HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 31-DEC-08 2KCZ
TITLE SOLUTION NMR STRUCTURE OF THE C-TERMINAL DOMAIN OF PROTEIN DR_A0006
TITLE 2 FROM DEINOCOCCUS RADIODURANS. NORTHEAST STRUCTURAL GENOMICS
TITLE 3 CONSORTIUM TARGET DRR147D
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UNCHARACTERIZED PROTEIN DR_A0006;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 98-243;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS R1;
SOURCE 3 ORGANISM_TAXID: 243230;
SOURCE 4 STRAIN: R1 / DSM 20539 / IFO 15346 / LMG 4051 / NCIB 9279;
SOURCE 5 ATCC: 13939;
SOURCE 6 GENE: DR_A0006;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET21-23C
KEYWDS PROTEIN STRUCTURE, NESG, STRUCTURAL GENOMICS, UNKNOWN FUNCTION, PSI-
KEYWDS 2 2, PROTEIN STRUCTURE INITIATIVE, NORTHEAST STRUCTURAL GENOMICS
KEYWDS 3 CONSORTIUM
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR J.L.MILLS,A.GHOSH,E.GARCIA,H.WANG,C.CICCOSANTI,R.XIAO,R.NAIR,
AUTHOR 2 J.K.EVERETT,G.V.T.SWAPNA,T.B.ACTON,B.ROST,G.T.MONTELIONE,
AUTHOR 3 T.SZYPERSKI,NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG)
REVDAT 2 16-MAR-22 2KCZ 1 REMARK SEQADV
REVDAT 1 20-JAN-09 2KCZ 0
JRNL AUTH J.L.MILLS,A.GHOSH,E.GARCIA,H.WANG,C.CICCOSANTI,R.XIAO,
JRNL AUTH 2 R.NAIR,J.K.EVERETT,G.V.T.SWAPNA,T.B.ACTON,B.ROST,
JRNL AUTH 3 G.T.MONTELIONE,T.SZYPERSKI
JRNL TITL SOLUTION NMR STRUCTURE OF THE C-TERMINAL DOMAIN OF PROTEIN
JRNL TITL 2 DR_A0006 FROM DEINOCOCCUS RADIODURANS. NORTHEAST STRUCTURAL
JRNL TITL 3 GENOMICS CONSORTIUM TARGET DRR147D.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMRJ, CNS, PSVS
REMARK 3 AUTHORS : VARIAN (VNMRJ), BRUNGER, ADAMS, CLORE, GROS,
REMARK 3 NILGES AND READ (CNS), BHATTACHARYA AND MONTELIONE
REMARK 3 (PSVS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2KCZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-JAN-09.
REMARK 100 THE DEPOSITION ID IS D_1000100966.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 4.5
REMARK 210 IONIC STRENGTH : 435
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.9 MM [U-99% 13C; U-99% 15N]
REMARK 210 DRR147D-1, 10 % [U-2H] D2O-2, 90
REMARK 210 % H2O-3, 50 UM DSS-4, 10 MM DTT-
REMARK 210 5, 200 MM SODIUM CHLORIDE-6,
REMARK 210 0.02 % SODIUM AZIDE-7, 5 MM
REMARK 210 CALCIUM CHLORIDE-8, 20 MM
REMARK 210 AMMONIUM ACETATE-9, 90% H2O/10%
REMARK 210 D2O; 0.9 MM [U-5% 13C; U-99% 15N]
REMARK 210 DRR147D-10, 10 % [U-2H] D2O-11,
REMARK 210 90 % H2O-12, 50 UM DSS-13, 10 MM
REMARK 210 DTT-14, 200 MM SODIUM CHLORIDE-
REMARK 210 15, 0.02 % SODIUM AZIDE-16, 5 MM
REMARK 210 CALCIUM CHLORIDE-17, 20 MM
REMARK 210 AMMONIUM ACETATE-18, 90% H2O/10%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC; 2D 1H-13C HSQC;
REMARK 210 3D HNCO; 3D HNCACB; 3D CBCA(CO)
REMARK 210 NH; 3D HBHA(CO)NH; 3D HCCH-COSY;
REMARK 210 3D SIMULTANEOUS NCALICARO HH
REMARK 210 NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE, NMRDRAW, XEASY, SPSCAN,
REMARK 210 AUTOASSIGN, CSI, TALOS, CYANA,
REMARK 210 MOLMOL
REMARK 210 METHOD USED : SIMULATED ANNEALING, MOLECULAR
REMARK 210 DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET 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 HG21 THR A 34 H HIS A 35 1.32
REMARK 500 HG3 ARG A 78 H LEU A 80 1.34
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 ALA A 16 -47.48 174.01
REMARK 500 1 ASP A 25 33.90 -94.13
REMARK 500 1 LEU A 26 85.25 55.26
REMARK 500 1 THR A 34 -163.45 64.53
REMARK 500 1 GLU A 40 48.27 -82.12
REMARK 500 1 ASP A 43 -11.86 75.19
REMARK 500 1 ARG A 46 170.87 75.81
REMARK 500 1 SER A 47 -39.05 -165.12
REMARK 500 1 ARG A 48 99.83 64.26
REMARK 500 1 VAL A 51 -42.71 72.69
REMARK 500 1 ALA A 55 144.55 69.19
REMARK 500 1 ALA A 59 -52.91 -166.74
REMARK 500 1 SER A 61 -47.28 75.21
REMARK 500 1 LYS A 73 -77.39 -127.87
REMARK 500 1 SER A 79 24.84 -145.64
REMARK 500 1 LEU A 80 149.64 63.96
REMARK 500 1 ARG A 84 103.92 63.31
REMARK 500 1 PHE A 125 90.05 -166.96
REMARK 500 1 GLN A 131 171.80 71.08
REMARK 500 1 HIS A 153 109.01 65.87
REMARK 500 2 ALA A 16 -72.91 -178.26
REMARK 500 2 ASP A 25 67.17 -66.83
REMARK 500 2 LEU A 26 79.30 41.86
REMARK 500 2 LEU A 31 -68.23 -150.72
REMARK 500 2 LEU A 32 -80.13 64.51
REMARK 500 2 MET A 33 -60.84 -175.44
REMARK 500 2 THR A 34 -68.94 -157.16
REMARK 500 2 VAL A 39 -61.49 -152.48
REMARK 500 2 ASP A 43 -69.35 73.70
REMARK 500 2 LYS A 45 39.74 -90.98
REMARK 500 2 ARG A 46 140.25 74.46
REMARK 500 2 THR A 50 -63.04 72.95
REMARK 500 2 VAL A 51 89.85 -66.28
REMARK 500 2 PRO A 54 -164.64 -73.99
REMARK 500 2 SER A 61 -77.78 -67.96
REMARK 500 2 PRO A 71 94.35 -59.81
REMARK 500 2 LYS A 73 -72.56 -104.66
REMARK 500 2 ALA A 83 -168.89 -109.62
REMARK 500 2 GLU A 86 -85.48 -105.99
REMARK 500 2 PHE A 125 177.62 68.09
REMARK 500 2 ASN A 126 -177.39 65.60
REMARK 500 2 SER A 130 -41.92 69.80
REMARK 500 3 ALA A 16 -52.87 173.56
REMARK 500 3 ARG A 24 -76.09 -105.53
REMARK 500 3 THR A 34 -71.53 -80.32
REMARK 500 3 HIS A 35 96.18 -170.49
REMARK 500 3 LEU A 36 -29.46 -168.02
REMARK 500 3 LEU A 42 -61.52 -130.22
REMARK 500 3 ASP A 43 -41.51 73.28
REMARK 500 3 ARG A 46 157.73 74.01
REMARK 500
REMARK 500 THIS ENTRY HAS 453 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: DRR147D RELATED DB: TARGETDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 AUTHORS STATE THAT ALA AT POSITION 59 COMPARED TO THR IN
REMARK 999 THE SEQUENCE REFERENCE IS NOT A MUTATION BUT NATURALLY
REMARK 999 OCCURING STRAIN VARIATION.
DBREF 2KCZ A 2 147 UNP Q9RZE3 Q9RZE3_DEIRA 98 243
SEQADV 2KCZ MET A 1 UNP Q9RZE3 EXPRESSION TAG
SEQADV 2KCZ ALA A 59 UNP Q9RZE3 THR 155 SEE REMARK 999
SEQADV 2KCZ LEU A 148 UNP Q9RZE3 EXPRESSION TAG
SEQADV 2KCZ GLU A 149 UNP Q9RZE3 EXPRESSION TAG
SEQADV 2KCZ HIS A 150 UNP Q9RZE3 EXPRESSION TAG
SEQADV 2KCZ HIS A 151 UNP Q9RZE3 EXPRESSION TAG
SEQADV 2KCZ HIS A 152 UNP Q9RZE3 EXPRESSION TAG
SEQADV 2KCZ HIS A 153 UNP Q9RZE3 EXPRESSION TAG
SEQADV 2KCZ HIS A 154 UNP Q9RZE3 EXPRESSION TAG
SEQADV 2KCZ HIS A 155 UNP Q9RZE3 EXPRESSION TAG
SEQRES 1 A 155 MET GLY GLU THR VAL VAL ARG ASP ALA VAL THR ILE GLY
SEQRES 2 A 155 LYS PRO ALA GLU GLN LEU TYR ALA VAL TRP ARG ASP LEU
SEQRES 3 A 155 PRO GLY LEU PRO LEU LEU MET THR HIS LEU ARG SER VAL
SEQRES 4 A 155 GLU VAL LEU ASP ASP LYS ARG SER ARG TRP THR VAL GLU
SEQRES 5 A 155 ALA PRO ALA PRO LEU GLY ALA VAL SER TRP GLU ALA GLU
SEQRES 6 A 155 LEU THR ALA ASP GLU PRO GLY LYS ARG ILE ALA TRP ARG
SEQRES 7 A 155 SER LEU PRO GLY ALA ARG ILE GLU ASN SER GLY GLU VAL
SEQRES 8 A 155 LEU PHE ARG PRO ALA PRO GLY ALA ARG GLY THR GLU VAL
SEQRES 9 A 155 VAL VAL ARG LEU THR TYR ARG PRO PRO GLY GLY SER ALA
SEQRES 10 A 155 GLY ALA VAL ILE ALA ARG MET PHE ASN GLN GLU PRO SER
SEQRES 11 A 155 GLN GLN LEU ARG ASP ASP LEU MET ARG PHE LYS ARG GLU
SEQRES 12 A 155 GLN GLU LEU GLY LEU GLU HIS HIS HIS HIS HIS HIS
HELIX 1 1 ALA A 16 ALA A 21 1 6
HELIX 2 2 VAL A 22 ARG A 24 5 3
HELIX 3 3 SER A 79 ARG A 84 1 6
HELIX 4 4 PRO A 97 ARG A 100 5 4
HELIX 5 5 SER A 116 ILE A 121 1 6
HELIX 6 6 ALA A 122 PHE A 125 5 4
HELIX 7 7 ARG A 134 GLY A 147 1 14
SHEET 1 A 4 THR A 4 ILE A 12 0
SHEET 2 A 4 THR A 102 TYR A 110 -1 O VAL A 104 N VAL A 10
SHEET 3 A 4 GLU A 90 PRO A 95 -1 N ARG A 94 O GLU A 103
SHEET 4 A 4 ARG A 74 ALA A 76 -1 N ILE A 75 O VAL A 91
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
(ATOM LINES ARE NOT SHOWN.)
END
