Header list of 2f65.pdb file
Complete list - r 9 2 Bytes
HEADER TRANSFERASE 28-NOV-05 2F65
TITLE SOLUTION STRUCTURE OF HPPK IN COMPLEX WITH INHIBITOR ANALOG AMPCPP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 2-AMINO-4-HYDROXY-6-HYDROXYMETHYLDIHYDROPTERIDINE
COMPND 3 PYROPHOSPHOKINASE;
COMPND 4 CHAIN: A;
COMPND 5 SYNONYM: 7,8-DIHYDRO-6-HYDROXYMETHYLPTERIN-PYROPHOSPHOKINASE, HPPK,
COMPND 6 6-HYDROXYMETHYL-7,8-DIHYDROPTERIN PYROPHOSPHOKINASE, PPPK;
COMPND 7 EC: 2.7.6.3;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: FOLK;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET17B
KEYWDS ALPHA-BETA-ALPHA FOLD, TRANSFERASE
EXPDTA SOLUTION NMR
NUMMDL 21
MDLTYP MINIMIZED AVERAGE
AUTHOR H.YAN,G.LI
REVDAT 3 09-MAR-22 2F65 1 REMARK
REVDAT 2 24-FEB-09 2F65 1 VERSN
REVDAT 1 17-JAN-06 2F65 0
JRNL AUTH H.YAN,G.LI
JRNL TITL SOLUTION STRUCTURE OF HPPK IN COMPLEX WITH INHIBITOR ANALOG
JRNL TITL 2 AMPCPP
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1B, ARIA 1.2
REMARK 3 AUTHORS : VARIAN (VNMR), LINGE (ARIA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: A TOTAL OF 4273 STRUCTURALLY USEFUL
REMARK 3 DISTANCE RESTRAINTS WERE USED FOR THE CALCULATION, OF WHICH 3069
REMARK 3 WERE UNAMBIGUOUS RESTRAINTS, 1204 AMBIGUOUS. TOTAL 47 H-BONDS
REMARK 3 INCLUDED.
REMARK 4
REMARK 4 2F65 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-NOV-05.
REMARK 100 THE DEPOSITION ID IS D_1000035498.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.4
REMARK 210 IONIC STRENGTH : 20 MM SODIUM PHOSPHATE,15MM
REMARK 210 MGCL2
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.6 MM HPPK,U-15N,13C;20 MM
REMARK 210 SODIUM PHOSPHATE,15MM MGCL2;
REMARK 210 10MM AMPCPP; 0.05 MM DSS;5% D2O,
REMARK 210 95%H2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE, NMRVIEW 5.0.4, CNS 1.0
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 21
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 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.
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 HA VAL A 83 H GLU A 87 1.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 16 TYR A 40 CE1 TYR A 40 CZ 0.139
REMARK 500 16 TYR A 40 CZ TYR A 40 CE2 -0.144
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 SER A 9 151.21 75.11
REMARK 500 1 ASN A 10 -146.88 -159.75
REMARK 500 1 LEU A 11 143.52 72.53
REMARK 500 1 ALA A 12 -75.69 -3.41
REMARK 500 1 LYS A 23 -70.90 -65.28
REMARK 500 1 PRO A 29 -43.00 -25.33
REMARK 500 1 LEU A 34 -58.29 -124.18
REMARK 500 1 SER A 37 -163.54 -172.66
REMARK 500 1 SER A 38 67.39 66.67
REMARK 500 1 LEU A 45 71.60 52.12
REMARK 500 1 GLN A 48 -159.59 -144.77
REMARK 500 1 ASP A 52 -95.44 179.23
REMARK 500 1 TYR A 53 169.53 60.11
REMARK 500 1 LEU A 54 85.06 -163.88
REMARK 500 1 ALA A 65 153.42 -48.22
REMARK 500 1 PRO A 66 -19.85 -46.61
REMARK 500 1 GLN A 79 31.80 -153.11
REMARK 500 1 GLN A 80 -78.05 -139.68
REMARK 500 1 ARG A 82 -88.88 62.17
REMARK 500 1 VAL A 83 26.47 36.05
REMARK 500 1 LYS A 85 66.76 -174.12
REMARK 500 1 GLU A 87 6.87 46.86
REMARK 500 1 ARG A 88 -77.50 63.19
REMARK 500 1 TRP A 89 -164.99 -109.94
REMARK 500 1 PRO A 91 -176.00 -48.23
REMARK 500 1 ARG A 92 -158.85 67.45
REMARK 500 1 THR A 93 174.40 56.86
REMARK 500 1 ASP A 95 85.69 -154.06
REMARK 500 1 PHE A 101 71.22 -150.20
REMARK 500 1 ASN A 103 -4.21 72.92
REMARK 500 1 THR A 108 -94.67 -150.03
REMARK 500 1 GLU A 109 -49.58 -146.71
REMARK 500 1 THR A 112 98.80 -160.14
REMARK 500 1 HIS A 115 124.31 55.37
REMARK 500 1 ASN A 120 47.21 -97.10
REMARK 500 1 ARG A 121 63.49 -156.52
REMARK 500 1 PHE A 123 34.18 -98.45
REMARK 500 1 MET A 124 -34.31 -153.03
REMARK 500 1 ALA A 132 88.44 -174.43
REMARK 500 1 PRO A 133 45.69 -92.94
REMARK 500 1 VAL A 136 -77.81 37.45
REMARK 500 1 PHE A 137 -58.65 -14.43
REMARK 500 1 PRO A 138 -51.76 -24.52
REMARK 500 1 MET A 142 -149.12 -60.30
REMARK 500 1 ALA A 151 -101.03 -86.90
REMARK 500 1 PHE A 152 -134.60 -107.43
REMARK 500 1 ASP A 153 -30.26 -151.02
REMARK 500 1 LYS A 154 107.09 174.67
REMARK 500 2 ASN A 10 100.50 -161.48
REMARK 500 2 LEU A 11 -169.90 -160.02
REMARK 500
REMARK 500 THIS ENTRY HAS 799 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 6 TYR A 40 0.05 SIDE CHAIN
REMARK 500 11 TYR A 40 0.07 SIDE CHAIN
REMARK 500 12 TYR A 40 0.06 SIDE CHAIN
REMARK 500 20 TYR A 4 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1EQ0 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH AMPPCP
REMARK 900 RELATED ID: 2F63 RELATED DB: PDB
DBREF 2F65 A 1 158 UNP P26281 HPPK_ECOLI 1 158
SEQRES 1 A 158 THR VAL ALA TYR ILE ALA ILE GLY SER ASN LEU ALA SER
SEQRES 2 A 158 PRO LEU GLU GLN VAL ASN ALA ALA LEU LYS ALA LEU GLY
SEQRES 3 A 158 ASP ILE PRO GLU SER HIS ILE LEU THR VAL SER SER PHE
SEQRES 4 A 158 TYR ARG THR PRO PRO LEU GLY PRO GLN ASP GLN PRO ASP
SEQRES 5 A 158 TYR LEU ASN ALA ALA VAL ALA LEU GLU THR SER LEU ALA
SEQRES 6 A 158 PRO GLU GLU LEU LEU ASN HIS THR GLN ARG ILE GLU LEU
SEQRES 7 A 158 GLN GLN GLY ARG VAL ARG LYS ALA GLU ARG TRP GLY PRO
SEQRES 8 A 158 ARG THR LEU ASP LEU ASP ILE MET LEU PHE GLY ASN GLU
SEQRES 9 A 158 VAL ILE ASN THR GLU ARG LEU THR VAL PRO HIS TYR ASP
SEQRES 10 A 158 MET LYS ASN ARG GLY PHE MET LEU TRP PRO LEU PHE GLU
SEQRES 11 A 158 ILE ALA PRO GLU LEU VAL PHE PRO ASP GLY GLU MET LEU
SEQRES 12 A 158 ARG GLN ILE LEU HIS THR ARG ALA PHE ASP LYS LEU ASN
SEQRES 13 A 158 LYS TRP
HELIX 1 1 SER A 13 ASP A 27 1 15
HELIX 2 2 ALA A 65 LEU A 78 1 14
HELIX 3 3 ARG A 121 ALA A 132 1 12
HELIX 4 4 LEU A 143 ARG A 150 1 8
SHEET 1 A 2 ALA A 3 ALA A 6 0
SHEET 2 A 2 ASP A 97 PHE A 101 -1 O MET A 99 N TYR A 4
SHEET 1 B 2 ILE A 33 THR A 42 0
SHEET 2 B 2 ASP A 52 LEU A 60 -1 O ALA A 59 N THR A 35
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