2 GLN B 297 154.99 72.95
REMARK 500 2 ASN B 298 152.79 67.31
REMARK 500 2 ASN B 299 -168.84 46.49
REMARK 500 2 GLN B 300 86.16 63.33
REMARK 500 2 PHE B 318 41.22 -102.24
REMARK 500 2 GLN B 321 79.26 -105.24
REMARK 500 2 PHE B 366 42.53 -88.61
REMARK 500 2 GLN B 369 52.40 -142.40
REMARK 500 2 PRO B 381 -159.66 -64.51
REMARK 500 3 ASN A 8 -53.63 -126.67
REMARK 500 3 GLN B 297 -82.76 76.54
REMARK 500 3 ASN B 298 -26.96 -150.91
REMARK 500 3 ASN B 348 33.68 -83.43
REMARK 500 3 PRO B 381 7.46 -68.81
REMARK 500 3 ASP B 382 31.61 -89.63
REMARK 500 4 ASN A 8 -127.16 -176.02
REMARK 500 4 ASN B 298 -78.46 -88.13
REMARK 500 4 THR B 350 127.56 66.89
REMARK 500 4 PHE B 366 41.81 -91.56
REMARK 500 4 LYS B 367 -71.76 -49.64
REMARK 500 4 ASN B 368 33.89 -85.19
REMARK 500 4 PRO B 381 -155.33 -56.81
REMARK 500 5 ASN A 8 -119.01 -147.83
REMARK 500 5 LEU B 296 99.39 61.68
REMARK 500 5 GLN B 321 79.34 -103.87
REMARK 500 5 ASN B 348 32.66 -83.90
REMARK 500 5 PHE B 366 -141.39 -88.40
REMARK 500 5 LYS B 367 -52.27 113.69
REMARK 500 5 GLN B 369 58.16 -142.31
REMARK 500 5 PRO B 381 19.97 -59.44
REMARK 500 5 ASP B 382 -79.96 67.51
REMARK 500 6 MET A 7 -20.26 76.21
REMARK 500 6 ASN B 298 -28.93 -149.81
REMARK 500 6 GLN B 300 137.90 68.86
REMARK 500 6 PHE B 318 38.46 -96.99
REMARK 500 6 PHE B 366 41.03 -90.53
REMARK 500 6 GLN B 369 53.38 -142.72
REMARK 500 6 PRO B 381 -156.90 -62.36
REMARK 500 7 ASN A 8 -129.95 -172.48
REMARK 500 7 GLN B 297 -170.58 53.88
REMARK 500
REMARK 500 THIS ENTRY HAS 131 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1G1E A 6 21 GB 4505069 NP_002348 6 21
DBREF 1G1E B 295 383 UNP Q60520 SIN3A_MOUSE 295 383
SEQRES 1 A 16 ARG MET ASN ILE GLN MET LEU LEU GLU ALA ALA ASP TYR
SEQRES 2 A 16 LEU GLU ARG
SEQRES 1 B 89 SER LEU GLN ASN ASN GLN PRO VAL GLU PHE ASN HIS ALA
SEQRES 2 B 89 ILE ASN TYR VAL ASN LYS ILE LYS ASN ARG PHE GLN GLY
SEQRES 3 B 89 GLN PRO ASP ILE TYR LYS ALA PHE LEU GLU ILE LEU HIS
SEQRES 4 B 89 THR TYR GLN LYS GLU GLN ARG ASN ALA LYS GLU ALA GLY
SEQRES 5 B 89 GLY ASN TYR THR PRO ALA LEU THR GLU GLN GLU VAL TYR
SEQRES 6 B 89 ALA GLN VAL ALA ARG LEU PHE LYS ASN GLN GLU ASP LEU
SEQRES 7 B 89 LEU SER GLU PHE GLY GLN PHE LEU PRO ASP ALA
HELIX 1 1 ILE A 9 GLU A 20 1 12
HELIX 2 2 VAL B 302 ARG B 317 1 16
HELIX 3 3 PRO B 322 ALA B 345 1 24
HELIX 4 4 GLU B 355 LEU B 365 1 11
HELIX 5 5 GLU B 370 GLY B 377 1 8
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