Header list of 1pjz.pdb file
Complete list - b 23 2 Bytes
HEADER TRANSFERASE 04-JUN-03 1PJZ
TITLE SOLUTION STRUCTURE OF THIOPURINE METHYLTRANSFERASE FROM PSEUDOMONAS
TITLE 2 SYRINGAE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THIOPURINE S-METHYLTRANSFERASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: THIOPURINE METHYLTRANSFERASE, TELLURITE-RESISTANCE
COMPND 5 DETERMINANT, TEL-R DETERMINANT;
COMPND 6 EC: 2.1.1.67;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS SYRINGAE PV. PISI;
SOURCE 3 ORGANISM_TAXID: 59510;
SOURCE 4 STRAIN: PV. PISI;
SOURCE 5 GENE: TPM;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: (DE3)BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX-2T
KEYWDS METHYLTRANSFERASE, POLYMORPHISM, S-ADENOSYLMETHIONINE, DRUG
KEYWDS 2 METABOLISM, TRANSFERASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR T.H.SCHEUERMANN,E.LOLIS,M.E.HODSDON
REVDAT 3 23-FEB-22 1PJZ 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1PJZ 1 VERSN
REVDAT 1 14-OCT-03 1PJZ 0
JRNL AUTH T.H.SCHEUERMANN,E.LOLIS,M.E.HODSDON
JRNL TITL TERTIARY STRUCTURE OF THIOPURINE METHYLTRANSFERASE FROM
JRNL TITL 2 PSEUDOMONAS SYRINGAE, A BACTERIAL ORTHOLOGUE OF A
JRNL TITL 3 POLYMORPHIC, DRUG-METABOLIZING ENZYME
JRNL REF J.MOL.BIOL. V. 333 573 2003
JRNL REFN ISSN 0022-2836
JRNL PMID 14556746
JRNL DOI 10.1016/J.JMB.2003.08.039
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1, CYANA 1.05
REMARK 3 AUTHORS : VARINA, INC. (VNMR), GUENTERT (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: 5000 MD STEPS AT HIGH TEMP, 35000 STEPS
REMARK 3 (COOLING), 10000 CONJUGATE GRADIENT MINIMZATION STEPS
REMARK 4
REMARK 4 1PJZ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-JUN-03.
REMARK 100 THE DEPOSITION ID IS D_1000019378.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 6.8
REMARK 210 IONIC STRENGTH : 150 MM NACL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 20 MM POTASSIUM PHOSPHATE, 150
REMARK 210 MM NACL, 0.05% NAN3, 1 UM
REMARK 210 LUPEPTIN, 1 UM PEPSTATIN, 1 UM
REMARK 210 PMSF, 1.5 MM PROTEIN, UNIFORM
REMARK 210 (RANDOM) LABELING WITH 13C, 15N
REMARK 210 AT KNOWN LABELING
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 4D_13C/15N-SEPARATED_NOESY;
REMARK 210 3D_15N-SEPARATED_NOESY; 3D_13C-
REMARK 210 SEPARATED_NOESY; HNHA
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 : NMRDRAW 2.1, NMRPIPE, SPARKY
REMARK 210 3.98, NMRVIEW 5.0.4, CYANA 1.05,
REMARK 210 TALOS
REMARK 210 METHOD USED : SIMULATED ANNEALING, MOLECULAR
REMARK 210 DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
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: 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 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 GLY A -1
REMARK 465 SER A 0
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 O TYR A 12 H LEU A 16 1.39
REMARK 500 O GLU A 49 H SER A 51 1.52
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 6 95.28 34.32
REMARK 500 1 GLN A 11 -74.07 -73.30
REMARK 500 1 ASN A 17 47.82 70.99
REMARK 500 1 VAL A 18 167.81 -48.30
REMARK 500 1 LEU A 28 38.76 30.83
REMARK 500 1 LYS A 31 -79.02 -118.25
REMARK 500 1 SER A 32 -54.60 164.53
REMARK 500 1 LEU A 50 64.60 -63.04
REMARK 500 1 GLU A 64 151.86 75.64
REMARK 500 1 GLN A 65 -49.10 161.89
REMARK 500 1 GLU A 83 49.98 -100.55
REMARK 500 1 PHE A 90 51.41 176.20
REMARK 500 1 ALA A 91 44.17 179.16
REMARK 500 1 THR A 93 82.75 44.62
REMARK 500 1 HIS A 99 -82.32 58.53
REMARK 500 1 ALA A 101 -104.33 148.42
REMARK 500 1 ALA A 107 104.32 -41.62
REMARK 500 1 ALA A 108 -48.29 -130.68
REMARK 500 1 PRO A 113 -168.03 -75.00
REMARK 500 1 PRO A 129 -159.37 -75.05
REMARK 500 1 GLU A 140 -78.81 -127.64
REMARK 500 1 TYR A 141 -85.06 -27.92
REMARK 500 1 ASP A 142 137.75 -27.02
REMARK 500 1 GLN A 143 -31.00 174.56
REMARK 500 1 LEU A 145 -31.48 -179.89
REMARK 500 1 SER A 152 47.44 32.62
REMARK 500 1 VAL A 153 121.49 -35.20
REMARK 500 1 MET A 162 6.26 -57.65
REMARK 500 1 ASN A 165 -21.91 151.31
REMARK 500 1 THR A 176 74.36 -115.40
REMARK 500 1 ARG A 190 100.47 148.47
REMARK 500 2 SER A 3 -79.91 64.61
REMARK 500 2 ASN A 6 92.36 34.07
REMARK 500 2 GLN A 11 -81.66 -73.27
REMARK 500 2 ASN A 17 36.74 70.60
REMARK 500 2 VAL A 19 144.46 -34.87
REMARK 500 2 LEU A 28 52.99 22.48
REMARK 500 2 LYS A 31 110.69 87.97
REMARK 500 2 GLU A 64 151.40 69.91
REMARK 500 2 GLN A 65 -49.57 159.90
REMARK 500 2 GLU A 83 53.97 -103.94
REMARK 500 2 PHE A 90 52.11 165.09
REMARK 500 2 ALA A 91 -41.35 -145.33
REMARK 500 2 HIS A 99 -82.08 57.90
REMARK 500 2 ALA A 101 -108.76 146.58
REMARK 500 2 ALA A 107 99.94 -52.86
REMARK 500 2 ALA A 108 -52.70 -132.89
REMARK 500 2 PRO A 129 -167.18 -74.97
REMARK 500 2 GLU A 140 -94.21 -123.38
REMARK 500 2 TYR A 141 -81.17 -22.25
REMARK 500
REMARK 500 THIS ENTRY HAS 673 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 17 N-TERMINAL RESIDUES WERE DELETED FROM THE SEQUENCE.
DBREF 1PJZ A 1 201 UNP O86262 TPMT_PSESJ 18 218
SEQADV 1PJZ GLY A -1 UNP O86262 CLONING ARTIFACT
SEQADV 1PJZ SER A 0 UNP O86262 CLONING ARTIFACT
SEQRES 1 A 203 GLY SER HIS GLN SER GLU VAL ASN LYS ASP LEU GLN GLN
SEQRES 2 A 203 TYR TRP SER SER LEU ASN VAL VAL PRO GLY ALA ARG VAL
SEQRES 3 A 203 LEU VAL PRO LEU CYS GLY LYS SER GLN ASP MET SER TRP
SEQRES 4 A 203 LEU SER GLY GLN GLY TYR HIS VAL VAL GLY ALA GLU LEU
SEQRES 5 A 203 SER GLU ALA ALA VAL GLU ARG TYR PHE THR GLU ARG GLY
SEQRES 6 A 203 GLU GLN PRO HIS ILE THR SER GLN GLY ASP PHE LYS VAL
SEQRES 7 A 203 TYR ALA ALA PRO GLY ILE GLU ILE TRP CYS GLY ASP PHE
SEQRES 8 A 203 PHE ALA LEU THR ALA ARG ASP ILE GLY HIS CYS ALA ALA
SEQRES 9 A 203 PHE TYR ASP ARG ALA ALA MET ILE ALA LEU PRO ALA ASP
SEQRES 10 A 203 MET ARG GLU ARG TYR VAL GLN HIS LEU GLU ALA LEU MET
SEQRES 11 A 203 PRO GLN ALA CYS SER GLY LEU LEU ILE THR LEU GLU TYR
SEQRES 12 A 203 ASP GLN ALA LEU LEU GLU GLY PRO PRO PHE SER VAL PRO
SEQRES 13 A 203 GLN THR TRP LEU HIS ARG VAL MET SER GLY ASN TRP GLU
SEQRES 14 A 203 VAL THR LYS VAL GLY GLY GLN ASP THR LEU HIS SER SER
SEQRES 15 A 203 ALA ARG GLY LEU LYS ALA GLY LEU GLU ARG MET ASP GLU
SEQRES 16 A 203 HIS VAL TYR VAL LEU GLU ARG VAL
HELIX 1 1 ASN A 6 ASN A 17 1 12
HELIX 2 2 SER A 32 GLY A 42 1 11
HELIX 3 3 SER A 51 GLY A 63 1 13
HELIX 4 4 THR A 93 HIS A 99 1 7
HELIX 5 5 ALA A 108 LEU A 112 5 5
HELIX 6 6 PRO A 113 MET A 128 1 16
HELIX 7 7 PRO A 154 VAL A 161 1 8
HELIX 8 8 SER A 180 GLY A 187 1 8
SHEET 1 A 9 HIS A 67 GLN A 71 0
SHEET 2 A 9 PHE A 74 ALA A 78 -1 O PHE A 74 N GLN A 71
SHEET 3 A 9 GLU A 83 GLY A 87 -1 O CYS A 86 N TYR A 77
SHEET 4 A 9 HIS A 44 LEU A 50 1 O GLU A 49 N GLY A 87
SHEET 5 A 9 ARG A 23 VAL A 26 1 N VAL A 24 O VAL A 46
SHEET 6 A 9 CYS A 100 ARG A 106 1 O CYS A 100 N ARG A 23
SHEET 7 A 9 ALA A 131 LEU A 139 1 O LEU A 135 N ASP A 105
SHEET 8 A 9 GLU A 193 ARG A 200 -1 O TYR A 196 N LEU A 136
SHEET 9 A 9 TRP A 166 GLY A 173 -1 N VAL A 171 O VAL A 195
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 - b 23 2 Bytes