Header list of 1p88.pdb file
Complete list - b 23 2 Bytes
HEADER TRANSFERASE 06-MAY-03 1P88
TITLE SUBSTRATE-INDUCED STRUCTURAL CHANGES TO THE ISOLATED N-TERMINAL DOMAIN
TITLE 2 OF 5-ENOLPYRUVYLSHIKIMATE-3-PHOSPHATE SYNTHASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 3-PHOSPHOSHIKIMATE 1-CARBOXYVINYLTRANSFERASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL DOMAIN (25-240);
COMPND 5 SYNONYM: 5- ENOLPYRUVYLSHIKIMATE-3-PHOSPHATE SYNTHASE, EPSP SYNTHASE,
COMPND 6 EPSPS;
COMPND 7 EC: 2.5.1.19;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 STRAIN: O157;
SOURCE 5 GENE: AROA OR B0908 OR Z1254 OR ECS0991;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS EPSP SYNTHASE, NMR STRUCTURE FROM MOLMOL, TRANSFERASE
EXPDTA SOLUTION NMR
NUMMDL 11
MDLTYP MINIMIZED AVERAGE
AUTHOR J.K.YOUNG,M.E.STAUFFER,H.J.KIM,G.L.HELMS,J.N.S.EVANS
REVDAT 3 23-FEB-22 1P88 1 REMARK
REVDAT 2 24-FEB-09 1P88 1 VERSN
REVDAT 1 02-NOV-04 1P88 0
JRNL AUTH J.K.YOUNG,M.E.STAUFFER,H.J.KIM,G.L.HELMS,J.N.S.EVANS
JRNL TITL LETTER: SUBSTRATE-INDUCED STRUCTURAL CHANGES TO THE ISOLATED
JRNL TITL 2 N-TERMINAL DOMAIN OF 5-ENOLPYRUVYLSHIKIMATE-3-PHOSPHATE
JRNL TITL 3 SYNTHASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1, CNS 1.1
REMARK 3 AUTHORS : BRUNGER (CNS), BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1P88 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-MAY-03.
REMARK 100 THE DEPOSITION ID IS D_1000019130.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : CNS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 10
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 11
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY
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 O HIS A 52 H ALA A 56 1.36
REMARK 500 H VAL A 162 O VAL A 188 1.50
REMARK 500 O ILE A 203 H LEU A 207 1.50
REMARK 500 O GLY A 37 H GLY A 77 1.53
REMARK 500 O PRO A 181 H GLN A 229 1.53
REMARK 500 H LEU A 88 O ASP A 112 1.54
REMARK 500 O ILE A 113 H LEU A 153 1.56
REMARK 500 O VAL A 40 H TYR A 237 1.56
REMARK 500 O PHE A 211 H GLN A 232 1.58
REMARK 500 H VAL A 40 O GLY A 235 1.58
REMARK 500 H THR A 65 O GLU A 74 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 ASN A 26 -81.91 63.84
REMARK 500 1 LEU A 44 -177.47 -52.92
REMARK 500 1 ASP A 48 -32.31 -36.10
REMARK 500 1 SER A 67 -158.99 -63.94
REMARK 500 1 ILE A 76 98.86 -67.73
REMARK 500 1 LEU A 92 54.82 -104.03
REMARK 500 1 ALA A 95 45.58 -92.76
REMARK 500 1 LEU A 108 -75.95 -85.51
REMARK 500 1 LEU A 143 -85.03 -88.50
REMARK 500 1 GLU A 144 -83.87 -66.28
REMARK 500 1 GLN A 154 27.23 -145.87
REMARK 500 1 VAL A 168 -79.86 -146.22
REMARK 500 1 SER A 197 63.61 -165.23
REMARK 500 1 GLN A 218 -143.23 -108.18
REMARK 500 1 GLN A 221 -129.99 -165.74
REMARK 500 1 GLN A 222 128.70 -3.06
REMARK 500 2 ASN A 26 -87.43 56.93
REMARK 500 2 LEU A 44 -172.94 -54.68
REMARK 500 2 ASP A 48 -30.45 -36.42
REMARK 500 2 SER A 67 -167.22 -61.21
REMARK 500 2 ILE A 76 99.62 -68.51
REMARK 500 2 LEU A 92 47.31 -104.89
REMARK 500 2 LEU A 108 -71.02 -91.91
REMARK 500 2 SER A 110 98.84 -58.16
REMARK 500 2 LEU A 143 -90.26 -91.09
REMARK 500 2 GLU A 144 -81.51 -58.99
REMARK 500 2 GLN A 154 26.93 -147.35
REMARK 500 2 VAL A 168 67.19 -179.31
REMARK 500 2 SER A 169 126.52 64.53
REMARK 500 2 SER A 197 65.05 -168.51
REMARK 500 2 GLN A 218 -136.70 -108.30
REMARK 500 2 GLN A 221 -128.32 -160.69
REMARK 500 2 GLN A 222 129.24 -4.53
REMARK 500 2 PRO A 234 1.10 -69.95
REMARK 500 3 ASN A 26 -81.20 62.99
REMARK 500 3 LEU A 44 -170.82 -55.05
REMARK 500 3 ASP A 48 -29.14 -36.71
REMARK 500 3 SER A 67 -167.44 -61.43
REMARK 500 3 LEU A 92 57.93 -114.29
REMARK 500 3 ALA A 95 45.53 -92.63
REMARK 500 3 LEU A 108 -76.60 -79.81
REMARK 500 3 LEU A 143 -88.50 -96.46
REMARK 500 3 GLU A 144 -80.98 -57.38
REMARK 500 3 GLN A 154 24.98 -148.33
REMARK 500 3 SER A 197 65.49 -168.16
REMARK 500 3 GLN A 218 -144.86 -108.07
REMARK 500 3 GLN A 221 -126.22 -159.78
REMARK 500 3 GLN A 222 134.98 -10.11
REMARK 500 3 PRO A 234 0.10 -66.75
REMARK 500 4 ASN A 26 -95.21 59.63
REMARK 500
REMARK 500 THIS ENTRY HAS 187 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1P88 A 25 240 UNP P0A6D3 AROA_ECOLI 25 240
SEQRES 1 A 216 SER ASN ARG ALA LEU LEU LEU ALA ALA LEU ALA HIS GLY
SEQRES 2 A 216 LYS THR VAL LEU THR ASN LEU LEU ASP SER ASP ASP VAL
SEQRES 3 A 216 ARG HIS MET LEU ASN ALA LEU THR ALA LEU GLY VAL SER
SEQRES 4 A 216 TYR THR LEU SER ALA ASP ARG THR ARG CYS GLU ILE ILE
SEQRES 5 A 216 GLY ASN GLY GLY PRO LEU HIS ALA GLU GLY ALA LEU GLU
SEQRES 6 A 216 LEU PHE LEU GLY ASN ALA GLY THR ALA MET ARG PRO LEU
SEQRES 7 A 216 ALA ALA ALA LEU CYS LEU GLY SER ASN ASP ILE VAL LEU
SEQRES 8 A 216 THR GLY GLU PRO ARG MET LYS GLU ARG PRO ILE GLY HIS
SEQRES 9 A 216 LEU VAL ASP ALA LEU ARG LEU GLY GLY ALA LYS ILE THR
SEQRES 10 A 216 TYR LEU GLU GLN GLU ASN TYR PRO PRO LEU ARG LEU GLN
SEQRES 11 A 216 GLY GLY PHE THR GLY GLY ASN VAL ASP VAL ASP GLY SER
SEQRES 12 A 216 VAL SER SER GLN PHE LEU THR ALA LEU LEU MET THR ALA
SEQRES 13 A 216 PRO LEU ALA PRO GLU ASP THR VAL ILE ARG ILE LYS GLY
SEQRES 14 A 216 ASP LEU VAL SER LYS PRO TYR ILE ASP ILE THR LEU ASN
SEQRES 15 A 216 LEU MET LYS THR PHE GLY VAL GLU ILE GLU ASN GLN HIS
SEQRES 16 A 216 TYR GLN GLN PHE VAL VAL LYS GLY GLY GLN SER TYR GLN
SEQRES 17 A 216 SER PRO GLY THR TYR LEU VAL GLU
HELIX 1 1 ASN A 26 LEU A 34 1 9
HELIX 2 2 SER A 47 GLY A 61 1 15
HELIX 3 3 ALA A 95 LEU A 106 1 12
HELIX 4 4 GLU A 118 ARG A 124 5 7
HELIX 5 5 ILE A 126 GLY A 136 1 11
HELIX 6 6 SER A 169 ALA A 180 1 12
HELIX 7 7 SER A 197 THR A 210 1 14
SHEET 1 A 2 ALA A 35 HIS A 36 0
SHEET 2 A 2 TYR A 231 GLN A 232 1 O TYR A 231 N HIS A 36
SHEET 1 B 4 SER A 63 LEU A 66 0
SHEET 2 B 4 CYS A 73 ILE A 76 -1 O GLU A 74 N THR A 65
SHEET 3 B 4 LYS A 38 THR A 42 -1 N LEU A 41 O CYS A 73
SHEET 4 B 4 THR A 236 LEU A 238 1 O TYR A 237 N VAL A 40
SHEET 1 C 4 LEU A 88 PHE A 91 0
SHEET 2 C 4 ILE A 113 THR A 116 1 O THR A 116 N LEU A 90
SHEET 3 C 4 ARG A 152 LEU A 153 -1 O LEU A 153 N ILE A 113
SHEET 4 C 4 ILE A 140 THR A 141 -1 N THR A 141 O ARG A 152
SHEET 1 D 4 VAL A 162 ASP A 165 0
SHEET 2 D 4 THR A 187 LYS A 192 1 O VAL A 188 N VAL A 162
SHEET 3 D 4 PHE A 223 VAL A 225 -1 O VAL A 225 N THR A 187
SHEET 4 D 4 ILE A 215 ASN A 217 -1 N GLU A 216 O VAL A 224
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