Header list of 1wgq.pdb file
Complete list - r 2 2 Bytes
HEADER SUGAR BINDING PROTEIN 28-MAY-04 1WGQ
TITLE SOLUTION STRUCTURE OF THE PLECKSTRIN HOMOLOGY DOMAIN OF MOUSE ETHANOL
TITLE 2 DECREASED 4 PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FYVE, RHOGEF AND PH DOMAIN CONTAINING 6; ETHANOL DECREASED
COMPND 3 4;
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: PLECKSTRIN HOMOLOGY DOMAIN;
COMPND 6 SYNONYM: ETHANOL DECREASED 4 PROTEIN;
COMPND 7 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: RIKEN CDNA 4933427A08;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P030212-46;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS PLECKSTRIN HOMOLOY DOMAIN, SIGNAL TRANSDUCTION, STRUCTURAL GENOMICS,
KEYWDS 2 RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, SUGAR BINDING
KEYWDS 3 PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR H.LI,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1WGQ 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1WGQ 1 VERSN
REVDAT 1 28-NOV-04 1WGQ 0
JRNL AUTH H.LI,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE PLECKSTRIN HOMOLOGY DOMAIN OF
JRNL TITL 2 MOUSE ETHANOL DECREASED 4 PROTEIN
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, CYANA 1.0.7
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUENTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1WGQ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 03-JUN-04.
REMARK 100 THE DEPOSITION ID IS D_1000023561.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.22MM PLECKSTRIN HOMOLOGY
REMARK 210 DOMAIN U-13C, 15N; 20MM
REMARK 210 PHOSPHATE BUFFER NA (PH6.0);
REMARK 210 100MM NACL; 1MM D-DTT; 0.02%
REMARK 210 NAN3; 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 : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20020425, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.897, CYANA 1.0.7
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS, TARGET
REMARK 210 FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: NULL
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 LEU A 73 H PHE A 80 1.52
REMARK 500 O SER A 17 H VAL A 82 1.52
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 3 145.88 61.41
REMARK 500 1 SER A 6 87.67 -158.38
REMARK 500 1 LYS A 21 -0.55 78.29
REMARK 500 1 ALA A 40 -46.03 -132.31
REMARK 500 1 GLU A 43 43.93 -94.34
REMARK 500 1 LEU A 53 36.30 -92.75
REMARK 500 1 ASP A 63 171.40 59.21
REMARK 500 1 SER A 68 35.02 -161.85
REMARK 500 1 LYS A 76 -6.65 84.12
REMARK 500 1 ASP A 86 -78.21 -44.81
REMARK 500 1 ILE A 95 -70.49 -53.66
REMARK 500 1 SER A 104 16.24 -140.87
REMARK 500 2 SER A 2 -58.14 -132.58
REMARK 500 2 SER A 3 89.96 50.60
REMARK 500 2 SER A 5 -82.01 65.21
REMARK 500 2 SER A 6 81.95 71.46
REMARK 500 2 SER A 11 133.13 -172.66
REMARK 500 2 LYS A 32 -102.90 -76.26
REMARK 500 2 LYS A 34 19.49 56.33
REMARK 500 2 ALA A 40 -46.29 -135.18
REMARK 500 2 ASP A 63 156.02 71.52
REMARK 500 2 GLU A 67 -44.09 -130.29
REMARK 500 2 SER A 68 34.07 -151.59
REMARK 500 2 SER A 107 88.95 52.70
REMARK 500 3 SER A 3 169.07 179.91
REMARK 500 3 SER A 6 -53.48 -148.09
REMARK 500 3 SER A 8 155.76 -49.08
REMARK 500 3 SER A 11 148.57 -178.40
REMARK 500 3 ALA A 40 -46.13 -130.23
REMARK 500 3 GLU A 43 46.07 -101.64
REMARK 500 3 ASP A 44 170.36 -58.02
REMARK 500 3 PHE A 56 -177.12 -64.51
REMARK 500 3 ASP A 63 176.44 52.46
REMARK 500 3 SER A 68 30.47 -163.56
REMARK 500 3 LYS A 76 -55.40 75.38
REMARK 500 4 SER A 2 81.47 62.04
REMARK 500 4 SER A 6 -58.35 -140.30
REMARK 500 4 SER A 11 145.01 -171.84
REMARK 500 4 GLU A 43 53.22 -110.05
REMARK 500 4 LEU A 53 39.85 -93.08
REMARK 500 4 PHE A 56 178.61 -58.08
REMARK 500 4 GLU A 67 58.84 -142.07
REMARK 500 4 SER A 68 -25.71 158.72
REMARK 500 4 LYS A 76 -2.95 83.58
REMARK 500 4 ASP A 86 -74.92 -56.34
REMARK 500 5 SER A 2 124.83 178.97
REMARK 500 5 SER A 11 125.40 -172.46
REMARK 500 5 LYS A 21 -3.42 80.25
REMARK 500 5 ASN A 33 -77.62 67.11
REMARK 500 5 LYS A 34 17.61 -143.81
REMARK 500
REMARK 500 THIS ENTRY HAS 222 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: MMT007011951.1 RELATED DB: TARGETDB
DBREF 1WGQ A 8 103 UNP Q69ZL1 FGD6_MOUSE 1302 1397
SEQADV 1WGQ GLY A 1 UNP Q69ZL1 CLONING ARTIFACT
SEQADV 1WGQ SER A 2 UNP Q69ZL1 CLONING ARTIFACT
SEQADV 1WGQ SER A 3 UNP Q69ZL1 CLONING ARTIFACT
SEQADV 1WGQ GLY A 4 UNP Q69ZL1 CLONING ARTIFACT
SEQADV 1WGQ SER A 5 UNP Q69ZL1 CLONING ARTIFACT
SEQADV 1WGQ SER A 6 UNP Q69ZL1 CLONING ARTIFACT
SEQADV 1WGQ GLY A 7 UNP Q69ZL1 CLONING ARTIFACT
SEQADV 1WGQ SER A 104 UNP Q69ZL1 CLONING ARTIFACT
SEQADV 1WGQ GLY A 105 UNP Q69ZL1 CLONING ARTIFACT
SEQADV 1WGQ PRO A 106 UNP Q69ZL1 CLONING ARTIFACT
SEQADV 1WGQ SER A 107 UNP Q69ZL1 CLONING ARTIFACT
SEQADV 1WGQ SER A 108 UNP Q69ZL1 CLONING ARTIFACT
SEQADV 1WGQ GLY A 109 UNP Q69ZL1 CLONING ARTIFACT
SEQRES 1 A 109 GLY SER SER GLY SER SER GLY SER THR MET SER GLY TYR
SEQRES 2 A 109 LEU TYR ARG SER LYS GLY SER LYS LYS PRO TRP LYS HIS
SEQRES 3 A 109 LEU TRP PHE VAL ILE LYS ASN LYS VAL LEU TYR THR TYR
SEQRES 4 A 109 ALA ALA SER GLU ASP VAL ALA ALA LEU GLU SER GLN PRO
SEQRES 5 A 109 LEU LEU GLY PHE THR VAL THR LEU VAL LYS ASP GLU ASN
SEQRES 6 A 109 SER GLU SER LYS VAL PHE GLN LEU LEU HIS LYS GLY MET
SEQRES 7 A 109 VAL PHE TYR VAL PHE LYS ALA ASP ASP ALA HIS SER THR
SEQRES 8 A 109 GLN ARG TRP ILE ASP ALA PHE GLN GLU GLY THR VAL SER
SEQRES 9 A 109 GLY PRO SER SER GLY
HELIX 1 1 ALA A 88 THR A 102 1 15
SHEET 1 A 7 GLU A 49 PRO A 52 0
SHEET 2 A 7 VAL A 35 TYR A 39 -1 N THR A 38 O GLU A 49
SHEET 3 A 7 LYS A 25 LYS A 32 -1 N LYS A 32 O VAL A 35
SHEET 4 A 7 SER A 11 SER A 17 -1 N LEU A 14 O LEU A 27
SHEET 5 A 7 MET A 78 LYS A 84 -1 O VAL A 82 N SER A 17
SHEET 6 A 7 VAL A 70 HIS A 75 -1 N LEU A 73 O PHE A 80
SHEET 7 A 7 PHE A 56 LEU A 60 -1 N THR A 57 O LEU A 74
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 - r 2 2 Bytes