Header list of 1mc7.pdb file
Complete list - t 27 2 Bytes
HEADER SIGNALING PROTEIN 05-AUG-02 1MC7
TITLE SOLUTION STRUCTURE OF MDVL1 PDZ DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SEGMENT POLARITY PROTEIN DISHEVELLED HOMOLOG DVL-1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PDZ DOMAIN;
COMPND 5 SYNONYM: DISHEVELLED-1, DSH HOMOLOG 1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL-21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28
KEYWDS PDZ DOMAIN, WNT SIGNALING, SIGNALING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR H.-C.WONG,A.BOURDELAS,Y.SHAO,D.WU,D.L.SHI,J.ZHENG
REVDAT 4 27-OCT-21 1MC7 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1MC7 1 VERSN
REVDAT 2 16-DEC-03 1MC7 1 JRNL
REVDAT 1 23-SEP-03 1MC7 0
JRNL AUTH H.-C.WONG,A.BOURDELAS,A.KRAUSS,H.-J.LEE,Y.SHAO,D.WU,
JRNL AUTH 2 M.MLODZIK,D.-L.SHI,J.ZHENG
JRNL TITL DIRECT BINDING OF THE PDZ DOMAIN OF DISHEVELLED TO A
JRNL TITL 2 CONSERVED INTERNAL SEQUENCE IN THE C-TERMINAL REGION OF
JRNL TITL 3 FRIZZLED
JRNL REF MOL.CELL V. 12 1251 2003
JRNL REFN ISSN 1097-2765
JRNL PMID 14636582
JRNL DOI 10.1016/S1097-2765(03)00427-1
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA, DYANA
REMARK 3 AUTHORS : GUNTERT (DYANA), GUNTERT (DYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 1190 RESTRAINTS: 1124 ARE
REMARK 3 NOE-DERIVED
REMARK 3 DISTANCE CONSTRAINTS, 44 ARE DIHEDRAL ANGLE RESTRAINTS AND 22 ARE
REMARK 3 DISTANCE RESTRAINTS
REMARK 3 FROM HYDROGEN BONDS.
REMARK 4
REMARK 4 1MC7 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-AUG-02.
REMARK 100 THE DEPOSITION ID IS D_1000016817.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM MDVL1 PDZ DOMAIN U-15N, 13C,
REMARK 210 100MM PHOSPHATE BUFFER PH 7.5,
REMARK 210 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE, XEASY
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 320
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY.
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: 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 GLN A 53 H THR A 84 1.51
REMARK 500 O VAL A 68 H ARG A 72 1.60
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 MET A 6 125.78 60.55
REMARK 500 1 GLU A 7 -47.31 -158.26
REMARK 500 1 HIS A 9 -60.95 78.83
REMARK 500 1 HIS A 10 173.35 -48.35
REMARK 500 1 GLN A 19 -64.60 -164.44
REMARK 500 1 SER A 20 140.81 164.82
REMARK 500 1 ASP A 22 -51.42 -175.12
REMARK 500 1 ARG A 23 115.90 -162.14
REMARK 500 1 ASP A 25 122.22 162.51
REMARK 500 1 ALA A 38 -88.34 -85.21
REMARK 500 1 ILE A 45 163.08 -41.85
REMARK 500 1 MET A 50 48.40 79.56
REMARK 500 1 ASN A 55 -141.31 39.84
REMARK 500 1 MET A 62 -83.15 -61.92
REMARK 500 1 SER A 63 54.03 36.60
REMARK 500 1 ASP A 65 25.26 46.04
REMARK 500 1 ASP A 66 29.46 -162.87
REMARK 500 1 ILE A 74 -91.76 -68.92
REMARK 500 1 VAL A 75 -37.33 -36.35
REMARK 500 1 GLN A 77 -134.05 -133.16
REMARK 500 1 THR A 78 160.22 -41.06
REMARK 500 1 SER A 82 45.65 156.85
REMARK 500 1 LEU A 83 146.30 -32.34
REMARK 500 1 ALA A 86 42.17 -92.75
REMARK 500 1 LYS A 87 171.16 54.22
REMARK 500 1 ALA A 88 118.76 179.50
REMARK 500 1 TRP A 89 101.64 -43.11
REMARK 500 1 ARG A 94 52.47 28.26
REMARK 500 2 MET A 6 170.67 60.88
REMARK 500 2 ARG A 8 94.09 43.86
REMARK 500 2 HIS A 9 105.39 -177.11
REMARK 500 2 LEU A 12 147.02 73.51
REMARK 500 2 GLN A 19 -55.68 -173.85
REMARK 500 2 SER A 20 89.57 44.72
REMARK 500 2 ASP A 25 90.27 45.44
REMARK 500 2 SER A 32 161.93 179.93
REMARK 500 2 MET A 34 83.13 -57.44
REMARK 500 2 LYS A 35 144.55 -39.28
REMARK 500 2 ALA A 38 -74.71 -86.34
REMARK 500 2 ARG A 44 54.55 35.33
REMARK 500 2 ILE A 45 164.90 -43.30
REMARK 500 2 MET A 50 50.72 80.78
REMARK 500 2 ASN A 55 -141.15 38.52
REMARK 500 2 GLU A 60 -75.48 -65.01
REMARK 500 2 MET A 62 -82.69 -56.69
REMARK 500 2 SER A 63 49.95 33.64
REMARK 500 2 ASP A 65 30.94 38.85
REMARK 500 2 ASP A 66 31.25 -166.62
REMARK 500 2 ILE A 74 -92.60 -66.71
REMARK 500 2 VAL A 75 -38.70 -38.58
REMARK 500
REMARK 500 THIS ENTRY HAS 613 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1MC7 A 1 95 UNP P51141 DVL1_MOUSE 251 345
SEQADV 1MC7 ALA A 88 UNP P51141 CYS 338 ENGINEERED MUTATION
SEQRES 1 A 95 THR VAL THR LEU ASN MET GLU ARG HIS HIS PHE LEU GLY
SEQRES 2 A 95 ILE SER ILE VAL GLY GLN SER ASN ASP ARG GLY ASP GLY
SEQRES 3 A 95 GLY ILE TYR ILE GLY SER ILE MET LYS GLY GLY ALA VAL
SEQRES 4 A 95 ALA ALA ASP GLY ARG ILE GLU PRO GLY ASP MET LEU LEU
SEQRES 5 A 95 GLN VAL ASN ASP VAL ASN PHE GLU ASN MET SER ASN ASP
SEQRES 6 A 95 ASP ALA VAL ARG VAL LEU ARG GLU ILE VAL SER GLN THR
SEQRES 7 A 95 GLY PRO ILE SER LEU THR VAL ALA LYS ALA TRP ASP PRO
SEQRES 8 A 95 THR PRO ARG SER
HELIX 1 1 ALA A 38 GLY A 43 1 6
HELIX 2 2 GLU A 46 ASP A 49 5 4
HELIX 3 3 ALA A 67 GLN A 77 1 11
SHEET 1 A 2 ILE A 14 VAL A 17 0
SHEET 2 A 2 TYR A 29 ILE A 33 -1 O GLY A 31 N SER A 15
SHEET 1 B 2 LEU A 51 VAL A 54 0
SHEET 2 B 2 LEU A 83 VAL A 85 -1 O THR A 84 N GLN A 53
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 - t 27 2 Bytes