Header list of 1ny8.pdb file
Complete list - b 23 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 11-FEB-03 1NY8
TITLE SOLUTION STRUCTURE OF PROTEIN YRBA FROM ESCHERICHIA COLI: NORTHEAST
TITLE 2 STRUCTURAL GENOMICS CONSORTIUM TARGET ER115
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN YRBA;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: YRBA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21MGK;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET21
KEYWDS ER115, YRBA, AUTOASSIGN, AUTOSTRUCTURE, NESG, STRUCTURAL GENOMICS,
KEYWDS 2 PSI, PROTEIN STRUCTURE INITIATIVE, NORTHEAST STRUCTURAL GENOMICS
KEYWDS 3 CONSORTIUM, UNKNOWN FUNCTION
EXPDTA SOLUTION NMR
NUMMDL 16
AUTHOR G.V.T.SWAPNA,J.Y.HUANG,T.B.ACTON,R.SHASTRY,Y.-W.CHIANG,
AUTHOR 2 G.T.MONTELIONE,NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG)
REVDAT 4 23-FEB-22 1NY8 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1NY8 1 VERSN
REVDAT 2 25-JAN-05 1NY8 1 AUTHOR KEYWDS REMARK
REVDAT 1 15-JUN-04 1NY8 0
JRNL AUTH G.V.T.SWAPNA,J.Y.HUANG,T.B.ACTON,R.SHASTRY,Y.-W.CHIANG,
JRNL AUTH 2 G.T.MONTELIONE
JRNL TITL SOLUTION STRUCTURE OF PROTEIN YRBA FROM ESCHERICHIA COLI:
JRNL TITL 2 NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET ER115
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1B, DYANA 1.5
REMARK 3 AUTHORS : VARIAN (VNMR), GUNTERT (DYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 1005 CONFORMATIONALLY-RESTRICTING NOE-DERIVED DISTANCE
REMARK 3 CONSTRAINTS. 74 DIHEDRAL ANGLE RESTRIANTS FROM TALOS AND 64
REMARK 3 HYDROGEN-BOND RESTRAINTS.
REMARK 4
REMARK 4 1NY8 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-FEB-03.
REMARK 100 THE DEPOSITION ID IS D_1000018343.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 5.5
REMARK 210 IONIC STRENGTH : 100 MM NACL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 13C,15N-ER115 0.8MM IN 20MM
REMARK 210 NH4OAC, 100MM NACL, 5MM CACL2,
REMARK 210 10MM DTT, 0.02% AZIDE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY
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 : NMRPIPE 2.1, SPARKY 3.106,
REMARK 210 AUTOASSIGN 1.9, AUTOSTRUCTURE
REMARK 210 1.1.2, HYPER 3.2
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 16
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
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 AUTOMATED RESONANCE ASSIGNMENTS OF BACKBONE RESONANCES USING
REMARK 210 AUTOASSIGN. MANUAL SIDECHAIN ASSIGNMENTS. AUTOMATED 3D 13C-NOESY
REMARK 210 AND 15N-NOESY ANALYSIS FOR STRUCTURE DETERMINATION USING
REMARK 210 AUTOSTRUCTURE
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 ASN A 65 H HIS A 68 1.48
REMARK 500 O SER A 46 H LYS A 50 1.55
REMARK 500 O TRP A 80 H ARG A 84 1.60
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 ILE A 2 122.48 -171.65
REMARK 500 1 ASP A 4 108.69 -179.79
REMARK 500 1 MET A 6 95.89 173.43
REMARK 500 1 GLU A 7 -146.86 -60.33
REMARK 500 1 ASN A 8 -0.74 81.23
REMARK 500 1 LEU A 19 112.15 -176.72
REMARK 500 1 SER A 20 -152.16 -75.43
REMARK 500 1 LEU A 21 -49.83 172.74
REMARK 500 1 GLN A 22 -62.81 173.67
REMARK 500 1 ASP A 29 -59.50 -121.73
REMARK 500 1 GLU A 40 -32.40 178.24
REMARK 500 1 PHE A 42 38.37 -84.85
REMARK 500 1 LYS A 50 -76.27 -70.08
REMARK 500 1 GLN A 52 -75.04 -66.01
REMARK 500 1 LEU A 58 39.15 -86.80
REMARK 500 1 ARG A 66 -37.93 -32.17
REMARK 500 1 ILE A 67 -32.83 -37.67
REMARK 500 1 HIS A 68 -147.38 -122.23
REMARK 500 1 TRP A 80 -75.99 -66.16
REMARK 500 1 LEU A 86 -165.02 -73.27
REMARK 500 1 GLU A 91 42.71 -179.84
REMARK 500 1 HIS A 93 77.97 69.32
REMARK 500 1 HIS A 95 120.84 62.60
REMARK 500 2 ILE A 2 87.53 76.32
REMARK 500 2 GLU A 3 115.10 -164.49
REMARK 500 2 ASP A 4 83.74 171.94
REMARK 500 2 MET A 6 -70.12 -164.31
REMARK 500 2 GLU A 7 45.58 166.54
REMARK 500 2 GLU A 10 -74.61 -39.40
REMARK 500 2 LEU A 19 -125.68 -165.03
REMARK 500 2 SER A 20 -161.26 176.61
REMARK 500 2 LEU A 21 -44.75 176.10
REMARK 500 2 GLN A 22 -70.32 154.93
REMARK 500 2 ASP A 29 -65.32 -122.67
REMARK 500 2 GLU A 40 19.08 -159.11
REMARK 500 2 PHE A 42 38.93 -87.74
REMARK 500 2 ARG A 47 -31.75 -37.18
REMARK 500 2 LYS A 50 -76.09 -70.70
REMARK 500 2 GLN A 52 -73.78 -64.87
REMARK 500 2 LEU A 58 38.93 -86.76
REMARK 500 2 ARG A 66 -35.41 -34.04
REMARK 500 2 ILE A 67 -37.80 -39.45
REMARK 500 2 HIS A 68 -146.33 -107.86
REMARK 500 2 ALA A 69 78.23 -150.66
REMARK 500 2 TRP A 80 -75.04 -60.33
REMARK 500 2 LEU A 86 -164.92 -75.08
REMARK 500 2 GLU A 91 -172.75 -178.52
REMARK 500 2 HIS A 92 100.42 -166.93
REMARK 500 2 HIS A 94 -179.76 63.62
REMARK 500 2 HIS A 95 80.40 68.09
REMARK 500
REMARK 500 THIS ENTRY HAS 382 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: ER115 RELATED DB: TARGETDB
DBREF 1NY8 A 1 89 UNP P0A9W6 YRBA_ECOLI 1 89
SEQADV 1NY8 LEU A 90 UNP P0A9W6 EXPRESSION TAG
SEQADV 1NY8 GLU A 91 UNP P0A9W6 EXPRESSION TAG
SEQADV 1NY8 HIS A 92 UNP P0A9W6 EXPRESSION TAG
SEQADV 1NY8 HIS A 93 UNP P0A9W6 EXPRESSION TAG
SEQADV 1NY8 HIS A 94 UNP P0A9W6 EXPRESSION TAG
SEQADV 1NY8 HIS A 95 UNP P0A9W6 EXPRESSION TAG
SEQADV 1NY8 HIS A 96 UNP P0A9W6 EXPRESSION TAG
SEQADV 1NY8 HIS A 97 UNP P0A9W6 EXPRESSION TAG
SEQRES 1 A 97 MET ILE GLU ASP PRO MET GLU ASN ASN GLU ILE GLN SER
SEQRES 2 A 97 VAL LEU MET ASN ALA LEU SER LEU GLN GLU VAL HIS VAL
SEQRES 3 A 97 SER GLY ASP GLY SER HIS PHE GLN VAL ILE ALA VAL GLY
SEQRES 4 A 97 GLU LEU PHE ASP GLY MET SER ARG VAL LYS LYS GLN GLN
SEQRES 5 A 97 THR VAL TYR GLY PRO LEU MET GLU TYR ILE ALA ASP ASN
SEQRES 6 A 97 ARG ILE HIS ALA VAL SER ILE LYS ALA TYR THR PRO ALA
SEQRES 7 A 97 GLU TRP ALA ARG ASP ARG LYS LEU ASN GLY PHE LEU GLU
SEQRES 8 A 97 HIS HIS HIS HIS HIS HIS
HELIX 1 1 ASN A 8 SER A 20 1 13
HELIX 2 2 SER A 46 GLY A 56 1 11
HELIX 3 3 LEU A 58 ARG A 66 1 9
HELIX 4 4 THR A 76 LEU A 86 1 11
SHEET 1 A 3 GLU A 23 GLY A 28 0
SHEET 2 A 3 HIS A 32 VAL A 38 -1 O ILE A 36 N HIS A 25
SHEET 3 A 3 ALA A 69 ALA A 74 1 O SER A 71 N VAL A 35
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 - b 23 2 Bytes