Header list of 2g7j.pdb file
Complete list - r 25 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 28-FEB-06 2G7J
TITLE SOLUTION NMR STRUCTURE OF THE PUTATIVE CYTOPLASMIC PROTEIN YGAC FROM
TITLE 2 SALMONELLA TYPHIMURIUM. NORTHEAST STRUCTURAL GENOMICS TARGET STR72.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE CYTOPLASMIC PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SALMONELLA TYPHIMURIUM;
SOURCE 3 ORGANISM_TAXID: 99287;
SOURCE 4 STRAIN: LT2;
SOURCE 5 GENE: YGAC;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)MGK;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PET21;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: STR72-21.1
KEYWDS STR72, AUTOSTRUCTURE, STRUCTURAL GENOMICS, PSI, PROTEIN STRUCTURE
KEYWDS 2 INITIATIVE, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM, NESG, UNKNOWN
KEYWDS 3 FUNCTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR J.M.ARAMINI,G.V.T.SWAPNA,T.A.RAMELOT,C.K.HO,K.CUNNINGHAM,L.-C.MA,
AUTHOR 2 K.SHETTY,R.XIAO,T.B.ACTON,M.A.KENNEDY,G.T.MONTELIONE,NORTHEAST
AUTHOR 3 STRUCTURAL GENOMICS CONSORTIUM (NESG)
REVDAT 3 13-JUL-11 2G7J 1 VERSN
REVDAT 2 24-FEB-09 2G7J 1 VERSN
REVDAT 1 02-MAY-06 2G7J 0
JRNL AUTH J.M.ARAMINI,G.V.T.SWAPNA,T.A.RAMELOT,C.K.HO,K.CUNNINGHAM,
JRNL AUTH 2 L.-C.MA,K.SHETTY,R.XIAO,T.B.ACTON,M.A.KENNEDY,G.T.MONTELIONE
JRNL TITL SOLUTION NMR STRUCTURE OF THE PUTATIVE CYTOPLASMIC PROTEIN
JRNL TITL 2 YGAC FROM SALMONELLA TYPHIMURIUM. NORTHEAST STRUCTURAL
JRNL TITL 3 GENOMICS TARGET STR72.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : AUTOSTRUCTURE 2.1.1, XPLOR-NIH 2.11.2, CNS 1.1
REMARK 3 AUTHORS : HUANG & MONTELIONE (AUTOSTRUCTURE), CLORE ET AL.
REMARK 3 (XPLOR-NIH), BRUNGER ET AL. (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 1759 CONFORMATIONALLY-RESTRICTING NOE-DERIVED DISTANCE
REMARK 3 CONSTRAINTS, 219 DIHEDRAL ANGLE CONSTRAINTS, AND 58 HYDROGEN BOND
REMARK 3 CONSTRAINTS (18.2 CONSTRAINTS PER RESIDUE, 6.7 LONG RANGE
REMARK 3 CONSTRAINTS PER RESIDUE, COMPUTED FOR RESIDUES 1 TO 112 BY PSVS
REMARK 3 1.2). STRUCTURE DETERMINATION WAS PERFORMED ITERATIVELY USING
REMARK 3 AUTOSTRUCTURE (XPLOR-NIH). AFTER A FINAL XPLOR CALCULATION USING
REMARK 3 THE FINAL CONSTRAINTS DERIVED FROM AUTOSTRUCTURE, THE 20 LOWEST
REMARK 3 ENERGY STRUCTURES OUT OF 100 WERE FURTHER REFINED BY RESTRAINED
REMARK 3 MOLECULAR DYANMICS/ENERGY MINIMIZATION IN EXPLICIT WATER (CNS).
REMARK 3 THE UNSTRUCTURED C-TERMINUS OF THE PROTEIN (EKTD + LEHHHHHH TAG)
REMARK 3 WERE INCLUDED IN ALL STRUCTURE CALCULATIONS BUT HAVE BEEN OMITTED
REMARK 3 FROM THIS DEPOSITION.
REMARK 4
REMARK 4 2G7J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-MAR-06.
REMARK 100 THE RCSB ID CODE IS RCSB036786.
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
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.12MM U-13C,15N STR72, 20MM
REMARK 210 MES, 100MM NACL, 5MM CACL2, 10MM
REMARK 210 DTT, 0.02% NAN3, PH 6.5, 5% D2O/
REMARK 210 95% H2O; 1.12MM U-13C,15N STR72,
REMARK 210 20MM MES, 100MM NACL, 5MM CACL2,
REMARK 210 10MM DTT, 0.02% NAN3, PH 6.5,
REMARK 210 100% D2O; 1.07MM 5%-13C,U-15N
REMARK 210 STR72, 20MM MES, 100MM NACL, 5MM
REMARK 210 CACL2, 10MM DTT, 0.02% NAN3, PH
REMARK 210 6.5, 5% D2O/95% H2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C-
REMARK 210 SEPARATED_NOESY; 4D_13C-
REMARK 210 SEPARATED_NOESY; HNHA; HIGH
REMARK 210 RESOLUTION CH-HSQC
REMARK 210 (STEREOSPECIFIC ASSIGNMENT OF
REMARK 210 VAL/LEU METHYLS); BACKBONE TR
REMARK 210 EXPTS; 3D HCCH-COSY; 3D TOCSYS,
REMARK 210 AROMATIC EXPTS
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE; INOVA
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 3.5PL6, VNMR 6.1C,
REMARK 210 SPARKY 3.110, AUTOASSIGN 1.17.0,
REMARK 210 PDBSTAT 4.01, PSVS 1.2
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE 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. AUTOMATED BACKBONE ASSIGNMENTS WERE MADE USING
REMARK 210 AUTOASSIGN, AND THE ASSIGNMENTS WERE COMPLETED MANUALLY.
REMARK 210 AUTOMATIC NOESY ASSIGNMENTS AS WELL AS DISTANCE AND HYDROGEN BOND
REMARK 210 CONSTRAINTS WERE DETERMINED USING AUTOSTRUCTURE. DIHEDRAL ANGLE
REMARK 210 CONSTRAINTS WERE DETERMINED USING HYPER AND TALOS. COMPLETENESS
REMARK 210 OF NMR ASSIGNMENTS (EXCLUDING C-TERMINAL HHHHHH): BACKBONE, 100%,
REMARK 210 SIDE CHAIN, 94.6%, AROMATICS, 91.1%, STEREOSPECIFIC METHYL, 94.4%
REMARK 210 . FINAL STRUCTURE QUALITY FACTORS (FOR RESIDUES 1 TO 112, PSVS
REMARK 210 1.2), WHERE ORDERED RESIDUES [S(PHI) + S(PSI) > 1.8] COMPRISE 3-
REMARK 210 43,49-50,55-66,69-71,75-76,88-96,98-109: (A) RMSD (ORDERED
REMARK 210 RESIDUES): BB, 0.6, HEAVY ATOM, 1.1. (B) RAMACHANDRAN STATISTICS
REMARK 210 FOR ORDERED RESIDUES: MOST FAVORED, 87.4%, ADDITIONALLY ALLOWED,
REMARK 210 12.4%, GENEROUSLY ALLOWED, 0.2%, DISALLOWED, 0.0%. (C) PROCHECK
REMARK 210 SCORES FOR ORDERED RESIDUES (RAW/Z-): PHI-PSI, -0.34/-1.02, ALL,
REMARK 210 -0.32/-1.89. (D) MOLPROBITY CLASH SCORE (RAW/Z-): 25.21/-2.80.
REMARK 210 (E) RPF SCORES FOR GOODNESS OF FIT TO NOESY DATA (ALL RESIDUES):
REMARK 210 RECALL, 0.971, PRECISION, 0.945, F-MEASURE, 0.958, DP-SCORE,
REMARK 210 0.846.
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-20
REMARK 465 RES C SSSEQI
REMARK 465 GLU A 113
REMARK 465 LYS A 114
REMARK 465 THR A 115
REMARK 465 ASP A 116
REMARK 465 LEU A 117
REMARK 465 GLU A 118
REMARK 465 HIS A 119
REMARK 465 HIS A 120
REMARK 465 HIS A 121
REMARK 465 HIS A 122
REMARK 465 HIS A 123
REMARK 465 HIS A 124
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 HG13 ILE A 51 H HIS A 52 1.16
REMARK 500 HB2 CYS A 72 HB2 HIS A 89 1.45
REMARK 500 HZ3 LYS A 56 OD1 ASP A 68 1.58
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 51 -86.40 -106.32
REMARK 500 1 PRO A 53 -168.14 -53.80
REMARK 500 1 ARG A 54 -50.38 74.50
REMARK 500 1 SER A 67 -111.93 -156.07
REMARK 500 1 ASP A 68 -69.29 -157.98
REMARK 500 1 ASN A 77 -29.53 66.41
REMARK 500 1 PHE A 78 -53.57 101.61
REMARK 500 1 PRO A 79 12.04 -68.51
REMARK 500 1 LEU A 80 106.33 -3.42
REMARK 500 1 SER A 97 18.97 -152.15
REMARK 500 2 ASP A 20 -69.31 -99.43
REMARK 500 2 PRO A 53 98.99 -60.56
REMARK 500 2 ARG A 54 -39.42 168.30
REMARK 500 2 SER A 67 -130.43 -162.46
REMARK 500 2 ASP A 68 -46.20 -157.27
REMARK 500 2 CYS A 72 123.11 175.29
REMARK 500 2 ASN A 77 -3.69 63.27
REMARK 500 2 PHE A 78 -60.68 101.98
REMARK 500 2 LEU A 80 118.86 66.49
REMARK 500 2 SER A 97 14.04 -152.64
REMARK 500 3 TYR A 2 165.83 67.27
REMARK 500 3 THR A 26 149.20 -171.53
REMARK 500 3 ALA A 48 -25.73 -160.59
REMARK 500 3 ILE A 51 -82.52 -72.72
REMARK 500 3 HIS A 52 138.34 -177.54
REMARK 500 3 PRO A 53 -172.11 -53.26
REMARK 500 3 ARG A 54 -44.68 70.36
REMARK 500 3 SER A 67 -130.16 -162.03
REMARK 500 3 ASP A 68 -46.20 -157.21
REMARK 500 3 CYS A 72 124.37 167.26
REMARK 500 3 ASN A 77 -85.24 60.87
REMARK 500 3 PHE A 78 -60.79 -174.63
REMARK 500 3 LEU A 80 116.85 45.68
REMARK 500 3 GLU A 85 -148.78 -79.29
REMARK 500 3 HIS A 87 13.44 -170.53
REMARK 500 3 SER A 97 17.12 -153.76
REMARK 500 4 ASP A 20 -62.03 -105.66
REMARK 500 4 ARG A 31 97.52 -173.51
REMARK 500 4 HIS A 52 144.84 73.27
REMARK 500 4 PRO A 53 -166.59 -59.31
REMARK 500 4 ARG A 54 -51.60 71.49
REMARK 500 4 LEU A 55 26.42 -79.16
REMARK 500 4 LYS A 56 -71.38 -60.23
REMARK 500 4 SER A 67 -116.99 -174.26
REMARK 500 4 ASP A 68 -66.83 -157.45
REMARK 500 4 TYR A 75 42.10 -80.57
REMARK 500 4 LEU A 80 133.36 76.28
REMARK 500 4 PHE A 96 -157.66 -137.24
REMARK 500 4 SER A 97 11.20 -152.57
REMARK 500 5 PRO A 53 -166.96 -57.47
REMARK 500
REMARK 500 THIS ENTRY HAS 256 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: STR72 RELATED DB: TARGETDB
DBREF 2G7J A 1 116 GB 16421350 AAL21686 1 116
SEQADV 2G7J LEU A 117 GB 16421350 CLONING ARTIFACT
SEQADV 2G7J GLU A 118 GB 16421350 CLONING ARTIFACT
SEQADV 2G7J HIS A 119 GB 16421350 EXPRESSION TAG
SEQADV 2G7J HIS A 120 GB 16421350 EXPRESSION TAG
SEQADV 2G7J HIS A 121 GB 16421350 EXPRESSION TAG
SEQADV 2G7J HIS A 122 GB 16421350 EXPRESSION TAG
SEQADV 2G7J HIS A 123 GB 16421350 EXPRESSION TAG
SEQADV 2G7J HIS A 124 GB 16421350 EXPRESSION TAG
SEQRES 1 A 124 MET TYR LEU ARG PRO ASP GLU VAL ALA ARG VAL LEU GLU
SEQRES 2 A 124 LYS ALA GLY PHE THR VAL ASP VAL VAL THR ASN LYS THR
SEQRES 3 A 124 TYR GLY TYR ARG ARG GLY GLU ASN TYR VAL TYR VAL ASN
SEQRES 4 A 124 ARG GLU ALA ARG MET GLY ARG THR ALA LEU ILE ILE HIS
SEQRES 5 A 124 PRO ARG LEU LYS ASP ARG SER SER SER LEU ALA ASP PRO
SEQRES 6 A 124 ALA SER ASP ILE LYS THR CYS ASP HIS TYR GLN ASN PHE
SEQRES 7 A 124 PRO LEU TYR LEU GLY GLY GLU THR HIS GLU HIS TYR GLY
SEQRES 8 A 124 ILE PRO HIS GLY PHE SER SER ARG ILE ALA LEU GLU ARG
SEQRES 9 A 124 TYR LEU ASN GLY LEU PHE GLY ASP GLU LYS THR ASP LEU
SEQRES 10 A 124 GLU HIS HIS HIS HIS HIS HIS
HELIX 1 1 ARG A 4 ALA A 15 1 12
HELIX 2 2 LEU A 55 ALA A 63 1 9
HELIX 3 3 SER A 98 GLY A 111 1 14
SHEET 1 A 5 THR A 18 THR A 23 0
SHEET 2 A 5 THR A 26 ARG A 31 -1 O GLY A 28 N VAL A 21
SHEET 3 A 5 ASN A 34 ASN A 39 -1 O VAL A 36 N TYR A 29
SHEET 4 A 5 LEU A 49 ILE A 50 -1 O ILE A 50 N TYR A 37
SHEET 5 A 5 PRO A 93 HIS A 94 -1 O HIS A 94 N LEU A 49
SHEET 1 B 2 LYS A 70 CYS A 72 0
SHEET 2 B 2 HIS A 89 GLY A 91 -1 O GLY A 91 N LYS A 70
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 25 2 Bytes