Header list of 1va8.pdb file
Complete list - r 2 2 Bytes
HEADER MEMBRANE PROTEIN 13-FEB-04 1VA8
TITLE SOLUTION STRUCTURE OF THE PDZ DOMAIN OF PALS1 PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MAGUK P55 SUBFAMILY MEMBER 5;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PDZ DOMAIN;
COMPND 5 SYNONYM: PALS1 PROTEIN, PROTEIN ASSOCIATED WITH LIN-7 1;
COMPND 6 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 3830420B02;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P030203-38;
SOURCE 8 OTHER_DETAILS: CELL FREE PROTEIN SYNTHESIS
KEYWDS PDZ DOMAIN, PALMITOYLATED 5, PALS1 PROTEIN, STRUCTURAL GENOMICS,
KEYWDS 2 RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, MEMBRANE
KEYWDS 3 PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR X.-R.QIN,F.HAYASHI,S.YOKOYAMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS
AUTHOR 2 INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1VA8 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1VA8 1 VERSN
REVDAT 1 22-FEB-05 1VA8 0
JRNL AUTH X.-R.QIN,F.HAYASHI,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE PDZ DOMAIN OF PALS1 PROTEIN
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1C, CYANA 1.0.7
REMARK 3 AUTHORS : VARIAN (VNMR), GUENTERT,P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1VA8 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-FEB-04.
REMARK 100 THE DEPOSITION ID IS D_1000006401.
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 : 1.05MM 13C, 15N-LABELED PROTEIN;
REMARK 210 20MM PINA(PH6.0); 100MM NACL;
REMARK 210 1MMD10-DTT; 0.02% NAN3; 90%H2O;
REMARK 210 10%D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20020425, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.854, 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 : NULL
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 LYS A 33 H GLY A 98 1.53
REMARK 500 O ASN A 87 H ASP A 91 1.54
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 2 117.29 -173.23
REMARK 500 1 SER A 5 -55.57 -147.40
REMARK 500 1 SER A 6 116.80 60.40
REMARK 500 1 THR A 10 -167.25 45.19
REMARK 500 1 ARG A 13 70.22 -154.33
REMARK 500 1 VAL A 14 21.69 -151.82
REMARK 500 1 TYR A 15 51.73 -94.70
REMARK 500 1 GLU A 16 141.30 71.10
REMARK 500 1 ASP A 36 33.98 -147.49
REMARK 500 1 MET A 47 -59.97 -19.26
REMARK 500 1 ASP A 48 23.13 -153.58
REMARK 500 1 LEU A 74 -56.15 -122.03
REMARK 500 1 LYS A 84 178.61 -56.97
REMARK 500 1 SER A 111 105.20 -177.42
REMARK 500 2 SER A 3 -63.74 -93.60
REMARK 500 2 PRO A 8 -167.27 -75.02
REMARK 500 2 GLU A 12 49.49 -92.25
REMARK 500 2 ARG A 13 77.19 -158.25
REMARK 500 2 VAL A 14 20.50 -142.69
REMARK 500 2 TYR A 21 144.27 -38.85
REMARK 500 2 ASP A 36 35.13 -154.68
REMARK 500 2 MET A 47 -58.82 -22.31
REMARK 500 2 ASP A 48 23.27 -152.31
REMARK 500 2 LEU A 74 -52.63 -124.57
REMARK 500 2 ILE A 81 -47.43 -130.02
REMARK 500 2 ARG A 82 122.06 -38.15
REMARK 500 2 LYS A 84 165.33 -46.58
REMARK 500 2 THR A 99 97.55 -69.79
REMARK 500 2 SER A 112 103.68 -54.44
REMARK 500 3 SER A 5 109.94 -164.19
REMARK 500 3 SER A 6 -66.57 -127.56
REMARK 500 3 ARG A 13 22.49 -149.89
REMARK 500 3 GLU A 16 -157.96 -109.90
REMARK 500 3 TYR A 21 60.44 -68.66
REMARK 500 3 ASP A 36 31.74 -166.71
REMARK 500 3 MET A 47 -58.14 -18.76
REMARK 500 3 ASP A 48 24.09 -155.54
REMARK 500 3 LEU A 74 -53.38 -125.71
REMARK 500 3 THR A 99 97.63 -69.96
REMARK 500 3 SER A 108 48.69 -84.22
REMARK 500 4 SER A 6 -88.43 62.91
REMARK 500 4 PRO A 8 -165.42 -75.02
REMARK 500 4 GLU A 12 59.75 -111.33
REMARK 500 4 ARG A 13 24.20 -151.82
REMARK 500 4 GLU A 16 -147.51 -115.47
REMARK 500 4 HIS A 20 61.76 170.74
REMARK 500 4 GLU A 24 -167.82 -54.76
REMARK 500 4 ASP A 36 33.86 -173.13
REMARK 500 4 MET A 47 -58.05 -18.37
REMARK 500 4 ASP A 48 24.61 -156.81
REMARK 500
REMARK 500 THIS ENTRY HAS 285 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: MMT007005271 RELATED DB: TARGETDB
DBREF 1VA8 A 8 107 UNP Q9JLB2 MPP5_MOUSE 236 335
SEQADV 1VA8 GLY A 1 UNP Q9JLB2 CLONING ARTIFACT
SEQADV 1VA8 SER A 2 UNP Q9JLB2 CLONING ARTIFACT
SEQADV 1VA8 SER A 3 UNP Q9JLB2 CLONING ARTIFACT
SEQADV 1VA8 GLY A 4 UNP Q9JLB2 CLONING ARTIFACT
SEQADV 1VA8 SER A 5 UNP Q9JLB2 CLONING ARTIFACT
SEQADV 1VA8 SER A 6 UNP Q9JLB2 CLONING ARTIFACT
SEQADV 1VA8 GLY A 7 UNP Q9JLB2 CLONING ARTIFACT
SEQADV 1VA8 SER A 108 UNP Q9JLB2 CLONING ARTIFACT
SEQADV 1VA8 GLY A 109 UNP Q9JLB2 CLONING ARTIFACT
SEQADV 1VA8 PRO A 110 UNP Q9JLB2 CLONING ARTIFACT
SEQADV 1VA8 SER A 111 UNP Q9JLB2 CLONING ARTIFACT
SEQADV 1VA8 SER A 112 UNP Q9JLB2 CLONING ARTIFACT
SEQADV 1VA8 GLY A 113 UNP Q9JLB2 CLONING ARTIFACT
SEQRES 1 A 113 GLY SER SER GLY SER SER GLY PRO ILE THR ASP GLU ARG
SEQRES 2 A 113 VAL TYR GLU SER ILE GLY HIS TYR GLY GLY GLU THR VAL
SEQRES 3 A 113 LYS ILE VAL ARG ILE GLU LYS ALA ARG ASP ILE PRO LEU
SEQRES 4 A 113 GLY ALA THR VAL ARG ASN GLU MET ASP SER VAL ILE ILE
SEQRES 5 A 113 SER ARG ILE VAL LYS GLY GLY ALA ALA GLU LYS SER GLY
SEQRES 6 A 113 LEU LEU HIS GLU GLY ASP GLU VAL LEU GLU ILE ASN GLY
SEQRES 7 A 113 ILE GLU ILE ARG GLY LYS ASP VAL ASN GLU VAL PHE ASP
SEQRES 8 A 113 LEU LEU SER ASP MET HIS GLY THR LEU THR PHE VAL LEU
SEQRES 9 A 113 ILE PRO SER SER GLY PRO SER SER GLY
HELIX 1 1 GLY A 59 GLY A 65 1 7
HELIX 2 2 ASP A 85 MET A 96 1 12
SHEET 1 A 2 HIS A 20 TYR A 21 0
SHEET 2 A 2 GLU A 24 THR A 25 -1 O GLU A 24 N TYR A 21
SHEET 1 B 5 LYS A 27 LYS A 33 0
SHEET 2 B 5 GLY A 98 ILE A 105 -1 O GLY A 98 N LYS A 33
SHEET 3 B 5 GLU A 72 ILE A 76 -1 N GLU A 75 O VAL A 103
SHEET 4 B 5 VAL A 50 ILE A 55 -1 N VAL A 50 O VAL A 73
SHEET 5 B 5 ALA A 41 ASN A 45 -1 N THR A 42 O SER A 53
SHEET 1 C 4 LYS A 27 LYS A 33 0
SHEET 2 C 4 GLY A 98 ILE A 105 -1 O GLY A 98 N LYS A 33
SHEET 3 C 4 GLU A 72 ILE A 76 -1 N GLU A 75 O VAL A 103
SHEET 4 C 4 ILE A 79 GLU A 80 -1 O ILE A 79 N ILE A 76
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