Header list of 2fvt.pdb file
Complete list - r 9 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 31-JAN-06 2FVT TITLE NMR STRUCTURE OF THE RPA2829 PROTEIN FROM RHODOPSEUDOMONAS PALUSTRIS: TITLE 2 NORTHEAST STRUCTURAL GENOMICS TARGET RPR43 COMPND MOL_ID: 1; COMPND 2 MOLECULE: CONSERVED HYPOTHETICAL PROTEIN; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: RHODOPSEUDOMONAS PALUSTRIS; SOURCE 3 ORGANISM_TAXID: 1076; SOURCE 4 GENE: RPA2829; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)+MAGIC; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET21 KEYWDS MTH938-LIKE FOLD, STRUCTURAL GENOMICS, PSI, PROTEIN STRUCTURE KEYWDS 2 INITIATIVE, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM, NESG, UNKNOWN KEYWDS 3 FUNCTION EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR J.R.CORT,C.K.HO,K.CUNNINGHAM,L.C.MA,K.CONOVER,R.XIAO,G.T.MONTELIONE, AUTHOR 2 M.A.KENNEDY,NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG) REVDAT 3 09-MAR-22 2FVT 1 REMARK SEQADV REVDAT 2 24-FEB-09 2FVT 1 VERSN REVDAT 1 14-FEB-06 2FVT 0 JRNL AUTH J.R.CORT,C.K.HO,K.CUNNINGHAM,L.C.MA,K.CONOVER,R.XIAO, JRNL AUTH 2 G.T.MONTELIONE,M.A.KENNEDY JRNL TITL NMR STRUCTURE OF THE RPA2829 PROTEIN FROM RHODOPSEUDOMONAS JRNL TITL 2 PALUSTRIS JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : VNMR 6.1C, X-PLOR NIH-XPLOR, CNS 1.1 REMARK 3 AUTHORS : VARIAN (VNMR), A. BRUNGER (X-PLOR), A. BRUNGER REMARK 3 (CNS) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 1039 RESTRAINTS. SUMMARY OF REMARK 3 EXPERIMENTAL CONSTRAINTS: RESTRAINING DISTANCE RESTRAINTS: TOTAL = REMARK 3 864; INTRA-RESIDUE [I=J] = 160; SEQUENTIAL [(I-J)=1] = 225; MEDIUM REMARK 3 RANGE [1<(I-J)<5] = 131; LONG RANGE [(I-J)>=5] = 348; HYDROGEN REMARK 3 BOND RESTRAINTS = 72 (2 PER H-BOND); NUMBER OF RESTRAINING REMARK 3 DISTANCE RESTRAINTS PER RESTRAINED RESIDUE = 8.2; DIHEDRAL-ANGLE REMARK 3 RESTRAINTS = 103 (50 PHI, 52 PSI, 1 CHI-1); TOTAL NUMBER OF REMARK 3 RESTRAINTS PER RESTRAINED RESIDUE = 8.9; NUMBER OF LONG RANGE NOE REMARK 3 DISTANCE RESTRAINTS PER RESTRAINED RESIDUE = 3.0; NUMBER OF REMARK 3 STRUCTURES COMPUTED = 30; NUMBER OF STRUCTURES USED = 20. AVERAGE REMARK 3 DISTANCE VIOLATIONS >0.0001 ANG = 26.8+/-6; AVERAGE R.M.S. REMARK 3 DISTANCE VIOLATION = 0.005 +/- 0.001 ANG; MAXIMUM NUMBER OF REMARK 3 DISTANCE VIOLATIONS 39.MAXIMUM DISTANCE VIOLATION = 0.26 ANG; REMARK 3 AVERAGE DIHEDRAL ANGLE VIOLATIONS: >0.0001 DEG = 3.3+/-1.3; MAX REMARK 3 NUMBER OF DIHEDRAL ANGLE VIOLATIONS = 5; AVERAGE R.M.S. ANGLE REMARK 3 VIOLATION = 0.42 +/- .01 DEG.; RMSD VALUES: BACKBONE ATOMS (N,C,C' REMARK 3 RESIDUES 10-126) = 0.86 ANG, ALL HEAVY ATOMS = 1.52 ANG; BACKBONE REMARK 3 ATOMS (N,C,C' RESIDUES 33-126) = 0.68 ANG, ALL HEAVY ATOMS = REMARK 3 1.1.38 ANG; BACKBONE ATOMS (N,C,C' RESIDUES 12-16,24-26,34-39,41- REMARK 3 49,52-74,79-92,95-114,119-126) = 0.67 ANG,ALL HEAVY ATOMS = 1.19 REMARK 3 ANG; REMARK 3 PROCHECK (RESDIUES 10-126): MOST FAVORED REGIONS = 83.8%; REMARK 3 ADDITIONAL ALLOWED REGIONS = 14.9%; GENEROUSLY ALLOWED REGIONS = REMARK 3 1.9%; DISALLOWED REGIONS = 0.4%. REMARK 4 REMARK 4 2FVT COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-FEB-06. REMARK 100 THE DEPOSITION ID IS D_1000036372. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 293; 293 REMARK 210 PH : 5.0; 4.5 REMARK 210 IONIC STRENGTH : 100 MM NACL; 5MM CACL2; 20 MM REMARK 210 AMMONIUM ACETATE; 100 MM NACL; REMARK 210 5MM CACL2; 20 MM AMMONIUM ACETATE REMARK 210 PRESSURE : AMBIENT; AMBIENT REMARK 210 SAMPLE CONTENTS : 1.2 MM RPA2829 U-15N,13C; 20 MM REMARK 210 AMMONIUM ACETATE PH 5.0; 100 MM REMARK 210 NACL; 5MM CACL2; 0.02% NAN3; 10 REMARK 210 MM DTT; 95% H2O; 10% D2O; 1.2 MM REMARK 210 RPA2829 U-15N,13C; 20 MM REMARK 210 AMMONIUM ACETATE PH 5.0; 100 MM REMARK 210 NACL, 5MM CACL2, 0.02% NAN3; 100% REMARK 210 D2O; 0.8 MM RPA2829 U-15N,5% REMARK 210 FRACTIONALLY LABELED 13C; 20 MM REMARK 210 AMMONIUM ACETATE PH 4.5; 100 MM REMARK 210 NACL, 5MM CACL2, 0.02% NAN3; 95% REMARK 210 H2O; 10% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 4D_13C-SEPARATED_NOESY; 3D_13C REMARK 210 -SEPARATED_NOESY; 3D_15N- REMARK 210 SEPARATED_NOESY; HNHA REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 750 MHZ; 600 MHZ; 500 REMARK 210 MHZ REMARK 210 SPECTROMETER MODEL : INOVA; UNITYPLUS REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : FELIX 98, SPARKY 3.106, REMARK 210 AUTOSTRUCTURE 2.1.1 REMARK 210 METHOD USED : THE INITIAL STRUCTURE WAS REMARK 210 DETERMINED USING AUTOMATED REMARK 210 STRUCTURE DETERMINATION REMARK 210 (AUTOSTRUCTURE) AND REFINED REMARK 210 MANUALLY. A FINAL REFINEMENT REMARK 210 USED SIMULTATED ANNEALING IN REMARK 210 EXPLICIT SOLVENT. REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 30 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH LOWEST ENERGY REMARK 210 AND FEWEST RESTRAINT VIOLATIONS 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 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 2 -160.84 56.38 REMARK 500 1 ARG A 12 89.48 61.40 REMARK 500 1 ALA A 18 84.57 52.89 REMARK 500 1 ALA A 27 83.23 60.67 REMARK 500 1 GLU A 51 -21.57 71.29 REMARK 500 1 GLU A 115 -70.60 -72.08 REMARK 500 1 HIS A 130 24.31 46.82 REMARK 500 1 HIS A 133 176.63 70.17 REMARK 500 2 ALA A 2 -162.62 58.79 REMARK 500 2 SER A 5 -42.03 -172.30 REMARK 500 2 GLU A 6 -97.53 -95.20 REMARK 500 2 ILE A 7 84.29 56.12 REMARK 500 2 HIS A 9 -81.75 -173.56 REMARK 500 2 ARG A 12 85.16 169.25 REMARK 500 2 ALA A 14 64.54 -106.44 REMARK 500 2 LYS A 21 124.72 70.01 REMARK 500 2 ALA A 27 15.21 59.89 REMARK 500 2 PRO A 50 91.80 -65.27 REMARK 500 2 GLU A 51 -46.37 -171.89 REMARK 500 2 GLN A 52 42.31 -80.81 REMARK 500 2 ASP A 69 -60.49 -94.53 REMARK 500 2 ASN A 94 -24.24 85.29 REMARK 500 2 ARG A 116 78.72 56.21 REMARK 500 2 ARG A 118 78.69 -69.59 REMARK 500 2 GLU A 129 51.71 -155.86 REMARK 500 3 ALA A 2 -80.29 -65.33 REMARK 500 3 GLN A 3 -77.90 -160.07 REMARK 500 3 SER A 5 -87.26 60.86 REMARK 500 3 ARG A 12 92.76 66.22 REMARK 500 3 GLN A 32 -71.53 -109.83 REMARK 500 3 ASP A 40 -32.14 -154.15 REMARK 500 3 GLU A 51 -27.39 75.26 REMARK 500 3 VAL A 93 -81.43 -83.28 REMARK 500 3 ASN A 94 15.25 -168.10 REMARK 500 3 LEU A 128 108.47 67.40 REMARK 500 3 GLU A 129 -138.40 -73.44 REMARK 500 3 HIS A 132 70.14 59.36 REMARK 500 3 HIS A 134 -78.49 65.74 REMARK 500 4 GLU A 6 -73.85 -76.02 REMARK 500 4 LYS A 21 111.85 68.27 REMARK 500 4 ALA A 27 93.11 -61.95 REMARK 500 4 VAL A 93 -85.01 -89.70 REMARK 500 4 ASN A 94 14.05 -160.00 REMARK 500 4 ARG A 116 90.39 -163.36 REMARK 500 4 ARG A 117 74.92 -64.92 REMARK 500 4 ARG A 118 29.94 -156.75 REMARK 500 4 GLU A 129 21.93 -74.35 REMARK 500 4 HIS A 130 -73.75 -107.67 REMARK 500 4 HIS A 132 -40.17 175.47 REMARK 500 5 GLU A 6 130.99 68.87 REMARK 500 REMARK 500 THIS ENTRY HAS 226 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: RPR43 RELATED DB: TARGETDB REMARK 999 REMARK 999 SEQUENCE REMARK 999 ACCORDING TO AUTHORS,THIS IS A SEQUENCING ERROR OR AN REMARK 999 ISOFORM RESULTING FROM A SLIGHT DIFFERENCE IN THE REMARK 999 SEQUENCED STRAIN AND THE CLONING STRAIN. DBREF 2FVT A 1 127 GB 39649750 CAE28271 1 127 SEQADV 2FVT GLY A 28 GB 39649750 ASP 28 SEE REMARK 999 SEQADV 2FVT LEU A 128 GB 39649750 CLONING ARTIFACT SEQADV 2FVT GLU A 129 GB 39649750 CLONING ARTIFACT SEQADV 2FVT HIS A 130 GB 39649750 EXPRESSION TAG SEQADV 2FVT HIS A 131 GB 39649750 EXPRESSION TAG SEQADV 2FVT HIS A 132 GB 39649750 EXPRESSION TAG SEQADV 2FVT HIS A 133 GB 39649750 EXPRESSION TAG SEQADV 2FVT HIS A 134 GB 39649750 EXPRESSION TAG SEQADV 2FVT HIS A 135 GB 39649750 EXPRESSION TAG SEQRES 1 A 135 MET ALA GLN ARG SER GLU ILE PRO HIS PHE PRO ARG THR SEQRES 2 A 135 ALA ALA ILE ASP ALA TYR GLY LYS GLY GLY PHE TYR PHE SEQRES 3 A 135 ALA GLY MET SER HIS GLN GLY SER LEU LEU PHE LEU PRO SEQRES 4 A 135 ASP ALA VAL TRP GLY TRP ASP VAL THR LYS PRO GLU GLN SEQRES 5 A 135 ILE ASP ARG TYR SER LEU GLN ARG VAL PHE ASP ASN ALA SEQRES 6 A 135 ASN ALA ILE ASP THR LEU ILE VAL GLY THR GLY ALA ASP SEQRES 7 A 135 VAL TRP ILE ALA PRO ARG GLN LEU ARG GLU ALA LEU ARG SEQRES 8 A 135 GLY VAL ASN VAL VAL LEU ASP THR MET GLN THR GLY PRO SEQRES 9 A 135 ALA ILE ARG THR TYR ASN ILE MET ILE GLY GLU ARG ARG SEQRES 10 A 135 ARG VAL ALA ALA ALA LEU ILE ALA VAL PRO LEU GLU HIS SEQRES 11 A 135 HIS HIS HIS HIS HIS HELIX 1 1 LEU A 58 ASN A 64 1 7 HELIX 2 2 PRO A 83 GLY A 92 1 10 HELIX 3 3 GLN A 101 ARG A 116 1 16 SHEET 1 A 3 TYR A 19 GLY A 20 0 SHEET 2 A 3 GLY A 23 TYR A 25 -1 O GLY A 23 N GLY A 20 SHEET 3 A 3 SER A 30 HIS A 31 -1 O HIS A 31 N PHE A 24 SHEET 1 B 5 VAL A 42 TRP A 45 0 SHEET 2 B 5 SER A 34 PHE A 37 -1 N LEU A 36 O TRP A 43 SHEET 3 B 5 VAL A 119 ILE A 124 -1 O ALA A 121 N PHE A 37 SHEET 4 B 5 THR A 70 GLY A 74 1 N ILE A 72 O ALA A 122 SHEET 5 B 5 VAL A 96 MET A 100 1 O VAL A 96 N LEU A 71 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 9 2 Bytes