Header list of 2gbs.pdb file
Complete list - t 20 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 11-MAR-06 2GBS
TITLE NMR STRUCTURE OF RPA0253 FROM RHODOPSEUDOMONAS PALUSTRIS. NORTHEAST
TITLE 2 STRUCTURAL GENOMICS CONSORTIUM TARGET RPR3
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYPOTHETICAL PROTEIN RPA0253;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOPSEUDOMONAS PALUSTRIS;
SOURCE 3 ORGANISM_TAXID: 258594;
SOURCE 4 STRAIN: CGA009;
SOURCE 5 GENE: RPA0253;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: XL-GOLD+PMGK;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PET21
KEYWDS ALPHA-BETA, RPR3, NESG, STRUCTURAL GENOMICS, RPA0253, COG2947, PSI,
KEYWDS 2 PROTEIN STRUCTURE INITIATIVE, NORTHEAST STRUCTURAL GENOMICS
KEYWDS 3 CONSORTIUM, UNKNOWN FUNCTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR T.A.RAMELOT,J.R.CORT,K.CONOVER,Y.CHEN,L.C.MA,M.CIANO,R.XIAO,
AUTHOR 2 T.B.ACTON,G.T.MONTELIONE,M.A.KENNEDY,NORTHEAST STRUCTURAL GENOMICS
AUTHOR 3 CONSORTIUM (NESG)
REVDAT 5 20-OCT-21 2GBS 1 REMARK SEQADV
REVDAT 4 13-JUL-11 2GBS 1 VERSN
REVDAT 3 09-JUN-10 2GBS 1 JRNL
REVDAT 2 24-FEB-09 2GBS 1 VERSN
REVDAT 1 11-APR-06 2GBS 0
JRNL AUTH C.BERTONATI,M.PUNTA,M.FISCHER,G.YACHDAV,F.FOROUHAR,W.ZHOU,
JRNL AUTH 2 A.P.KUZIN,J.SEETHARAMAN,M.ABASHIDZE,T.A.RAMELOT,M.A.KENNEDY,
JRNL AUTH 3 J.R.CORT,A.BELACHEW,J.F.HUNT,L.TONG,G.T.MONTELIONE,B.ROST
JRNL TITL STRUCTURAL GENOMICS REVEALS EVE AS A NEW ASCH/PUA-RELATED
JRNL TITL 2 DOMAIN.
JRNL REF PROTEINS V. 75 760 2009
JRNL REFN ISSN 0887-3585
JRNL PMID 19191354
JRNL DOI 10.1002/PROT.22287
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : SPARKY 3.1, CNS 1.1
REMARK 3 AUTHORS : T.D. GODDARD AND D.G. KNELLER (SPARKY), A.
REMARK 3 BRUNGER, G.L. WARREN (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 1690 RESTRAINTS. 1512 ARE
REMARK 3 NOE-DERIVED; SEQUENTIAL [(I-J)=1] = 201; MEDIUM RANGE [1<(I-J)<5] =
REMARK 3 411; LONG RANGE [(I-J)>=5] = 900; HYDROGEN BOND RESTRAINTS = 80
REMARK 3 (2 PER H-BOND); NUMBER OF NOE RESTRAINTS PER RESIDUE = 11.0
REMARK 3 (RESIDES 2-138); DIHEDRAL-ANGLE RESTRAINTS = 178 (89 PHI, 89 PSI);
REMARK 3 TOTAL NUMBER OF RESTRAINTS PER RESIDUE = 12.2 (RESIDES 1-138);
REMARK 3 NUMBER OF LONG RANGE RESTRAINTS PER RESIDUE = 6.5; NUMBER OF
REMARK 3 STRUCTURES COMPUTED = 20; NUMBER OF STRUCTURES USED = 20. AVERAGE
REMARK 3 DISTANCE VIOLATIONS >0.1 ANG = 0; AVERAGE RMS DISTANCE VIOLATION /
REMARK 3 CONSTRAINT = 0.001 ANG.; MAXIMUM DISTANCE VIOLATION 0.038.
REMARK 3 AVERAGE DIHEDRAL ANGLE VIOLATIONS: >1 DEG = 0; MAX DIHEDRAL ANGLE
REMARK 3 VIOLATION = 0.73; AVERAGE RMS ANGLE VIOLATION / CONSTRAINT = 0.03
REMARK 3 DEG. RMSD VALUES: BACKBONE ATOMS (N,C,C', RESIDUES 2-136) = 0.57
REMARK 3 ANG; ALL HEAVY ATOMS = 0.93 ANG; PROCHECK (RESIDUES 2-136): MOST
REMARK 3 FAVORED REGIONS = 90%; ADDITIONAL ALLOWED REGIONS = 9%; GENEROUSLY
REMARK 3 ALLOWED REGIONS = 0%; DISALLOWED REGIONS = 1%.
REMARK 3
REMARK 3 THE 8 RESIDUE C-TERMINAL HIS TAG (LEHHHHHH) WAS INCLUDED IN THE
REMARK 3 STRUCTURE CALCULATION.
REMARK 4
REMARK 4 2GBS COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-MAR-06.
REMARK 100 THE DEPOSITION ID IS D_1000036929.
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 : 100MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1 MM RPA0253, U-15N, 13C; 20MM
REMARK 210 MES, 100MM NACL, 5MM CACL2, 10
REMARK 210 MM DTT, 0.02% NAN3; 95% H2O, 5%
REMARK 210 D2O, PH 6.5
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 4D_13C-
REMARK 210 SEPARATED_NOESY; HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE LINUX9, AUTOSTRUCTURE
REMARK 210 2.1.1, X-PLOR XPLOR-NIH-2.10,
REMARK 210 VNMR 6.1C
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING, TORSION ANGLE
REMARK 210 DYNAMICS, CNS WATER REFINEMENT
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : ALL CALCULATED STRUCTURES
REMARK 210 SUBMITTED
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 HZ2 LYS A 21 OE2 GLU A 26 1.57
REMARK 500 OD2 ASP A 89 HZ1 LYS A 90 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 ASN A 55 -74.23 72.62
REMARK 500 1 ASP A 89 -72.69 -83.37
REMARK 500 1 LEU A 137 42.08 -88.93
REMARK 500 2 VAL A 12 -61.20 -105.40
REMARK 500 2 ASN A 55 -65.61 71.84
REMARK 500 2 LYS A 58 74.55 54.68
REMARK 500 2 ALA A 88 99.14 -64.68
REMARK 500 2 HIS A 140 -68.18 69.48
REMARK 500 2 HIS A 141 -40.84 -175.65
REMARK 500 2 HIS A 142 129.80 72.86
REMARK 500 2 HIS A 143 96.98 37.68
REMARK 500 3 VAL A 12 -68.25 -94.37
REMARK 500 3 ASN A 55 -74.45 70.33
REMARK 500 3 ASP A 89 -71.99 -94.16
REMARK 500 3 LEU A 138 -67.93 -155.48
REMARK 500 3 HIS A 141 -9.41 -176.32
REMARK 500 4 ASN A 55 -82.45 66.90
REMARK 500 4 HIS A 140 134.00 73.96
REMARK 500 4 HIS A 144 119.13 -178.41
REMARK 500 5 ASN A 55 -64.83 70.45
REMARK 500 5 PRO A 105 -7.73 -58.64
REMARK 500 5 LYS A 114 -55.28 -130.03
REMARK 500 5 HIS A 140 -76.77 67.81
REMARK 500 5 HIS A 141 -56.78 -158.85
REMARK 500 5 HIS A 142 149.65 70.44
REMARK 500 5 HIS A 143 94.40 59.10
REMARK 500 5 HIS A 144 70.86 -108.70
REMARK 500 6 ASN A 55 -80.18 66.59
REMARK 500 6 ASP A 89 -74.37 -79.15
REMARK 500 6 LYS A 114 -60.81 -121.96
REMARK 500 7 VAL A 12 -63.46 -94.69
REMARK 500 7 ASN A 55 -72.07 71.16
REMARK 500 7 GLU A 69 -165.96 -69.55
REMARK 500 7 ALA A 70 104.66 -48.62
REMARK 500 7 PHE A 81 -165.69 -108.79
REMARK 500 7 HIS A 141 -103.26 52.46
REMARK 500 7 HIS A 142 18.85 -172.78
REMARK 500 8 ASN A 55 -71.23 67.40
REMARK 500 8 SER A 78 30.54 -165.79
REMARK 500 8 LYS A 80 -25.36 -169.02
REMARK 500 8 LEU A 138 19.59 -153.60
REMARK 500 9 ASN A 55 -69.75 70.45
REMARK 500 9 ARG A 68 118.06 -165.55
REMARK 500 9 LYS A 114 -60.37 -103.11
REMARK 500 10 VAL A 12 -60.51 -103.36
REMARK 500 10 ASN A 55 -69.53 69.35
REMARK 500 10 LYS A 58 70.45 55.08
REMARK 500 10 HIS A 144 24.86 -152.02
REMARK 500 11 VAL A 12 -61.94 -124.35
REMARK 500 11 ASN A 55 -76.70 68.72
REMARK 500
REMARK 500 THIS ENTRY HAS 95 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 7004 RELATED DB: BMRB
REMARK 900 RELATED ID: RPR3 RELATED DB: TARGETDB
DBREF 2GBS A 1 137 UNP Q6ND56 Q6ND56_RHOPA 1 137
SEQADV 2GBS VAL A 1 UNP Q6ND56 MET 1 ENGINEERED MUTATION
SEQADV 2GBS LEU A 138 UNP Q6ND56 CLONING ARTIFACT
SEQADV 2GBS GLU A 139 UNP Q6ND56 CLONING ARTIFACT
SEQADV 2GBS HIS A 140 UNP Q6ND56 CLONING ARTIFACT
SEQADV 2GBS HIS A 141 UNP Q6ND56 CLONING ARTIFACT
SEQADV 2GBS HIS A 142 UNP Q6ND56 CLONING ARTIFACT
SEQADV 2GBS HIS A 143 UNP Q6ND56 CLONING ARTIFACT
SEQADV 2GBS HIS A 144 UNP Q6ND56 CLONING ARTIFACT
SEQADV 2GBS HIS A 145 UNP Q6ND56 CLONING ARTIFACT
SEQRES 1 A 145 VAL ALA TYR TRP LEU VAL LYS SER GLU PRO SER VAL TRP
SEQRES 2 A 145 SER TRP ASP GLN GLN VAL ALA LYS GLY ALA ALA GLY GLU
SEQRES 3 A 145 ALA TRP THR GLY VAL ARG ASN HIS SER ALA LYS LEU HIS
SEQRES 4 A 145 MET VAL ALA MET ARG ARG GLY ASP ARG ALA PHE TYR TYR
SEQRES 5 A 145 HIS SER ASN GLU GLY LYS GLU ILE VAL GLY ILE ALA GLU
SEQRES 6 A 145 ILE ILE ARG GLU ALA TYR PRO ASP PRO THR ASP ALA SER
SEQRES 7 A 145 GLY LYS PHE VAL CYS VAL ASP ILE LYS ALA ASP LYS PRO
SEQRES 8 A 145 LEU LYS THR PRO VAL THR LEU ALA ALA VAL LYS ALA GLU
SEQRES 9 A 145 PRO ARG LEU ALA ASP MET ALA LEU MET LYS TYR SER ARG
SEQRES 10 A 145 LEU SER VAL GLN PRO VAL THR ALA GLU GLU TRP LYS LEU
SEQRES 11 A 145 VAL CYS LYS MET GLY GLY LEU LEU GLU HIS HIS HIS HIS
SEQRES 12 A 145 HIS HIS
HELIX 1 1 SER A 14 ALA A 20 1 7
HELIX 2 2 ASN A 33 MET A 43 1 11
HELIX 3 3 LEU A 98 GLU A 104 1 7
HELIX 4 4 ARG A 106 ASP A 109 5 4
HELIX 5 5 MET A 110 TYR A 115 1 6
HELIX 6 6 THR A 124 GLY A 135 1 12
SHEET 1 A 6 GLU A 26 ALA A 27 0
SHEET 2 A 6 VAL A 82 THR A 97 -1 O ILE A 86 N GLU A 26
SHEET 3 A 6 GLU A 59 PRO A 72 -1 N ILE A 67 O ASP A 85
SHEET 4 A 6 ARG A 48 HIS A 53 -1 N HIS A 53 O GLU A 59
SHEET 5 A 6 TYR A 3 SER A 8 1 N SER A 8 O TYR A 52
SHEET 6 A 6 GLN A 121 VAL A 123 -1 O VAL A 123 N TYR A 3
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 - t 20 2 Bytes