HEADER ISOMERASE 17-JUN-10 2KZH
TITLE THREE-DIMENSIONAL STRUCTURE OF A TRUNCATED PHOSPHORIBOSYLANTHRANILATE
TITLE 2 ISOMERASE (RESIDUES 255-384) FROM ESCHERICHIA COLI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRYPTOPHAN BIOSYNTHESIS PROTEIN TRPCF;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: N-(5'-PHOSPHO-RIBOSYL)ANTHRANILATE ISOMERASE, PRAI, TRPRAI;
COMPND 5 EC: 5.3.1.24;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K12;
SOURCE 5 GENE: TRPC, B1262, JW1254;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: VECTOR;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: PWP107
KEYWDS TIM-BARREL, TRYPTOPHAN BIOSYNTHESIS, PROTEIN EVOLUTION, SUBDOMAIN,
KEYWDS 2 ISOMERASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR S.SETIYAPUTRA,J.P.MACKAY,W.M.PATRICK
REVDAT 4 14-JUN-23 2KZH 1 REMARK
REVDAT 3 26-FEB-20 2KZH 1 REMARK SEQADV
REVDAT 2 13-JUL-11 2KZH 1 JRNL
REVDAT 1 09-MAR-11 2KZH 0
JRNL AUTH S.SETIYAPUTRA,J.P.MACKAY,W.M.PATRICK
JRNL TITL THE STRUCTURE OF A TRUNCATED PHOSPHORIBOSYLANTHRANILATE
JRNL TITL 2 ISOMERASE SUGGESTS A UNIFIED MODEL FOR EVOLUTION OF THE
JRNL TITL 3 (BETA ALPHA)8 BARREL FOLD
JRNL REF J.MOL.BIOL. V. 408 291 2011
JRNL REFN ISSN 0022-2836
JRNL PMID 21354426
JRNL DOI 10.1016/J.JMB.2011.02.048
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH W.M.PATRICK,J.M.BLACKBURN
REMARK 1 TITL IN VITRO SELECTION AND CHARACTERIZATION OF A STABLE
REMARK 1 TITL 2 SUBDOMAIN OF PHOSPHORIBOSYLANTHRANILATE ISOMERASE.
REMARK 1 REF FEBS J. V. 272 3684 2005
REMARK 1 REFN ISSN 1742-464X
REMARK 1 PMID 16008567
REMARK 1 DOI 10.1111/J.1742-4658.2005.04794.X
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CYANA 3.0, CNS 1.21
REMARK 3 AUTHORS : GUNTERT, MUMENTHALER AND WUTHRICH (CYANA),
REMARK 3 BRUNGER, ADAMS, CLORE, GROS, NILGES AND READ (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: CARTESIAN MOLECULAR DYNAMICS
REMARK 4
REMARK 4 2KZH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-JUN-10.
REMARK 100 THE DEPOSITION ID IS D_1000101767.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 0.1
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.8 MM TRPRAI-1, 20 MM HEPES-2,
REMARK 210 100 MM SODIUM CHLORIDE-3, 1 MM
REMARK 210 DTT-4, 0.1 MM DSS-5, 95% H2O/5%
REMARK 210 D2O; 0.6-1.0 MM [U-99% 15N]
REMARK 210 TRPRAI-6, 20 MM HEPES-7, 100 MM
REMARK 210 SODIUM CHLORIDE-8, 1 MM DTT-9,
REMARK 210 0.1 MM DSS-10, 95% H2O/5% D2O;
REMARK 210 0.6-0.8 MM [U-98% 13C; U-98% 15N]
REMARK 210 TRPRAI-11, 20 MM HEPES-12, 100
REMARK 210 MM SODIUM CHLORIDE-13, 1 MM DTT-
REMARK 210 14, 0.1 MM DSS-15, 95% H2O/5%
REMARK 210 D2O; 0.7 MM [U-98% 13C; U-98%
REMARK 210 15N] TRPRAI-16, 20 MM HEPES-17,
REMARK 210 100 MM SODIUM CHLORIDE-18, 1 MM
REMARK 210 DTT-19, 0.1 MM DSS-20, 100% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC; 2D 1H-13C HSQC;
REMARK 210 3D CBCA(CO)NH; 3D HNCACB; 3D
REMARK 210 HNCO; 2D 1H-1H NOESY; 3D HBHA(CO)
REMARK 210 NH; 3D H(CCO)NH; 3D C(CO)NH; 3D
REMARK 210 HCCH-TOCSY; 3D HCCH-COSY; 3D 1H-
REMARK 210 15N NOESY; 3D 1H-13C NOESY; 3D
REMARK 210 1H-13C NOESY AROMATIC; 3D HNHA;
REMARK 210 3D 1H-15N TOCSY; 3D HN(CA)CO
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CYANA 3.0, TOPSPIN 2.1, SPARKY
REMARK 210 3.113, TALOS TALOS+, CNS 1.21,
REMARK 210 PROCHECKNMR 3.5.3
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
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 HIS A 135
REMARK 465 HIS A 136
REMARK 465 HIS A 137
REMARK 465 HIS A 138
REMARK 465 HIS A 139
REMARK 465 HIS A 140
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
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 4 25.83 -149.28
REMARK 500 1 ALA A 32 108.84 -49.69
REMARK 500 1 SER A 74 88.84 62.28
REMARK 500 1 ALA A 98 4.12 -69.14
REMARK 500 1 GLN A 129 114.32 69.30
REMARK 500 2 SER A 74 74.88 67.75
REMARK 500 2 LEU A 75 -168.40 -77.81
REMARK 500 2 ALA A 76 -52.39 -128.70
REMARK 500 2 GLU A 85 147.88 -179.50
REMARK 500 2 GLU A 116 -61.51 -132.07
REMARK 500 2 ALA A 132 117.65 68.58
REMARK 500 3 ASN A 4 29.75 -149.82
REMARK 500 3 PRO A 51 71.39 -68.12
REMARK 500 3 SER A 74 72.21 59.09
REMARK 500 3 ASN A 83 -24.84 -39.00
REMARK 500 3 GLU A 85 148.65 -175.11
REMARK 500 3 GLU A 116 -85.07 -103.30
REMARK 500 4 ASN A 4 28.50 -148.20
REMARK 500 4 SER A 74 73.29 52.32
REMARK 500 4 GLU A 85 135.45 -175.74
REMARK 500 4 GLU A 116 -58.75 -149.08
REMARK 500 5 GLU A 3 -75.49 -86.20
REMARK 500 5 LYS A 5 93.15 -47.22
REMARK 500 5 THR A 33 72.89 52.33
REMARK 500 5 PRO A 35 5.83 -65.67
REMARK 500 5 PRO A 51 45.02 -73.25
REMARK 500 5 HIS A 61 -74.65 -106.28
REMARK 500 5 SER A 107 107.28 -59.02
REMARK 500 5 GLU A 110 -73.93 -90.10
REMARK 500 5 ASP A 126 89.00 -66.95
REMARK 500 6 GLU A 3 111.05 68.54
REMARK 500 6 ASN A 4 37.90 -148.52
REMARK 500 6 ALA A 32 96.80 -43.86
REMARK 500 6 PRO A 35 19.90 -67.74
REMARK 500 6 PRO A 51 48.30 -76.06
REMARK 500 6 HIS A 61 -61.43 -107.93
REMARK 500 6 SER A 74 74.43 59.89
REMARK 500 6 GLU A 85 148.90 -176.88
REMARK 500 6 GLU A 116 -60.44 -134.87
REMARK 500 6 ASP A 126 102.74 -56.56
REMARK 500 7 ASN A 4 44.78 -153.28
REMARK 500 7 LYS A 5 96.20 -67.59
REMARK 500 7 LEU A 9 147.58 -172.29
REMARK 500 7 SER A 74 82.83 60.09
REMARK 500 7 GLU A 116 -68.62 -136.23
REMARK 500 8 LYS A 5 101.49 -51.03
REMARK 500 8 TYR A 25 -172.09 -170.60
REMARK 500 8 THR A 33 9.63 53.73
REMARK 500 8 PRO A 35 0.16 -67.32
REMARK 500 8 SER A 74 73.63 54.69
REMARK 500
REMARK 500 THIS ENTRY HAS 144 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 1 ARG A 59 0.07 SIDE CHAIN
REMARK 500 14 ARG A 93 0.08 SIDE CHAIN
REMARK 500 15 ARG A 93 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR DETERMINED
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: AUTHOR DETERMINED
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1PII RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE FULL-LENGTH PHOSPHORYBOSILANTHRANILATE
REMARK 900 ISOMERASE (PRAI) FROM ESCHERICIA COLI
REMARK 900 RELATED ID: 17005 RELATED DB: BMRB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 RESIDUES 132-134 ARE ACTUALLY RESIDUES FROM A LINKER THAT CONNECTS
REMARK 999 THE MOLECULE TO THE HEXAHISTIDINE TAG
DBREF 2KZH A 2 131 UNP P00909 TRPC_ECOLI 255 384
SEQADV 2KZH MET A 1 UNP P00909 INITIATING METHIONINE
SEQADV 2KZH ALA A 132 UNP P00909 SEE REMARK 999
SEQADV 2KZH GLY A 133 UNP P00909 SEE REMARK 999
SEQADV 2KZH SER A 134 UNP P00909 SEE REMARK 999
SEQADV 2KZH HIS A 135 UNP P00909 EXPRESSION TAG
SEQADV 2KZH HIS A 136 UNP P00909 EXPRESSION TAG
SEQADV 2KZH HIS A 137 UNP P00909 EXPRESSION TAG
SEQADV 2KZH HIS A 138 UNP P00909 EXPRESSION TAG
SEQADV 2KZH HIS A 139 UNP P00909 EXPRESSION TAG
SEQADV 2KZH HIS A 140 UNP P00909 EXPRESSION TAG
SEQRES 1 A 140 MET GLY GLU ASN LYS VAL CYS GLY LEU THR ARG GLY GLN
SEQRES 2 A 140 ASP ALA LYS ALA ALA TYR ASP ALA GLY ALA ILE TYR GLY
SEQRES 3 A 140 GLY LEU ILE PHE VAL ALA THR SER PRO ARG CYS VAL ASN
SEQRES 4 A 140 VAL GLU GLN ALA GLN GLU VAL MET ALA ALA ALA PRO LEU
SEQRES 5 A 140 GLN TYR VAL GLY VAL PHE ARG ASN HIS ASP ILE ALA ASP
SEQRES 6 A 140 VAL VAL ASP LYS ALA LYS VAL LEU SER LEU ALA ALA VAL
SEQRES 7 A 140 GLN LEU HIS GLY ASN GLU GLU GLN LEU TYR ILE ASP THR
SEQRES 8 A 140 LEU ARG GLU ALA LEU PRO ALA HIS VAL ALA ILE TRP LYS
SEQRES 9 A 140 ALA LEU SER VAL GLY GLU THR LEU PRO ALA ARG GLU PHE
SEQRES 10 A 140 GLN HIS VAL ASP LYS TYR VAL LEU ASP ASN GLY GLN GLY
SEQRES 11 A 140 GLY ALA GLY SER HIS HIS HIS HIS HIS HIS
HELIX 1 1 ARG A 11 GLY A 22 1 12
HELIX 2 2 ASN A 39 MET A 47 1 9
HELIX 3 3 ASP A 62 LEU A 73 1 12
HELIX 4 4 GLY A 82 GLU A 84 5 3
HELIX 5 5 GLN A 86 LEU A 96 1 11
SHEET 1 A 4 TYR A 54 PHE A 58 0
SHEET 2 A 4 ALA A 76 LEU A 80 1 O GLN A 79 N GLY A 56
SHEET 3 A 4 ALA A 101 LEU A 106 1 O TRP A 103 N VAL A 78
SHEET 4 A 4 LYS A 122 LEU A 125 1 O VAL A 124 N LEU A 106
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
(ATOM LINES ARE NOT SHOWN.)
END
