Header list of 2gov.pdb file
Complete list - r 9 2 Bytes
HEADER HEME BINDING PROTEIN 14-APR-06 2GOV TITLE SOLUTION STRUCTURE OF MURINE P22HBP COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEME-BINDING PROTEIN 1; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: P22HBP; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE; SOURCE 4 ORGANISM_TAXID: 10090; SOURCE 5 GENE: HEBP1, HBP; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PNJ2 KEYWDS P22HBP, HEME BINDING, STRUCTURAL GENOMICS, PROTEIN STRUCTURE KEYWDS 2 INITIATIVE, PSI, CENTER FOR EUKARYOTIC STRUCTURAL GENOMICS, CESG, KEYWDS 3 HEME BINDING PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR B.F.VOLKMAN,J.S.DIAS,B.J.GOODFELLOW,F.C.PETERSON,CENTER FOR AUTHOR 2 EUKARYOTIC STRUCTURAL GENOMICS (CESG) REVDAT 5 09-MAR-22 2GOV 1 REMARK SEQADV REVDAT 4 24-FEB-09 2GOV 1 VERSN REVDAT 3 31-OCT-06 2GOV 1 JRNL REVDAT 2 05-SEP-06 2GOV 1 JRNL REVDAT 1 09-MAY-06 2GOV 0 JRNL AUTH J.S.DIAS,A.L.MACEDO,G.C.FERREIRA,F.C.PETERSON,B.F.VOLKMAN, JRNL AUTH 2 B.J.GOODFELLOW JRNL TITL THE FIRST STRUCTURE FROM THE SOUL/HBP FAMILY OF HEME-BINDING JRNL TITL 2 PROTEINS, MURINE P22HBP. JRNL REF J.BIOL.CHEM. V. 281 31553 2006 JRNL REFN ISSN 0021-9258 JRNL PMID 16905545 JRNL DOI 10.1074/JBC.M605988200 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH J.S.DIAS,A.L.MACEDO,G.C.FERREIRA,N.JEANTY,S.TAKETANI, REMARK 1 AUTH 2 B.J.GOODFELLOW,F.C.PETERSON,B.F.VOLKMAN REMARK 1 TITL 1H, 15N AND 13C RESONANCE ASSIGNMENTS OF THE HEME-BINDING REMARK 1 TITL 2 PROTEIN MURINE P22HBP. REMARK 1 REF J.BIOMOL.NMR V. 32 338 2005 REMARK 1 REFN ISSN 0925-2738 REMARK 1 PMID 16211492 REMARK 1 DOI 10.1007/S10858-005-0470-8 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 3.5, XPLOR-NIH 2.9.3 REMARK 3 AUTHORS : BRUKER (XWINNMR), SCHWIETERS, C.D., KUSZEWSKI, REMARK 3 J.J., TJANDRA, N., CLORE, G.M. (XPLOR-NIH) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: STRUCTURES ARE BASED ON A TOTAL OF 1851 REMARK 3 NOE CONSTRAINTS ( 372 INTRA, 425 SEQUENTIAL, 276 MEDIUM AND 778 REMARK 3 LONG RANGE CONSTRAINTS) AND 276 PHI AND PSI DIHEDRAL ANGLE REMARK 3 CONSTRAINTS. REMARK 4 REMARK 4 2GOV COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-APR-06. REMARK 100 THE DEPOSITION ID IS D_1000037377. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 303 REMARK 210 PH : 8.0 REMARK 210 IONIC STRENGTH : 28 MM REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1.0 MM P22HBP U-15N/13C, 50 MM REMARK 210 SODIUM PHOSPHATE REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C REMARK 210 -SEPARATED_NOESY; 3D_13C- REMARK 210 SEPARATED_NOESY (AROMATIC) REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : DRX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE 2004, XEASY 1.3, SPSCAN REMARK 210 1.1.0, GARANT 2.1, CYANA 2.1 REMARK 210 METHOD USED : AUTOMATED METHODS WERE USED FOR REMARK 210 BACKBONE CHEMICAL SHIFT REMARK 210 ASSIGNMENT AND ITERATIVE NOE REMARK 210 REFINEMENT. FINAL STRUCTURES REMARK 210 WERE OBTAINED BY MOLECULAR REMARK 210 DYNAMICS IN EXPLICIT SOLVENT 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: ALL TRIPLE-RESONANCE AND NOESY SPECTRA WERE ACQUIRED USING REMARK 210 A CRYOGENIC PROBE. 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 MET A -4 REMARK 465 LYS A -3 REMARK 465 GLN A -2 REMARK 465 SER A -1 REMARK 465 THR A 0 REMARK 465 HIS A 1 REMARK 465 HIS A 2 REMARK 465 HIS A 3 REMARK 465 HIS A 4 REMARK 465 HIS A 5 REMARK 465 HIS A 6 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 THR A 15 -52.85 -142.37 REMARK 500 1 ASP A 28 -62.07 73.86 REMARK 500 1 ASP A 48 -40.02 72.22 REMARK 500 1 LYS A 177 -72.42 -153.87 REMARK 500 2 THR A 15 68.79 73.75 REMARK 500 2 ASP A 28 -49.38 75.48 REMARK 500 2 ASP A 48 -36.97 73.72 REMARK 500 2 LYS A 96 -70.10 -176.63 REMARK 500 2 SER A 111 92.22 -161.00 REMARK 500 2 TYR A 179 -81.80 -70.30 REMARK 500 3 SER A 22 158.74 179.08 REMARK 500 3 ASP A 28 -45.77 153.25 REMARK 500 3 ASP A 48 -25.31 72.80 REMARK 500 3 LYS A 96 -68.79 -168.77 REMARK 500 3 SER A 111 90.77 -160.74 REMARK 500 4 ASP A 28 -45.40 78.15 REMARK 500 4 LYS A 96 -65.74 105.09 REMARK 500 5 LEU A 9 -72.07 -153.72 REMARK 500 5 PHE A 10 173.84 61.29 REMARK 500 5 THR A 15 -69.45 -102.70 REMARK 500 5 ASP A 28 -64.77 72.58 REMARK 500 5 ASP A 48 -9.38 79.60 REMARK 500 5 LYS A 96 21.87 -70.35 REMARK 500 6 THR A 15 106.86 72.14 REMARK 500 6 ASP A 28 -58.28 72.74 REMARK 500 6 ASP A 48 -26.47 76.16 REMARK 500 6 PRO A 50 158.79 -49.48 REMARK 500 6 MET A 76 -38.51 178.00 REMARK 500 6 PRO A 159 36.56 -64.66 REMARK 500 6 LYS A 177 -67.48 162.40 REMARK 500 7 ASP A 28 -52.81 74.35 REMARK 500 7 ASP A 48 -12.89 68.73 REMARK 500 7 SER A 111 89.02 -160.18 REMARK 500 7 ASP A 165 27.66 49.38 REMARK 500 7 TYR A 172 -38.59 -142.46 REMARK 500 8 SER A 8 112.16 73.29 REMARK 500 8 VAL A 13 78.70 -109.08 REMARK 500 8 ASP A 28 -52.78 76.26 REMARK 500 8 ASP A 48 -16.37 67.60 REMARK 500 8 THR A 69 34.32 -92.06 REMARK 500 8 MET A 76 -75.66 -76.61 REMARK 500 8 LYS A 96 -62.41 178.19 REMARK 500 8 PRO A 105 151.25 -46.83 REMARK 500 8 SER A 111 97.30 -160.34 REMARK 500 8 TYR A 179 -81.45 -68.37 REMARK 500 9 ASP A 28 -41.92 82.00 REMARK 500 9 ASP A 48 -36.17 71.88 REMARK 500 9 THR A 69 33.76 -86.25 REMARK 500 9 LYS A 96 -66.33 -178.87 REMARK 500 9 SER A 111 87.77 -158.67 REMARK 500 REMARK 500 THIS ENTRY HAS 131 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 14 ARG A 34 0.08 SIDE CHAIN REMARK 500 17 ARG A 34 0.09 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: GO.79130 RELATED DB: TARGETDB DBREF 2GOV A 7 190 UNP Q9R257 HEBP1_MOUSE 7 190 SEQADV 2GOV MET A -4 UNP Q9R257 CLONING ARTIFACT SEQADV 2GOV LYS A -3 UNP Q9R257 CLONING ARTIFACT SEQADV 2GOV GLN A -2 UNP Q9R257 CLONING ARTIFACT SEQADV 2GOV SER A -1 UNP Q9R257 CLONING ARTIFACT SEQADV 2GOV THR A 0 UNP Q9R257 CLONING ARTIFACT SEQADV 2GOV HIS A 1 UNP Q9R257 CLONING ARTIFACT SEQADV 2GOV HIS A 2 UNP Q9R257 CLONING ARTIFACT SEQADV 2GOV HIS A 3 UNP Q9R257 CLONING ARTIFACT SEQADV 2GOV HIS A 4 UNP Q9R257 CLONING ARTIFACT SEQADV 2GOV HIS A 5 UNP Q9R257 CLONING ARTIFACT SEQADV 2GOV HIS A 6 UNP Q9R257 CLONING ARTIFACT SEQRES 1 A 195 MET LYS GLN SER THR HIS HIS HIS HIS HIS HIS ASN SER SEQRES 2 A 195 LEU PHE GLY SER VAL GLU THR TRP PRO TRP GLN VAL LEU SEQRES 3 A 195 SER THR GLY GLY LYS GLU ASP VAL SER TYR GLU GLU ARG SEQRES 4 A 195 ALA CYS GLU GLY GLY LYS PHE ALA THR VAL GLU VAL THR SEQRES 5 A 195 ASP LYS PRO VAL ASP GLU ALA LEU ARG GLU ALA MET PRO SEQRES 6 A 195 LYS ILE MET LYS TYR VAL GLY GLY THR ASN ASP LYS GLY SEQRES 7 A 195 VAL GLY MET GLY MET THR VAL PRO VAL SER PHE ALA VAL SEQRES 8 A 195 PHE PRO ASN GLU ASP GLY SER LEU GLN LYS LYS LEU LYS SEQRES 9 A 195 VAL TRP PHE ARG ILE PRO ASN GLN PHE GLN GLY SER PRO SEQRES 10 A 195 PRO ALA PRO SER ASP GLU SER VAL LYS ILE GLU GLU ARG SEQRES 11 A 195 GLU GLY ILE THR VAL TYR SER THR GLN PHE GLY GLY TYR SEQRES 12 A 195 ALA LYS GLU ALA ASP TYR VAL ALA HIS ALA THR GLN LEU SEQRES 13 A 195 ARG THR THR LEU GLU GLY THR PRO ALA THR TYR GLN GLY SEQRES 14 A 195 ASP VAL TYR TYR CYS ALA GLY TYR ASP PRO PRO MET LYS SEQRES 15 A 195 PRO TYR GLY ARG ARG ASN GLU VAL TRP LEU VAL LYS ALA HELIX 1 1 PRO A 50 GLY A 68 1 19 HELIX 2 2 PRO A 105 SER A 111 1 7 HELIX 3 3 LYS A 140 LEU A 155 1 16 SHEET 1 A 9 GLN A 19 THR A 23 0 SHEET 2 A 9 TYR A 31 ALA A 35 -1 O GLU A 33 N LEU A 21 SHEET 3 A 9 THR A 129 GLY A 136 -1 O VAL A 130 N ARG A 34 SHEET 4 A 9 ARG A 182 LYS A 189 -1 O LEU A 187 N TYR A 131 SHEET 5 A 9 TYR A 162 GLY A 171 -1 N ALA A 170 O GLU A 184 SHEET 6 A 9 VAL A 82 PRO A 88 -1 N VAL A 82 O GLY A 171 SHEET 7 A 9 LEU A 94 PHE A 102 -1 O GLN A 95 N PHE A 87 SHEET 8 A 9 LYS A 40 THR A 47 -1 N VAL A 44 O VAL A 100 SHEET 9 A 9 LYS A 121 GLU A 124 -1 O GLU A 123 N PHE A 41 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