Header list of 1wr0.pdb file
Complete list - r 2 2 Bytes
HEADER PROTEIN TRANSPORT 07-OCT-04 1WR0
TITLE STRUCTURAL CHARACTERIZATION OF THE MIT DOMAIN FROM HUMAN VPS4B
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SKD1 PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: MIT DOMAIN;
COMPND 5 SYNONYM: VACUOLAR SORTING PROTEIN 4B;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PRESAT
KEYWDS VPS4B, SKD1, MIT DOMAIN, ESCORT, MVB, SNPS, PROTEIN TRANSPORT,
KEYWDS 2 STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL
KEYWDS 3 AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS
KEYWDS 4 INITIATIVE, RSGI
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR H.TAKASU,J.G.JEE,A.OHNO,N.GODA,K.FUJIWARA,H.TOCHIO,M.SHIRAKAWA,
AUTHOR 2 H.HIROAKI,RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 4 02-MAR-22 1WR0 1 REMARK SEQADV ATOM
REVDAT 3 24-FEB-09 1WR0 1 VERSN
REVDAT 2 09-OCT-07 1WR0 1 REMARK AUTHOR KEYWDS
REVDAT 1 02-AUG-05 1WR0 0
JRNL AUTH H.TAKASU,J.G.JEE,A.OHNO,N.GODA,K.FUJIWARA,H.TOCHIO,
JRNL AUTH 2 M.SHIRAKAWA,H.HIROAKI
JRNL TITL STRUCTURAL CHARACTERIZATION OF THE MIT DOMAIN FROM HUMAN
JRNL TITL 2 VPS4B
JRNL REF BIOCHEM.BIOPHYS.RES.COMMUN. V. 334 460 2005
JRNL REFN ISSN 0006-291X
JRNL PMID 16018968
JRNL DOI 10.1016/J.BBRC.2005.06.110
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.5, AMBER 7.0
REMARK 3 AUTHORS : PEARLMAN (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 1539 RESTRAINTS, 1471 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 68
REMARK 3 DIHEDRAL ANGLE RESTRAINTS.
REMARK 4
REMARK 4 1WR0 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-OCT-04.
REMARK 100 THE DEPOSITION ID IS D_1000023897.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : NACL 50MM
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1MM PROTEIN U-15N; 20MM TRIS
REMARK 210 BUFFER; 50MM NACL; 95% H2O, 5%
REMARK 210 D2O; 1MM DTT; 1MM PROTEIN U-15N,
REMARK 210 13C; 20MM TRIS BUFFER; 50MM NACL;
REMARK 210 95% H2O, 5% D2O; 1MM DTT
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 2.1, SPARKY 3.110, CYANA
REMARK 210 2.0
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS,
REMARK 210 SIMULATED ANNEALING, MOLECULAR
REMARK 210 DYNAMICS, ENERGY MINIMIZATION
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 94
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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: 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 8 ARG A 72 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 9 ARG A 72 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 11 ARG A 72 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 14 ARG A 72 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 17 ARG A 72 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 19 ARG A 72 NE - CZ - NH1 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 ASP A 3 52.23 38.72
REMARK 500 1 HIS A 4 -22.44 61.28
REMARK 500 1 TYR A 31 55.90 36.17
REMARK 500 1 GLU A 32 -75.16 -130.85
REMARK 500 1 ASP A 56 -89.45 48.86
REMARK 500 1 LEU A 80 107.20 -38.54
REMARK 500 2 MET A 5 -9.67 49.12
REMARK 500 2 SER A 7 -2.34 60.93
REMARK 500 2 TYR A 31 54.35 35.97
REMARK 500 2 GLU A 32 -71.42 -134.79
REMARK 500 3 SER A 6 -33.87 62.36
REMARK 500 3 TYR A 31 55.09 34.37
REMARK 500 3 GLU A 32 -76.12 -132.40
REMARK 500 3 GLU A 52 -147.91 -136.40
REMARK 500 3 ALA A 53 178.81 66.25
REMARK 500 3 ASP A 56 -65.47 -125.17
REMARK 500 4 MET A 5 -37.47 66.76
REMARK 500 4 TYR A 31 54.98 32.95
REMARK 500 4 GLU A 32 -78.82 -130.14
REMARK 500 4 ASP A 56 -91.38 39.87
REMARK 500 5 SER A 2 -11.15 -143.04
REMARK 500 5 MET A 5 -73.33 55.41
REMARK 500 5 SER A 7 -28.31 67.37
REMARK 500 5 TYR A 31 71.32 -63.56
REMARK 500 5 GLU A 32 -67.91 -160.15
REMARK 500 5 GLU A 52 38.12 -141.49
REMARK 500 5 LEU A 80 105.86 -34.93
REMARK 500 6 TYR A 31 54.13 35.00
REMARK 500 6 GLU A 32 -79.26 -132.84
REMARK 500 7 TYR A 31 56.56 35.85
REMARK 500 7 GLU A 32 -57.48 -128.95
REMARK 500 7 GLU A 52 32.80 -146.56
REMARK 500 7 ASP A 56 -83.69 -80.53
REMARK 500 7 LEU A 80 104.89 -41.77
REMARK 500 8 MET A 5 -1.19 48.20
REMARK 500 8 TYR A 31 65.65 25.21
REMARK 500 8 GLU A 32 -79.08 -141.80
REMARK 500 8 ALA A 53 109.11 -49.16
REMARK 500 9 TYR A 31 62.90 28.58
REMARK 500 9 GLU A 32 -72.73 -139.11
REMARK 500 9 ASP A 56 -70.07 -75.36
REMARK 500 10 HIS A 4 -30.46 -150.46
REMARK 500 10 SER A 6 -24.39 62.79
REMARK 500 10 TYR A 31 54.88 35.86
REMARK 500 10 GLU A 32 -75.63 -131.54
REMARK 500 10 ASP A 56 -76.94 -103.50
REMARK 500 11 MET A 5 31.08 -76.74
REMARK 500 11 TYR A 31 54.97 35.16
REMARK 500 11 GLU A 32 -78.96 -132.94
REMARK 500 11 ASP A 56 -70.31 -68.98
REMARK 500
REMARK 500 THIS ENTRY HAS 88 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 5 ARG A 72 0.08 SIDE CHAIN
REMARK 500 16 ARG A 72 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: AR_001000797.1 RELATED DB: TARGETDB
DBREF 1WR0 A 5 81 UNP O75351 VPS4B_HUMAN 1 77
SEQADV 1WR0 GLY A 1 UNP O75351 EXPRESSION TAG
SEQADV 1WR0 SER A 2 UNP O75351 EXPRESSION TAG
SEQADV 1WR0 ASP A 3 UNP O75351 EXPRESSION TAG
SEQADV 1WR0 HIS A 4 UNP O75351 EXPRESSION TAG
SEQRES 1 A 81 GLY SER ASP HIS MET SER SER THR SER PRO ASN LEU GLN
SEQRES 2 A 81 LYS ALA ILE ASP LEU ALA SER LYS ALA ALA GLN GLU ASP
SEQRES 3 A 81 LYS ALA GLY ASN TYR GLU GLU ALA LEU GLN LEU TYR GLN
SEQRES 4 A 81 HIS ALA VAL GLN TYR PHE LEU HIS VAL VAL LYS TYR GLU
SEQRES 5 A 81 ALA GLN GLY ASP LYS ALA LYS GLN SER ILE ARG ALA LYS
SEQRES 6 A 81 CYS THR GLU TYR LEU ASP ARG ALA GLU LYS LEU LYS GLU
SEQRES 7 A 81 TYR LEU LYS
HELIX 1 1 SER A 9 ALA A 28 1 20
HELIX 2 2 GLU A 33 GLU A 52 1 20
HELIX 3 3 GLY A 55 ALA A 58 5 4
HELIX 4 4 LYS A 59 LYS A 77 1 19
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