Header list of 1vae.pdb file
Complete list - v 10 2 Bytes
HEADER SIGNALING PROTEIN 14-FEB-04 1VAE
TITLE SOLUTION STRUCTURE OF THE PDZ DOMAIN OF MOUSE RHOPHILIN-2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RHOPHILIN, RHO GTPASE BINDING PROTEIN 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PDZ DOMAIN;
COMPND 5 SYNONYM: RHOPHILIN 2;
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 GENE: RIKEN CDNA 1300002E07;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P030203-40;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS PDZ DOMAIN, INTRACELLULAR SIGNALING CASCADE, SIGNAL TRANSDUCTION, RHO
KEYWDS 2 GTPASE BINDING PROTEIN 2, ALPHA-ACTIN-4 BINDING DOMAIN, STRUCTURAL
KEYWDS 3 GENOMICS, RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI,
KEYWDS 4 SIGNALING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.YONEYAMA,N.TOCHIO,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA,RIKEN
AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 10-NOV-21 1VAE 1 REMARK SEQADV SHEET
REVDAT 2 24-FEB-09 1VAE 1 VERSN
REVDAT 1 14-AUG-04 1VAE 0
JRNL AUTH M.YONEYAMA,N.TOCHIO,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE PDZ DOMAIN OF MOUSE RHOPHILIN-2
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 1VAE 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_1000006403.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 4.0
REMARK 210 IONIC STRENGTH : 120
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM PDZ DOMAIN U-15N,13C; 20MM
REMARK 210 ACETATE BUFFER NA; 100MM NACL;
REMARK 210 1MM D-DTT; 0.02% NAN3; 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 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 KUJIR 0.891, 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 H LYS A 55 OD2 ASP A 58 1.55
REMARK 500 O VAL A 61 H CYS A 68 1.55
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 -58.14 -122.62
REMARK 500 1 SER A 6 156.12 60.56
REMARK 500 1 VAL A 23 159.96 -40.65
REMARK 500 1 ASP A 27 89.19 -153.09
REMARK 500 1 ASN A 35 -69.56 -109.98
REMARK 500 1 THR A 36 140.40 -174.96
REMARK 500 1 HIS A 41 65.99 -103.56
REMARK 500 1 CYS A 47 -123.63 -63.20
REMARK 500 1 SER A 48 -58.81 -142.61
REMARK 500 1 LEU A 71 154.92 -42.32
REMARK 500 1 THR A 72 -147.28 -98.05
REMARK 500 1 PHE A 83 44.44 -88.95
REMARK 500 1 SER A 98 165.62 -48.92
REMARK 500 1 SER A 100 146.83 64.90
REMARK 500 2 SER A 6 114.78 -179.23
REMARK 500 2 ALA A 9 171.15 61.68
REMARK 500 2 SER A 10 156.79 61.33
REMARK 500 2 VAL A 23 164.92 -43.52
REMARK 500 2 ASP A 27 89.35 -156.09
REMARK 500 2 ASN A 35 -67.68 -95.96
REMARK 500 2 THR A 36 139.21 -177.78
REMARK 500 2 VAL A 38 170.16 -50.10
REMARK 500 2 CYS A 47 -105.90 -108.59
REMARK 500 2 SER A 48 -67.45 -143.75
REMARK 500 2 GLN A 64 33.71 71.22
REMARK 500 2 LEU A 71 154.21 -44.18
REMARK 500 2 THR A 72 -155.28 -94.59
REMARK 500 2 PHE A 83 37.83 -89.22
REMARK 500 2 THR A 99 151.24 -40.45
REMARK 500 2 SER A 101 127.03 61.81
REMARK 500 2 MET A 102 -44.95 -175.95
REMARK 500 2 HIS A 103 145.04 61.40
REMARK 500 2 SER A 106 119.57 -167.16
REMARK 500 3 SER A 5 106.50 62.98
REMARK 500 3 SER A 6 -58.43 -139.39
REMARK 500 3 SER A 10 118.76 63.81
REMARK 500 3 LYS A 11 161.15 -49.06
REMARK 500 3 GLU A 25 60.28 -69.24
REMARK 500 3 ASP A 27 94.57 -162.45
REMARK 500 3 ASN A 35 -67.91 -101.35
REMARK 500 3 THR A 36 139.81 -178.50
REMARK 500 3 HIS A 41 77.78 -106.62
REMARK 500 3 PHE A 42 120.73 -39.11
REMARK 500 3 HIS A 46 36.13 -90.55
REMARK 500 3 CYS A 47 -125.32 -70.97
REMARK 500 3 SER A 48 -57.83 -138.88
REMARK 500 3 GLN A 64 33.88 70.40
REMARK 500 3 THR A 72 -159.06 -103.00
REMARK 500 3 GLU A 75 -71.43 -45.87
REMARK 500 3 PHE A 83 39.79 -90.94
REMARK 500
REMARK 500 THIS ENTRY HAS 316 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: MMT007006845.1 RELATED DB: TARGETDB
DBREF 1VAE A 8 105 UNP Q8BWR8 RHPN2_MOUSE 506 603
SEQADV 1VAE GLY A 1 UNP Q8BWR8 CLONING ARTIFACT
SEQADV 1VAE SER A 2 UNP Q8BWR8 CLONING ARTIFACT
SEQADV 1VAE SER A 3 UNP Q8BWR8 CLONING ARTIFACT
SEQADV 1VAE GLY A 4 UNP Q8BWR8 CLONING ARTIFACT
SEQADV 1VAE SER A 5 UNP Q8BWR8 CLONING ARTIFACT
SEQADV 1VAE SER A 6 UNP Q8BWR8 CLONING ARTIFACT
SEQADV 1VAE GLY A 7 UNP Q8BWR8 CLONING ARTIFACT
SEQADV 1VAE HIS A 20 UNP Q8BWR8 ASP 518 ENGINEERED MUTATION
SEQADV 1VAE SER A 106 UNP Q8BWR8 CLONING ARTIFACT
SEQADV 1VAE GLY A 107 UNP Q8BWR8 CLONING ARTIFACT
SEQADV 1VAE PRO A 108 UNP Q8BWR8 CLONING ARTIFACT
SEQADV 1VAE SER A 109 UNP Q8BWR8 CLONING ARTIFACT
SEQADV 1VAE SER A 110 UNP Q8BWR8 CLONING ARTIFACT
SEQADV 1VAE GLY A 111 UNP Q8BWR8 CLONING ARTIFACT
SEQRES 1 A 111 GLY SER SER GLY SER SER GLY SER ALA SER LYS ARG TRP
SEQRES 2 A 111 SER PRO PRO ARG GLY ILE HIS PHE THR VAL GLU GLU GLY
SEQRES 3 A 111 ASP LEU GLY PHE THR LEU ARG GLY ASN THR PRO VAL GLN
SEQRES 4 A 111 VAL HIS PHE LEU ASP PRO HIS CYS SER ALA SER LEU ALA
SEQRES 5 A 111 GLY ALA LYS GLU GLY ASP TYR ILE VAL SER ILE GLN GLY
SEQRES 6 A 111 VAL ASP CYS LYS TRP LEU THR VAL SER GLU VAL MET LYS
SEQRES 7 A 111 LEU LEU LYS SER PHE GLY GLY GLU GLU VAL GLU MET LYS
SEQRES 8 A 111 VAL VAL SER LEU LEU ASP SER THR SER SER MET HIS ASN
SEQRES 9 A 111 LYS SER GLY PRO SER SER GLY
HELIX 1 1 SER A 48 ALA A 52 1 5
HELIX 2 2 THR A 72 PHE A 83 1 12
SHEET 1 A 2 ARG A 12 TRP A 13 0
SHEET 2 A 2 LEU A 95 LEU A 96 -1 O LEU A 96 N ARG A 12
SHEET 1 B 2 ARG A 17 THR A 22 0
SHEET 2 B 2 GLU A 87 VAL A 93 -1 O VAL A 88 N PHE A 21
SHEET 1 C 2 TYR A 59 ILE A 63 0
SHEET 2 C 2 VAL A 66 ASP A 67 0
SHEET 1 D 2 PHE A 30 ARG A 33 0
SHEET 2 D 2 GLN A 39 VAL A 40 -1 O GLN A 39 N ARG A 33
CISPEP 1 THR A 36 PRO A 37 1 0.00
CISPEP 2 THR A 36 PRO A 37 2 0.06
CISPEP 3 THR A 36 PRO A 37 3 0.00
CISPEP 4 THR A 36 PRO A 37 4 0.01
CISPEP 5 THR A 36 PRO A 37 5 -0.02
CISPEP 6 THR A 36 PRO A 37 6 0.06
CISPEP 7 THR A 36 PRO A 37 7 0.02
CISPEP 8 THR A 36 PRO A 37 8 0.03
CISPEP 9 THR A 36 PRO A 37 9 -0.03
CISPEP 10 THR A 36 PRO A 37 10 -0.12
CISPEP 11 THR A 36 PRO A 37 11 0.02
CISPEP 12 THR A 36 PRO A 37 12 0.03
CISPEP 13 THR A 36 PRO A 37 13 0.03
CISPEP 14 THR A 36 PRO A 37 14 0.07
CISPEP 15 THR A 36 PRO A 37 15 0.02
CISPEP 16 THR A 36 PRO A 37 16 0.06
CISPEP 17 THR A 36 PRO A 37 17 -0.01
CISPEP 18 THR A 36 PRO A 37 18 -0.04
CISPEP 19 THR A 36 PRO A 37 19 -0.02
CISPEP 20 THR A 36 PRO A 37 20 -0.03
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 - v 10 2 Bytes