Header list of 1tvm.pdb file
Complete list - r 2 2 Bytes
HEADER TRANSFERASE 29-JUN-04 1TVM
TITLE NMR STRUCTURE OF ENZYME GATB OF THE GALACTITOL-SPECIFIC
TITLE 2 PHOSPHOENOLPYRUVATE-DEPENDENT PHOSPHOTRANSFERASE SYSTEM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PTS SYSTEM, GALACTITOL-SPECIFIC IIB COMPONENT;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: EIIB-GAT, GALACTICOL-PERMEASE IIB COMPONENT,
COMPND 5 PHOSPHOTRANSFERASE ENZYME II, B COMPONENT, GATB;
COMPND 6 EC: 2.7.1.69;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: GATB, C2618, Z3256, ECS2896, SF2155, S2281;
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: PHIVTEV
KEYWDS PHOSPHOTRANSFERASE SYSTEM (PTS), P-LOOP, FOUR-STRANDED PARALLEL OPEN
KEYWDS 2 TWISTED BETA SHEET FLANKED BY ALPHA HELICES ON BOTH SIDES, E. COLI,
KEYWDS 3 MONTREAL-KINGSTON BACTERIAL STRUCTURAL GENOMICS INITIATIVE, BSGI,
KEYWDS 4 STRUCTURAL GENOMICS, TRANSFERASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR L.VOLPON,C.R.YOUNG,N.S.LIM,P.IANNUZZI,M.CYGLER,K.GEHRING,MONTREAL-
AUTHOR 2 KINGSTON BACTERIAL STRUCTURAL GENOMICS INITIATIVE (BSGI)
REVDAT 4 02-MAR-22 1TVM 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1TVM 1 VERSN
REVDAT 2 10-OCT-06 1TVM 1 JRNL
REVDAT 1 06-SEP-05 1TVM 0
JRNL AUTH L.VOLPON,C.R.YOUNG,A.MATTE,K.GEHRING
JRNL TITL NMR STRUCTURE OF THE ENZYME GATB OF THE GALACTITOL-SPECIFIC
JRNL TITL 2 PHOSPHOENOLPYRUVATE-DEPENDENT PHOSPHOTRANSFERASE SYSTEM AND
JRNL TITL 3 ITS INTERACTION WITH GATA.
JRNL REF PROTEIN SCI. V. 15 2435 2006
JRNL REFN ISSN 0961-8368
JRNL PMID 16963640
JRNL DOI 10.1110/PS.062337406
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.5, TALOS 2003.027.13.05, CNS 1.1
REMARK 3 AUTHORS : BAX (TALOS), BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 1377 RESTRAINTS: 1119 NOE-DERIVED DISTANCE CONSTRAINTS, 120
REMARK 3 DIHEDRAL ANGLE RESTRAINTS, 56 DISTANCE RESTRAINTS FROM HYDROGEN
REMARK 3 BONDS (28 HYDROGEN BONDS), AND 82 15N-1H RESIDUAL DIPOLAR
REMARK 3 COUPLINGS.
REMARK 4
REMARK 4 1TVM COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JUN-04.
REMARK 100 THE DEPOSITION ID IS D_1000022946.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.8
REMARK 210 IONIC STRENGTH : 100 MM PHOSPHATE, 75 MM NACL, 75
REMARK 210 MM KCL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1 MM U-15N,13C GATB, 100 MM
REMARK 210 PHOSPHATE BUFFER, 75 MM KCL, 75
REMARK 210 MM NACL, 1 MM DTT, 1 MM SODIUM
REMARK 210 AZIDE, 90% H2O, 10 % D2O; 1 MM U-
REMARK 210 15N,13C GATB, 100 MM PHOSPHATE
REMARK 210 BUFFER, 75 MM KCL, 75 MM NACL, 1
REMARK 210 MM DTT, 1 MM SODIUM AZIDE, 100 %
REMARK 210 D2O; 1 MM U-15N,13C GATB, 100 MM
REMARK 210 PHOSPHATE BUFFER, 75 MM KCL, 75
REMARK 210 MM NACL, 1 MM DTT, 1 MM SODIUM
REMARK 210 AZIDE, 5 MG/ML OF PF1 PHAGE, 90%
REMARK 210 H2O, 10 % D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; MOTHER-NOESY (1H-13C
REMARK 210 REGION); 3D_15N-SEPARATED_NOESY;
REMARK 210 IPAP-HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 3.5, NMRVIEW 4.0, SPARKY
REMARK 210 3.106
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : 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: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR AND 3D HETERONUCLEAR TECHNIQUES.
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 O ALA A 38 H ILE A 42 1.58
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 4 97.71 51.43
REMARK 500 1 HIS A 6 102.66 62.79
REMARK 500 1 HIS A 10 138.50 172.08
REMARK 500 1 HIS A 11 55.49 -96.90
REMARK 500 1 HIS A 12 90.93 -60.22
REMARK 500 1 GLN A 18 34.15 -84.39
REMARK 500 1 SER A 20 -67.80 66.21
REMARK 500 1 LYS A 21 -65.56 -164.44
REMARK 500 1 CYS A 28 -56.18 -150.53
REMARK 500 1 ALA A 33 -33.94 77.17
REMARK 500 1 ASN A 50 60.60 60.06
REMARK 500 1 GLU A 62 -35.93 -143.99
REMARK 500 1 MET A 67 49.80 -75.77
REMARK 500 1 ALA A 77 84.00 52.22
REMARK 500 1 ARG A 78 -60.24 -151.60
REMARK 500 1 ASP A 85 30.38 -156.41
REMARK 500 1 ILE A 86 104.22 -53.33
REMARK 500 1 PRO A 87 72.91 -69.17
REMARK 500 2 HIS A 6 78.97 -113.47
REMARK 500 2 LEU A 15 71.03 59.06
REMARK 500 2 TYR A 16 -53.30 -145.07
REMARK 500 2 GLN A 18 93.13 -166.53
REMARK 500 2 LYS A 21 -55.72 -132.38
REMARK 500 2 ALA A 31 -76.34 -82.03
REMARK 500 2 VAL A 32 -21.10 75.84
REMARK 500 2 PRO A 52 98.96 -55.45
REMARK 500 2 GLU A 62 -34.85 -153.90
REMARK 500 2 MET A 67 46.78 -77.03
REMARK 500 2 ALA A 77 -23.73 177.89
REMARK 500 2 VAL A 79 42.01 -77.51
REMARK 500 2 ASP A 85 18.77 -154.10
REMARK 500 2 ILE A 86 103.60 -55.85
REMARK 500 2 PRO A 87 74.41 -66.24
REMARK 500 3 HIS A 5 89.83 -158.52
REMARK 500 3 HIS A 7 48.23 -98.92
REMARK 500 3 HIS A 8 86.24 -154.29
REMARK 500 3 GLU A 13 119.01 66.49
REMARK 500 3 LEU A 15 -77.35 -75.83
REMARK 500 3 TYR A 16 106.10 179.56
REMARK 500 3 LYS A 21 -82.98 -144.71
REMARK 500 3 VAL A 32 -43.86 75.35
REMARK 500 3 ALA A 33 64.23 -153.40
REMARK 500 3 THR A 34 -40.23 -154.44
REMARK 500 3 ARG A 59 -163.89 -72.80
REMARK 500 3 ASN A 61 69.95 -151.30
REMARK 500 3 GLU A 62 -33.47 -150.05
REMARK 500 3 MET A 67 49.46 -74.36
REMARK 500 3 ALA A 77 -26.74 178.76
REMARK 500 3 VAL A 79 47.09 -74.91
REMARK 500 3 ASP A 85 22.36 -159.58
REMARK 500
REMARK 500 THIS ENTRY HAS 366 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: PTKB_ECO57 RELATED DB: TARGETDB
DBREF 1TVM A 21 113 UNP Q8X7H5 PTKB_ECOL6 2 94
SEQADV 1TVM MET A 1 UNP Q8X7H5 EXPRESSION TAG
SEQADV 1TVM GLY A 2 UNP Q8X7H5 EXPRESSION TAG
SEQADV 1TVM SER A 3 UNP Q8X7H5 EXPRESSION TAG
SEQADV 1TVM SER A 4 UNP Q8X7H5 EXPRESSION TAG
SEQADV 1TVM HIS A 5 UNP Q8X7H5 EXPRESSION TAG
SEQADV 1TVM HIS A 6 UNP Q8X7H5 EXPRESSION TAG
SEQADV 1TVM HIS A 7 UNP Q8X7H5 EXPRESSION TAG
SEQADV 1TVM HIS A 8 UNP Q8X7H5 EXPRESSION TAG
SEQADV 1TVM HIS A 9 UNP Q8X7H5 EXPRESSION TAG
SEQADV 1TVM HIS A 10 UNP Q8X7H5 EXPRESSION TAG
SEQADV 1TVM HIS A 11 UNP Q8X7H5 EXPRESSION TAG
SEQADV 1TVM HIS A 12 UNP Q8X7H5 EXPRESSION TAG
SEQADV 1TVM GLU A 13 UNP Q8X7H5 EXPRESSION TAG
SEQADV 1TVM ASN A 14 UNP Q8X7H5 EXPRESSION TAG
SEQADV 1TVM LEU A 15 UNP Q8X7H5 EXPRESSION TAG
SEQADV 1TVM TYR A 16 UNP Q8X7H5 EXPRESSION TAG
SEQADV 1TVM PHE A 17 UNP Q8X7H5 EXPRESSION TAG
SEQADV 1TVM GLN A 18 UNP Q8X7H5 EXPRESSION TAG
SEQADV 1TVM GLY A 19 UNP Q8X7H5 EXPRESSION TAG
SEQADV 1TVM SER A 20 UNP Q8X7H5 EXPRESSION TAG
SEQRES 1 A 113 MET GLY SER SER HIS HIS HIS HIS HIS HIS HIS HIS GLU
SEQRES 2 A 113 ASN LEU TYR PHE GLN GLY SER LYS ARG LYS ILE ILE VAL
SEQRES 3 A 113 ALA CYS GLY GLY ALA VAL ALA THR SER THR MET ALA ALA
SEQRES 4 A 113 GLU GLU ILE LYS GLU LEU CYS GLN SER HIS ASN ILE PRO
SEQRES 5 A 113 VAL GLU LEU ILE GLN CYS ARG VAL ASN GLU ILE GLU THR
SEQRES 6 A 113 TYR MET ASP GLY VAL HIS LEU ILE CYS THR THR ALA ARG
SEQRES 7 A 113 VAL ASP ARG SER PHE GLY ASP ILE PRO LEU VAL HIS GLY
SEQRES 8 A 113 MET PRO PHE VAL SER GLY VAL GLY ILE GLU ALA LEU GLN
SEQRES 9 A 113 ASN LYS ILE LEU THR ILE LEU GLN GLY
HELIX 1 1 ALA A 33 HIS A 49 1 17
HELIX 2 2 GLY A 91 GLY A 97 1 7
HELIX 3 3 GLY A 99 GLY A 113 1 15
SHEET 1 A 4 VAL A 53 CYS A 58 0
SHEET 2 A 4 ARG A 22 ALA A 27 1 N VAL A 26 O CYS A 58
SHEET 3 A 4 LEU A 72 THR A 75 1 O CYS A 74 N ALA A 27
SHEET 4 A 4 LEU A 88 VAL A 89 1 O VAL A 89 N ILE A 73
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