Header list of 1wmv.pdb file
Complete list - r 2 2 Bytes
HEADER OXIDOREDUCTASE, APOPTOSIS 21-JUL-04 1WMV
TITLE SOLUTION STRUCTURE OF THE SECOND WW DOMAIN OF WWOX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: WW DOMAIN CONTAINING OXIDOREDUCTASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SECOND WW DOMAIN;
COMPND 5 SYNONYM: WWOX;
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 GENE: WOX/FOR;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX-4T
KEYWDS WW DOMAIN, ALL-BETA, OXIDOREDUCTASE, APOPTOSIS
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR K.KOWALSKI,A.L.MERKEL,A.COLELLA,R.I.RICHARDS,G.W.BOOKER
REVDAT 3 02-MAR-22 1WMV 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1WMV 1 VERSN
REVDAT 1 09-AUG-05 1WMV 0
JRNL AUTH K.KOWALSKI,A.L.MERKEL,A.COLELLA,R.I.RICHARDS,G.W.BOOKER
JRNL TITL SOLUTION STRUCTURE OF THE SECOND WW DOMAIN OF WWOX
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 1.8, ARIA 1.2
REMARK 3 AUTHORS : DELAGLIO, ET AL (NMRPIPE), LINGE, ET AL (ARIA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: STRUCTURES ARE BASED ON A TOTAL OF 709
REMARK 3 RESTRAINTS; 670 NOE-DERIVED DISTANCE RCONSTRAINTS, 39 DIHEDRAL
REMARK 3 ANGLE RESTRAINTS
REMARK 4
REMARK 4 1WMV COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 23-JUL-04.
REMARK 100 THE DEPOSITION ID IS D_1000023757.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 100MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.75MM WW2; 25MM PHOSPHATE
REMARK 210 BUFFER; 100MM NACL; 0.01% NAN3;
REMARK 210 90% H2O, 10% D2O; 0.75MM WW2;
REMARK 210 25MM PHOSPHATE BUFFER; 100MM
REMARK 210 NACL; 0.01% NAN3; 100% D2O;
REMARK 210 0.7MM WW2 U-15N; 25MM PHOSPHATE
REMARK 210 BUFFER; 100MM NACL; 0.01% NAN3;
REMARK 210 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; HNHA
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 : SPARKY 3.11, CNS 1.1, ARIA 1.2
REMARK 210 METHOD USED : SIMULATED ANNEALING, MOLECULAR
REMARK 210 DYNAMICS, TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
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 : 1
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS CALCULATED USING NOE DATA DERIVED FROM
REMARK 210 1H NOESY IN H2O AND D2O, AND DIHEDRAL ANGLE DATA DERIVED FROM
REMARK 210 15N HNHA AND HNHB EXPERIMENTS.
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
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 ARG A 5 -35.84 -142.46
REMARK 500 1 ARG A 7 53.02 -91.29
REMARK 500 1 ALA A 9 -36.40 -167.83
REMARK 500 1 LYS A 34 62.64 77.11
REMARK 500 1 PRO A 41 43.75 -94.18
REMARK 500 1 LEU A 43 -79.78 -52.70
REMARK 500 1 PHE A 45 64.92 -102.16
REMARK 500 1 ASP A 49 -162.70 58.37
REMARK 500 1 ASN A 50 55.38 -147.31
REMARK 500 2 ALA A 3 -135.66 -95.18
REMARK 500 2 ARG A 5 -79.51 -71.36
REMARK 500 2 LEU A 43 -81.34 -74.12
REMARK 500 2 PHE A 45 55.05 -117.62
REMARK 500 2 ASN A 50 49.99 -143.00
REMARK 500 2 THR A 52 -91.61 -143.24
REMARK 500 3 ASP A 11 -84.39 -80.55
REMARK 500 3 LYS A 34 62.99 60.61
REMARK 500 3 PRO A 41 39.36 -86.39
REMARK 500 3 LEU A 43 -81.65 -112.57
REMARK 500 3 ASP A 49 -81.19 -59.20
REMARK 500 4 ARG A 7 -48.76 74.19
REMARK 500 4 ALA A 9 -24.84 -141.54
REMARK 500 4 PRO A 13 174.67 -58.82
REMARK 500 4 LYS A 34 39.49 74.31
REMARK 500 4 LEU A 43 -93.84 -88.54
REMARK 500 4 VAL A 47 152.81 77.00
REMARK 500 4 ASP A 48 85.85 70.99
REMARK 500 4 ASN A 50 -52.16 -167.80
REMARK 500 4 LYS A 53 100.88 -160.18
REMARK 500 5 SER A 2 -82.15 63.40
REMARK 500 5 LYS A 34 75.38 38.10
REMARK 500 5 PRO A 41 35.71 -88.79
REMARK 500 5 LEU A 43 -71.63 -50.96
REMARK 500 5 THR A 46 -102.44 -108.79
REMARK 500 5 VAL A 47 -44.34 -147.11
REMARK 500 5 ASP A 49 34.64 -156.75
REMARK 500 5 ASN A 50 -50.79 -123.66
REMARK 500 5 PRO A 51 -90.30 -63.77
REMARK 500 6 ARG A 5 167.68 72.45
REMARK 500 6 LYS A 34 61.29 62.15
REMARK 500 6 LEU A 43 -79.95 -87.92
REMARK 500 6 THR A 52 -70.63 -58.93
REMARK 500 6 LYS A 53 130.29 -171.03
REMARK 500 7 LYS A 6 -107.08 60.31
REMARK 500 7 ARG A 7 -58.56 -165.58
REMARK 500 7 ASP A 11 -88.89 -100.61
REMARK 500 7 LYS A 34 79.42 73.61
REMARK 500 7 LEU A 43 -88.61 -83.92
REMARK 500 7 ASP A 49 -42.29 -159.26
REMARK 500 8 ALA A 3 71.62 -110.04
REMARK 500
REMARK 500 THIS ENTRY HAS 137 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1WMV A 4 54 UNP Q9NZC7 WWOX_HUMAN 51 101
SEQADV 1WMV GLY A 1 UNP Q9NZC7 CLONING ARTIFACT
SEQADV 1WMV SER A 2 UNP Q9NZC7 CLONING ARTIFACT
SEQADV 1WMV ALA A 3 UNP Q9NZC7 CLONING ARTIFACT
SEQRES 1 A 54 GLY SER ALA LYS ARG LYS ARG VAL ALA GLY ASP LEU PRO
SEQRES 2 A 54 TYR GLY TRP GLU GLN GLU THR ASP GLU ASN GLY GLN VAL
SEQRES 3 A 54 PHE PHE VAL ASP HIS ILE ASN LYS ARG THR THR TYR LEU
SEQRES 4 A 54 ASP PRO ARG LEU ALA PHE THR VAL ASP ASP ASN PRO THR
SEQRES 5 A 54 LYS PRO
SHEET 1 A 3 TRP A 16 THR A 20 0
SHEET 2 A 3 VAL A 26 ASP A 30 -1 O PHE A 27 N GLU A 19
SHEET 3 A 3 THR A 36 THR A 37 -1 O THR A 37 N PHE A 28
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