Header list of 1sou.pdb file
Complete list - r 2 2 Bytes
HEADER LIGASE 15-MAR-04 1SOU
TITLE NMR STRUCTURE OF AQUIFEX AEOLICUS 5,10-METHENYLTETRAHYDROFOLATE
TITLE 2 SYNTHETASE: NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET QR46
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 5,10-METHENYLTETRAHYDROFOLATE SYNTHETASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 6.3.3.2;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: AQUIFEX AEOLICUS;
SOURCE 3 ORGANISM_TAXID: 63363;
SOURCE 4 GENE: AQ_1731;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PMGK;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET21D
KEYWDS STRUCTURAL GENOMICS, PSI, PROTEIN STRUCTURE INITIATIVE, NORTHEAST
KEYWDS 2 STRUCTURAL GENOMICS CONSORTIUM, NESG, LIGASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR J.R.CORT,Y.CHIANG,T.ACTON,M.WU,G.T.MONTELIONE,M.A.KENNEDY,NORTHEAST
AUTHOR 2 STRUCTURAL GENOMICS CONSORTIUM (NESG)
REVDAT 4 02-MAR-22 1SOU 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1SOU 1 VERSN
REVDAT 2 25-JAN-05 1SOU 1 AUTHOR KEYWDS REMARK
REVDAT 1 22-JUN-04 1SOU 0
JRNL AUTH J.R.CORT,Y.CHIANG,T.ACTON,M.WU,G.T.MONTELIONE,M.A.KENNEDY
JRNL TITL NMR STRUCTURE OF AQUIFEX AEOLICUS
JRNL TITL 2 5,10-METHENYLTETRAHYDROFOLATE SYNTHETASE: NORTHEAST
JRNL TITL 3 STRUCTURAL GENOMICS CONSORTIUM TARGET QR46
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NIH-XPLOR 2.0.4, CNS 1.1
REMARK 3 AUTHORS : AT BRUNGER, GM CLORE, J KUSZEWSKI, CD SCHWIETERS,
REMARK 3 N TJANDRA (NIH-XPLOR), AT BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 FINAL REFINEMENT IN EXPLICIT SOLVENT WITH LEONARD-JONES
REMARK 3 AND ELECTROSTATIC POTENTIALS. BACKBONE AND SIDECHAIN
REMARK 3 ASSIGNMENTS WERE DETERMINED MANUALLY FROM TRIPLE-RESONANCE
REMARK 3 NMR DATA. NOE DISTANCE RESTRAINTS WERE DERIVED MANUALLY
REMARK 3 FROM NOESY DATA. THE STRUCTURE IS BASED ON 1235 RESTRAINTS:
REMARK 3 938 NOE DISTANCE RESTRAINTS, 112 H-BOND RESTRAINTS (56 H-BONDS),
REMARK 3 AND 185 DIHEDRAL RESTRAINTS. PHI DIHEDRAL RESTRAINTS WERE DERIVED
REMARK 3 FROM THE HNHA EXPERIMENT AND TALOS. PSI DIHEDRAL RESTRAINTS WERE
REMARK 3 DERIVED FROM NOE RATIOS, SECONDARY STRUCTURE PROPENSITIES EVIDENT
REMARK 3 IN PRELIMINARY STRUCTURES, ALPHA CARBON CHEMICAL SHIFTS, AND TALOS.
REMARK 3 RESIDUES 1-2 AND 182-194 ARE UNSTRUCTURED TERMINI IN THIS ENSEMBLE.
REMARK 4
REMARK 4 1SOU COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-MAR-04.
REMARK 100 THE DEPOSITION ID IS D_1000021883.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 0.115
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1 MM 5,10
REMARK 210 -METHENYLTETRAHYDROFOLATE
REMARK 210 SYNTHETASE U-15N,13C; 20 MM MES,
REMARK 210 100 MM NACL, 5 MM CACL2, 10 MM
REMARK 210 DTT, 0.02% NAN3 PH 6.5 95% H2O,
REMARK 210 5% D2O; 0.5 MM 5,10-
REMARK 210 METHENYLTETRAHYDROFOLATE SYNTHETA
REMARK 210 SE U-15N,5%-13C; 20 MM MES, 100
REMARK 210 MM NACL, 5 MM CACL2, 10 MM DTT,
REMARK 210 0.02% NAN3 PH 6.5 95% H2O, 5%
REMARK 210 D2O; 1 MM 5,10-
REMARK 210 METHENYLTETRAHYDROFOLATE SYNTHETA
REMARK 210 SE U-15N,13C; 20 MM MES, 100 MM
REMARK 210 NACL, 5 MM CACL2, 10 MM DTT,
REMARK 210 0.02% NAN3 PH 6.5 100% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 4D_13C-
REMARK 210 SEPARATED_NOESY; HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 750 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY; INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : VNMR 6.1C, FELIX 97, TALOS
REMARK 210 METHOD USED : MOLECULAR DYNAMICS, SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 29
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY,STRUCTURES
REMARK 210 WITH FAVORABLE NON-BOND ENERGY,
REMARK 210 STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS,STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY
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 OE2 GLU A 110 HZ3 LYS A 144 1.58
REMARK 500 OE1 GLU A 38 HH22 ARG A 182 1.58
REMARK 500 HH21 ARG A 128 OD1 ASP A 166 1.60
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 TYR A 48 -90.02 -77.84
REMARK 500 1 CYS A 49 127.23 176.05
REMARK 500 1 LYS A 52 -69.24 -96.70
REMARK 500 1 GLU A 54 -156.18 -97.87
REMARK 500 1 GLU A 67 -60.55 -101.81
REMARK 500 1 ASN A 78 -56.96 70.83
REMARK 500 1 PRO A 88 44.37 -76.60
REMARK 500 1 ALA A 89 -74.31 -86.13
REMARK 500 1 ALA A 95 -152.48 -87.67
REMARK 500 1 ASP A 123 -169.62 -127.23
REMARK 500 1 PHE A 131 -72.10 -119.83
REMARK 500 1 PHE A 157 -169.52 -120.93
REMARK 500 1 ASP A 163 -78.71 -62.71
REMARK 500 1 ALA A 164 -96.26 -128.60
REMARK 500 1 HIS A 189 -76.36 -108.10
REMARK 500 1 HIS A 193 159.58 72.02
REMARK 500 2 SER A 42 105.81 -55.53
REMARK 500 2 CYS A 49 97.04 65.17
REMARK 500 2 LYS A 52 -55.25 70.91
REMARK 500 2 VAL A 55 101.67 68.26
REMARK 500 2 PRO A 88 31.87 -74.42
REMARK 500 2 ALA A 89 -28.76 -143.33
REMARK 500 2 CYS A 90 38.46 -84.75
REMARK 500 2 PHE A 96 -52.13 72.49
REMARK 500 2 LYS A 133 1.21 -155.37
REMARK 500 2 TYR A 135 123.55 77.41
REMARK 500 2 LYS A 144 68.21 -103.89
REMARK 500 2 LYS A 176 -62.01 -120.31
REMARK 500 2 ARG A 185 28.48 -169.19
REMARK 500 2 LEU A 187 12.05 -144.39
REMARK 500 2 HIS A 190 67.20 -156.32
REMARK 500 3 LEU A 2 -47.08 -160.43
REMARK 500 3 CYS A 49 102.08 67.11
REMARK 500 3 GLU A 54 -85.01 64.08
REMARK 500 3 PHE A 96 -53.47 72.12
REMARK 500 3 VAL A 102 -81.59 -54.04
REMARK 500 3 ARG A 128 -71.98 -103.99
REMARK 500 3 LEU A 129 -11.42 71.45
REMARK 500 3 GLU A 158 -76.72 -64.13
REMARK 500 3 ALA A 164 -85.98 -152.69
REMARK 500 3 TRP A 165 66.87 -103.72
REMARK 500 3 LEU A 181 37.78 -82.09
REMARK 500 3 HIS A 192 29.06 -171.12
REMARK 500 4 TYR A 48 -98.68 -80.47
REMARK 500 4 CYS A 49 116.46 177.89
REMARK 500 4 LYS A 52 -51.15 71.85
REMARK 500 4 GLU A 54 150.75 77.34
REMARK 500 4 VAL A 55 126.98 -36.85
REMARK 500 4 ASP A 56 76.96 -68.08
REMARK 500 4 ASN A 78 -50.80 70.44
REMARK 500
REMARK 500 THIS ENTRY HAS 270 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: QR46 RELATED DB: TARGETDB
DBREF 1SOU A 1 186 UNP O67621 O67621_AQUAE 1 186
SEQADV 1SOU LEU A 187 UNP O67621 CLONING ARTIFACT
SEQADV 1SOU GLU A 188 UNP O67621 CLONING ARTIFACT
SEQADV 1SOU HIS A 189 UNP O67621 EXPRESSION TAG
SEQADV 1SOU HIS A 190 UNP O67621 EXPRESSION TAG
SEQADV 1SOU HIS A 191 UNP O67621 EXPRESSION TAG
SEQADV 1SOU HIS A 192 UNP O67621 EXPRESSION TAG
SEQADV 1SOU HIS A 193 UNP O67621 EXPRESSION TAG
SEQADV 1SOU HIS A 194 UNP O67621 EXPRESSION TAG
SEQRES 1 A 194 MET LEU LYS SER GLU LEU ARG LYS LYS VAL LEU HIS LYS
SEQRES 2 A 194 ARG ILE ASN LEU SER GLU GLU GLU ARG ARG ARG LEU SER
SEQRES 3 A 194 GLU LYS VAL ILE SER ASN LEU LYS SER LEU PRO GLU PHE
SEQRES 4 A 194 LYS LYS SER LYS LYS VAL ALA LEU TYR CYS PRO ILE LYS
SEQRES 5 A 194 GLY GLU VAL ASP LEU THR PRO LEU PHE PRO GLU VAL LEU
SEQRES 6 A 194 LYS GLU LYS GLU LEU ILE LEU PRO LYS VAL GLU GLY ASN
SEQRES 7 A 194 GLU ILE SER LEU TYR ARG VAL HIS SER PRO ALA CYS LEU
SEQRES 8 A 194 GLY VAL GLY ALA PHE GLY ILE MET GLU PRO VAL GLU GLY
SEQRES 9 A 194 GLU ARG VAL ASN PRO GLU ASP VAL ASP PHE ILE ALA VAL
SEQRES 10 A 194 PRO GLY VAL ALA PHE ASP LEU GLU GLY TYR ARG LEU GLY
SEQRES 11 A 194 PHE GLY LYS GLY TYR TYR ASP ARG LEU LEU LYS ARG VAL
SEQRES 12 A 194 LYS GLY LEU LYS VAL GLY VAL ALA TYR SER PHE GLN VAL
SEQRES 13 A 194 PHE GLU ARG LEU PRO ARG ASP ALA TRP ASP ILE PRO VAL
SEQRES 14 A 194 ASP VAL LEU VAL THR GLU LYS ASN VAL ARG ARG LEU ARG
SEQRES 15 A 194 ASP GLY ARG SER LEU GLU HIS HIS HIS HIS HIS HIS
HELIX 1 1 LEU A 2 ILE A 15 1 14
HELIX 2 2 SER A 18 LEU A 36 1 19
HELIX 3 3 LEU A 36 SER A 42 1 7
HELIX 4 4 LEU A 57 PRO A 59 5 3
HELIX 5 5 LEU A 60 LYS A 68 1 9
HELIX 6 6 ASN A 108 VAL A 112 5 5
HELIX 7 7 TYR A 135 VAL A 143 1 9
HELIX 8 8 TYR A 152 VAL A 156 5 5
SHEET 1 A 8 GLU A 105 VAL A 107 0
SHEET 2 A 8 ILE A 80 VAL A 85 -1 N LEU A 82 O VAL A 107
SHEET 3 A 8 GLU A 69 VAL A 75 -1 N LYS A 74 O SER A 81
SHEET 4 A 8 LYS A 44 LEU A 47 1 N VAL A 45 O ILE A 71
SHEET 5 A 8 PHE A 114 VAL A 117 1 O PHE A 114 N ALA A 46
SHEET 6 A 8 LEU A 146 VAL A 150 1 O VAL A 148 N ILE A 115
SHEET 7 A 8 VAL A 171 VAL A 173 1 O VAL A 171 N GLY A 149
SHEET 8 A 8 VAL A 178 ARG A 180 -1 O ARG A 179 N LEU A 172
SHEET 1 B 2 GLY A 92 VAL A 93 0
SHEET 2 B 2 MET A 99 GLU A 100 -1 O GLU A 100 N GLY A 92
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 2 2 Bytes