Header list of 1ywl.pdb file
Complete list - r 2 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 18-FEB-05 1YWL
TITLE SOLUTION NMR STRUCTURE OF THE PROTEIN EF2693 FROM E. FAECALIS:
TITLE 2 NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET EFR36
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYPOTHETICAL UPF0213 PROTEIN EF2693;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ENTEROCOCCUS FAECALIS;
SOURCE 3 ORGANISM_TAXID: 1351;
SOURCE 4 GENE: EF2693;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PMGK;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET21
KEYWDS ALPHA AND BETA, STRUCTURAL GENOMICS, NORTHEAST STRUCTURAL GENOMICS
KEYWDS 2 CONSORTIUM (NESG), PROTEIN STRUCTURE INITIATIVE (PSI), UNKNOWN
KEYWDS 3 FUNCTION
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG)
REVDAT 3 02-MAR-22 1YWL 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1YWL 1 VERSN
REVDAT 1 29-MAR-05 1YWL 0
JRNL AUTH G.V.T.SWAPNA,A.BHATTACHARYA,J.M.ARAMINI,T.B.ACTON,L.MA,
JRNL AUTH 2 R.XIAO,R.SHASTRY,L.SHIH,K.E.CUNNINGHAM,G.T.MONTELIONE
JRNL TITL SOLUTION NMR STRUCTURE OF THE PROTEIN EF2693 FROM E.
JRNL TITL 2 FAECALIS: NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET
JRNL TITL 3 EFR36
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA 1.5, PSVS 1.0
REMARK 3 AUTHORS : GUENTERT, ET AL (DYANA), BHATTACHARYA (PSVS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 912 CONFORMATIONALLY-RESTRICTING NOE-DERIVED DISTANCE RESTRAINTS,
REMARK 3 216 DIHEDRAL RESTRAINTS AND 54 HYDROGEN BOND RESTRAINTS.
REMARK 4
REMARK 4 1YWL COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-MAR-05.
REMARK 100 THE DEPOSITION ID IS D_1000032003.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 100 MM NACL, 5 MM CACL2
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 5% D2O, 0.02% NAN3, 10MM DTT,
REMARK 210 5MM CACL2, 100MM NACL, 20MM MES,
REMARK 210 5 % D20, 95 % H20
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE; INOVA
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : AUTOSTRUCTURE 2.0.0, AUTOASSIGN
REMARK 210 1.14, NMRPIPE 2.1, VNMR 6.1B,
REMARK 210 XWINNMR 3.5, PDBSTAT 4.01, HYPER
REMARK 210 3.2, TALOS 2.1, SPINS 5.0
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 56
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY. AUTOMATIC BACKBONE RESONANCE ASSIGNMENTS WERE MADE
REMARK 210 USING AUTOASSIGN. SIDE-CHAIN ASSIGNMENTS WERE MADE MANUALLY.
REMARK 210 AUTOMATIC NOE ASSIGNMENTS WERE MADE USING AUTOSTRUCTURE.
REMARK 210 DIHEDRAL ANGLE RESTRAINTS WERE MADE USING HYPER AND TALOS. THE
REMARK 210 SPINS DATABASE SOFTWARE WAS USED AS AN INTEGRATING AGENT. PSVS
REMARK 210 WAS USED TO VALIDATE STRUCTURE QUALITY.
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 GLN A 82 H THR A 86 1.51
REMARK 500 O GLN A 79 H TYR A 83 1.56
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 GLU A 2 -175.21 -54.59
REMARK 500 1 ASN A 3 76.21 59.81
REMARK 500 1 LYS A 4 83.57 163.19
REMARK 500 1 LYS A 5 -168.38 45.19
REMARK 500 1 SER A 6 131.18 61.73
REMARK 500 1 GLU A 26 63.73 67.59
REMARK 500 1 LEU A 31 -71.84 -72.01
REMARK 500 1 SER A 36 41.82 -90.94
REMARK 500 1 LYS A 41 -73.77 -120.60
REMARK 500 1 ALA A 46 100.84 63.65
REMARK 500 1 ARG A 49 84.27 53.93
REMARK 500 1 LYS A 78 -75.02 -91.85
REMARK 500 1 TYR A 83 -39.99 -37.32
REMARK 500 1 HIS A 91 88.05 -155.62
REMARK 500 1 HIS A 93 139.42 -176.23
REMARK 500 1 HIS A 94 126.61 62.51
REMARK 500 1 HIS A 95 175.05 57.84
REMARK 500 2 LYS A 5 167.79 56.48
REMARK 500 2 SER A 6 -150.75 80.17
REMARK 500 2 GLU A 26 68.05 73.97
REMARK 500 2 GLU A 33 -73.00 -51.87
REMARK 500 2 THR A 38 -56.79 -157.88
REMARK 500 2 TYR A 42 -68.72 66.39
REMARK 500 2 ARG A 48 169.32 -45.81
REMARK 500 2 ARG A 49 95.82 67.50
REMARK 500 2 ILE A 54 41.86 -152.65
REMARK 500 2 HIS A 55 101.89 174.16
REMARK 500 2 THR A 76 -165.53 -116.69
REMARK 500 2 LYS A 78 -74.31 -90.94
REMARK 500 2 THR A 86 -33.64 -38.86
REMARK 500 3 GLU A 2 -169.29 -58.50
REMARK 500 3 ASN A 3 152.48 67.28
REMARK 500 3 LYS A 4 178.58 85.51
REMARK 500 3 LYS A 5 -176.88 -52.10
REMARK 500 3 SER A 6 138.34 66.51
REMARK 500 3 THR A 38 98.98 60.57
REMARK 500 3 ALA A 40 -59.68 -132.46
REMARK 500 3 THR A 43 119.41 -169.00
REMARK 500 3 ALA A 46 86.17 56.87
REMARK 500 3 ARG A 49 85.46 70.87
REMARK 500 3 ARG A 77 -19.52 -49.93
REMARK 500 3 LYS A 78 -74.09 -98.47
REMARK 500 4 GLU A 2 77.21 -159.31
REMARK 500 4 LYS A 5 152.54 72.86
REMARK 500 4 SER A 6 -168.89 85.75
REMARK 500 4 GLU A 26 74.09 77.95
REMARK 500 4 THR A 38 -87.25 58.89
REMARK 500 4 ALA A 40 153.93 177.77
REMARK 500 4 TYR A 42 -50.21 -138.20
REMARK 500 4 ALA A 46 88.75 -63.50
REMARK 500
REMARK 500 THIS ENTRY HAS 138 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EFR36 RELATED DB: TARGETDB
DBREF 1YWL A 1 88 UNP Q830S9 Y2693_ENTFA 1 88
SEQADV 1YWL LEU A 89 UNP Q830S9 CLONING ARTIFACT
SEQADV 1YWL GLU A 90 UNP Q830S9 CLONING ARTIFACT
SEQADV 1YWL HIS A 91 UNP Q830S9 CLONING ARTIFACT
SEQADV 1YWL HIS A 92 UNP Q830S9 CLONING ARTIFACT
SEQADV 1YWL HIS A 93 UNP Q830S9 CLONING ARTIFACT
SEQADV 1YWL HIS A 94 UNP Q830S9 CLONING ARTIFACT
SEQADV 1YWL HIS A 95 UNP Q830S9 CLONING ARTIFACT
SEQADV 1YWL HIS A 96 UNP Q830S9 CLONING ARTIFACT
SEQRES 1 A 96 MET GLU ASN LYS LYS SER HIS TYR PHE TYR VAL LEU LEU
SEQRES 2 A 96 CYS GLN ASP GLY SER PHE TYR GLY GLY TYR THR THR GLU
SEQRES 3 A 96 PRO GLU ARG ARG LEU THR GLU HIS ASN SER GLY THR GLY
SEQRES 4 A 96 ALA LYS TYR THR ARG LEU ALA LYS ARG ARG PRO VAL ILE
SEQRES 5 A 96 MET ILE HIS THR GLU LYS PHE GLU THR ARG SER GLU ALA
SEQRES 6 A 96 THR LYS ALA GLU ALA ALA PHE LYS LYS LEU THR ARG LYS
SEQRES 7 A 96 GLN LYS GLU GLN TYR LEU LYS THR PHE HIS LEU GLU HIS
SEQRES 8 A 96 HIS HIS HIS HIS HIS
HELIX 1 1 GLU A 26 GLY A 39 1 14
HELIX 2 2 THR A 61 LEU A 75 1 15
HELIX 3 3 THR A 76 GLU A 90 1 15
SHEET 1 A 3 TYR A 20 THR A 24 0
SHEET 2 A 3 HIS A 7 LEU A 13 -1 N TYR A 10 O GLY A 22
SHEET 3 A 3 ILE A 52 PHE A 59 -1 O GLU A 57 N PHE A 9
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