Header list of 2fek.pdb file
Complete list - r 9 2 Bytes
HEADER HYDROLASE 16-DEC-05 2FEK
TITLE STRUCTURE OF A PROTEIN TYROSINE PHOSPHATASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LOW MOLECULAR WEIGHT PROTEIN-TYROSINE-PHOSPHATASE WZB;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.3.48;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI K12;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K-12;
SOURCE 5 GENE: WZB;
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: PET28A
KEYWDS LOW MOLECULAR WEIGHT PROTEIN TYROSINE PHOSPHATASE, ESCHERICHIA COLI,
KEYWDS 2 PHOSPHATE BINDING, HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR E.LESCOP,C.JIN
REVDAT 4 09-MAR-22 2FEK 1 REMARK SEQADV
REVDAT 3 24-FEB-09 2FEK 1 VERSN
REVDAT 2 26-SEP-06 2FEK 1 JRNL
REVDAT 1 09-MAY-06 2FEK 0
JRNL AUTH E.LESCOP,Y.HU,H.XU,W.HU,J.CHEN,B.XIA,C.JIN
JRNL TITL THE SOLUTION STRUCTURE OF ESCHERICHIA COLI WZB REVEALS A
JRNL TITL 2 NOVEL SUBSTRATE RECOGNITION MECHANISM OF PROKARYOTIC LOW
JRNL TITL 3 MOLECULAR WEIGHT PROTEIN-TYROSINE PHOSPHATASES
JRNL REF J.BIOL.CHEM. V. 281 19570 2006
JRNL REFN ISSN 0021-9258
JRNL PMID 16651264
JRNL DOI 10.1074/JBC.M601263200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.5, AMBER 7
REMARK 3 AUTHORS : BRUKER (XWINNMR), CASE (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: A TOTAL OF 4689 RESTRAINTS WERE USED.
REMARK 3 INCLUDED ARE 1630 AMBIGUOUS AND 2640 UNAMBIGUOUS NOE-DERIVED
REMARK 3 DISTANCES, 100 HYDROGEN BOND RESTRAINTS, 190 BACKBONE DIHEDRAL
REMARK 3 ANGLES, 32 SIDE-CHAIN CHI1 AND 97 1H-15N RESIDUAL DIPOLAR
REMARK 3 COUPLINGS VALUES.
REMARK 4
REMARK 4 2FEK COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-DEC-05.
REMARK 100 THE DEPOSITION ID IS D_1000035783.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6
REMARK 210 IONIC STRENGTH : 100MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : ~1MM WZB U-15N, 13C; 50MM SODIUM
REMARK 210 PHOSPHATE, 50MM NACL BUFFER;
REMARK 210 25MM DTT; 5MM EDTA; PH 6; ~1MM
REMARK 210 WZB U-15N; 50MM SODIUM PHOSPHATE,
REMARK 210 50MM NACL BUFFER; 25MM DTT; 5MM
REMARK 210 EDTA; PH 6
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 1, CYANA 1.2, NMRVIEW 5
REMARK 210 METHOD USED : 200 STRUCTURES WERE GENERATED IN
REMARK 210 CYANA. THE 100 STRUCTURES WITH
REMARK 210 LOWEST ENERGY WERE FURTHER
REMARK 210 REFINED IN AMBER7. THE 20 LOWEST
REMARK 210 ENERGY STRUCTURES WERE FINALLY
REMARK 210 SELECTED.
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: 97 1H-15N RESIDUAL DIPOLAR, MEASURED IN PEG/HEXANOL (5.5
REMARK 210 WT%, MOLAR RATIO=0.92), WERE INCLUDED IN STRUCTURE CALCULATION.
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 -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS 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 OE1 GLU A 20 HG SER A 34 1.56
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
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 ATM2 ATM3
REMARK 500 6 ARG A 66 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 6 ARG A 89 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 8 ARG A 89 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 9 ARG A 85 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 12 ARG A 85 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 17 ARG A 74 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 18 ARG A 21 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 18 ARG A 66 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
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 12 -49.33 77.52
REMARK 500 1 ILE A 13 -5.26 -58.26
REMARK 500 1 CYS A 14 -75.90 -126.28
REMARK 500 1 LEU A 40 57.63 -101.47
REMARK 500 1 LEU A 60 25.05 -77.93
REMARK 500 1 TYR A 117 -85.81 22.64
REMARK 500 1 ALA A 144 -157.02 -77.75
REMARK 500 2 PHE A 2 58.42 -67.90
REMARK 500 2 ASN A 12 -50.44 71.11
REMARK 500 2 CYS A 14 -75.08 -117.11
REMARK 500 2 LEU A 60 22.87 -78.11
REMARK 500 2 PRO A 114 172.09 -57.28
REMARK 500 3 CYS A 14 -42.02 -135.84
REMARK 500 3 ALA A 35 -168.64 -163.14
REMARK 500 3 PRO A 114 176.82 -57.62
REMARK 500 4 ASN A 12 -36.70 67.39
REMARK 500 4 ILE A 13 0.83 -60.48
REMARK 500 4 CYS A 14 -63.20 -147.74
REMARK 500 4 LEU A 40 76.37 -114.61
REMARK 500 4 ASP A 108 59.83 -91.29
REMARK 500 5 ASN A 12 -39.97 66.03
REMARK 500 5 CYS A 14 -78.84 -128.04
REMARK 500 5 TYR A 117 -95.55 22.45
REMARK 500 5 GLU A 145 26.77 39.74
REMARK 500 6 ASN A 3 -19.22 52.68
REMARK 500 6 ASN A 12 -58.75 65.47
REMARK 500 6 ARG A 15 -45.16 -139.24
REMARK 500 6 PRO A 114 171.86 -56.55
REMARK 500 6 TYR A 117 -67.65 -20.18
REMARK 500 6 GLU A 145 36.41 39.77
REMARK 500 7 ASN A 3 -46.70 68.85
REMARK 500 7 ASN A 12 -55.10 66.62
REMARK 500 7 ILE A 13 6.49 -58.39
REMARK 500 7 CYS A 14 -64.86 -139.14
REMARK 500 7 PRO A 114 171.02 -55.40
REMARK 500 7 TYR A 117 -69.82 2.38
REMARK 500 7 GLU A 145 32.64 -152.91
REMARK 500 8 PHE A 2 50.80 -68.37
REMARK 500 8 ASN A 12 -50.46 64.02
REMARK 500 8 CYS A 14 -69.76 -124.88
REMARK 500 9 ASN A 12 -49.05 71.66
REMARK 500 9 ILE A 13 2.05 -65.65
REMARK 500 9 CYS A 14 -73.96 -121.10
REMARK 500 9 LEU A 40 68.17 -116.80
REMARK 500 9 PRO A 114 171.65 -59.56
REMARK 500 9 ALA A 144 -152.39 -77.52
REMARK 500 10 ASN A 12 -58.46 67.39
REMARK 500 10 ILE A 13 0.33 -60.71
REMARK 500 10 ARG A 15 -49.75 -135.45
REMARK 500 10 LEU A 40 67.27 -109.31
REMARK 500
REMARK 500 THIS ENTRY HAS 108 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 5 ARG A 66 0.09 SIDE CHAIN
REMARK 500 6 TYR A 128 0.07 SIDE CHAIN
REMARK 500 13 ARG A 21 0.10 SIDE CHAIN
REMARK 500 13 ARG A 85 0.09 SIDE CHAIN
REMARK 500 14 ARG A 70 0.09 SIDE CHAIN
REMARK 500 15 TYR A 76 0.08 SIDE CHAIN
REMARK 500 15 ARG A 118 0.08 SIDE CHAIN
REMARK 500 17 ARG A 85 0.11 SIDE CHAIN
REMARK 500 18 ARG A 85 0.12 SIDE CHAIN
REMARK 500 19 TYR A 128 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2FEK A 1 147 UNP P0AAB2 WZB_ECOLI 1 147
SEQADV 2FEK MET A -19 UNP P0AAB2 EXPRESSION TAG
SEQADV 2FEK GLY A -18 UNP P0AAB2 EXPRESSION TAG
SEQADV 2FEK SER A -17 UNP P0AAB2 EXPRESSION TAG
SEQADV 2FEK SER A -16 UNP P0AAB2 EXPRESSION TAG
SEQADV 2FEK HIS A -15 UNP P0AAB2 EXPRESSION TAG
SEQADV 2FEK HIS A -14 UNP P0AAB2 EXPRESSION TAG
SEQADV 2FEK HIS A -13 UNP P0AAB2 EXPRESSION TAG
SEQADV 2FEK HIS A -12 UNP P0AAB2 EXPRESSION TAG
SEQADV 2FEK HIS A -11 UNP P0AAB2 EXPRESSION TAG
SEQADV 2FEK HIS A -10 UNP P0AAB2 EXPRESSION TAG
SEQADV 2FEK SER A -9 UNP P0AAB2 EXPRESSION TAG
SEQADV 2FEK SER A -8 UNP P0AAB2 EXPRESSION TAG
SEQADV 2FEK GLY A -7 UNP P0AAB2 EXPRESSION TAG
SEQADV 2FEK LEU A -6 UNP P0AAB2 EXPRESSION TAG
SEQADV 2FEK VAL A -5 UNP P0AAB2 EXPRESSION TAG
SEQADV 2FEK PRO A -4 UNP P0AAB2 EXPRESSION TAG
SEQADV 2FEK ARG A -3 UNP P0AAB2 EXPRESSION TAG
SEQADV 2FEK GLY A -2 UNP P0AAB2 EXPRESSION TAG
SEQADV 2FEK SER A -1 UNP P0AAB2 EXPRESSION TAG
SEQADV 2FEK HIS A 0 UNP P0AAB2 EXPRESSION TAG
SEQRES 1 A 167 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 167 LEU VAL PRO ARG GLY SER HIS MET PHE ASN ASN ILE LEU
SEQRES 3 A 167 VAL VAL CYS VAL GLY ASN ILE CYS ARG SER PRO THR ALA
SEQRES 4 A 167 GLU ARG LEU LEU GLN ARG TYR HIS PRO GLU LEU LYS VAL
SEQRES 5 A 167 GLU SER ALA GLY LEU GLY ALA LEU VAL GLY LYS GLY ALA
SEQRES 6 A 167 ASP PRO THR ALA ILE SER VAL ALA ALA GLU HIS GLN LEU
SEQRES 7 A 167 SER LEU GLU GLY HIS CYS ALA ARG GLN ILE SER ARG ARG
SEQRES 8 A 167 LEU CYS ARG ASN TYR ASP LEU ILE LEU THR MET GLU LYS
SEQRES 9 A 167 ARG HIS ILE GLU ARG LEU CYS GLU MET ALA PRO GLU MET
SEQRES 10 A 167 ARG GLY LYS VAL MET LEU PHE GLY HIS TRP ASP ASN GLU
SEQRES 11 A 167 CYS GLU ILE PRO ASP PRO TYR ARG LYS SER ARG GLU THR
SEQRES 12 A 167 PHE ALA ALA VAL TYR THR LEU LEU GLU ARG SER ALA ARG
SEQRES 13 A 167 GLN TRP ALA GLN ALA LEU ASN ALA GLU GLN VAL
HELIX 1 1 CYS A 14 HIS A 27 1 14
HELIX 2 2 ASP A 46 HIS A 56 1 11
HELIX 3 3 SER A 69 TYR A 76 1 8
HELIX 4 4 GLU A 83 ALA A 94 1 12
HELIX 5 5 PRO A 95 GLY A 99 5 5
HELIX 6 6 GLY A 105 ASP A 108 5 4
HELIX 7 7 SER A 120 ALA A 144 1 25
SHEET 1 A 4 LYS A 31 GLY A 36 0
SHEET 2 A 4 ASN A 4 CYS A 9 1 N VAL A 7 O ALA A 35
SHEET 3 A 4 LEU A 78 THR A 81 1 O LEU A 80 N LEU A 6
SHEET 4 A 4 VAL A 101 LEU A 103 1 O MET A 102 N ILE A 79
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