Header list of 1pzr.pdb file
Complete list - r 2 2 Bytes
HEADER TRANSFERASE 14-JUL-03 1PZR
TITLE STRUCTURE OF FUSED DOCKING DOMAINS FROM THE ERYTHROMYCIN POLYKETIDE
TITLE 2 SYNTHASE (DEBS), A MODEL FOR THE INTERACTION BETWEEN DEBS2 AND DEBS3:
TITLE 3 THE B DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ERYTHRONOLIDE SYNTHASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 61-120;
COMPND 5 SYNONYM: ORF 2, 6-DEOXYERYTHRONOLIDE B SYNTHASE II, DEBS 2/ORF 3, 6-
COMPND 6 DEOXYERYTHRONOLIDE B SYNTHASE III, DEBS 3;
COMPND 7 EC: 2.3.1.94;
COMPND 8 ENGINEERED: YES;
COMPND 9 OTHER_DETAILS: C-TERMINAL FRAGMENT OF DEBS2 FUSED TO N-TERMINAL
COMPND 10 FRAGMENT OF DEBS3
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROPOLYSPORA ERYTHRAEA;
SOURCE 3 ORGANISM_TAXID: 1836;
SOURCE 4 GENE: ERYA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21-CODONPLUS;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX4T-3
KEYWDS FOUR HELIX BUNDLE, HOMODIMER, TRANSFERASE
EXPDTA SOLUTION NMR
NUMMDL 7
AUTHOR R.W.BROADHURST,D.NIETLISPACH,M.P.WHEATCROFT,P.F.LEADLAY,K.J.WEISSMAN
REVDAT 3 02-MAR-22 1PZR 1 REMARK
REVDAT 2 24-FEB-09 1PZR 1 VERSN
REVDAT 1 24-FEB-04 1PZR 0
JRNL AUTH R.W.BROADHURST,D.NIETLISPACH,M.P.WHEATCROFT,P.F.LEADLAY,
JRNL AUTH 2 K.J.WEISSMAN
JRNL TITL THE STRUCTURE OF DOCKING DOMAINS IN MODULAR POLYKETIDE
JRNL TITL 2 SYNTHASES.
JRNL REF CHEM.BIOL. V. 10 723 2003
JRNL REFN ISSN 1074-5521
JRNL PMID 12954331
JRNL DOI 10.1016/S1074-5521(03)00156-X
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : AZARA 1.0, CNS 1.0
REMARK 3 AUTHORS : BOUCHER (AZARA), BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 1754 RESTRAINTS: 1618 NOE-DERIVED DISTANCE RESTRAINTS, 78
REMARK 3 DIHEDRAL ANGLE RESTRAINTS, 58 DISTANCE RESTRAINTS FROM HYDROGEN
REMARK 3 BONDS.
REMARK 4
REMARK 4 1PZR COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-JUL-03.
REMARK 100 THE DEPOSITION ID IS D_1000019735.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 100MM PHOSPHATE BUFFER NA
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM DOCK23 U-15N,13C: 100MM
REMARK 210 PHOSPHATE BUFFER NA: TRACE
REMARK 210 AMOUNTS OF SODIUM AZIDE, AEBSF
REMARK 210 PROTEASE INHIBITOR COCKTAIL AND
REMARK 210 TSP 1H SHIFT REFERENCE: 90% H2O,
REMARK 210 10% D2O; 1MM DOCK23 (50% U-15N,
REMARK 210 13C: 50% UNLABELED): 100MM
REMARK 210 PHOSPHATE BUFFER NA: TRACE
REMARK 210 AMOUNTS OF SODIUM AZIDE, AEBSF
REMARK 210 PROTEASE INHIBITOR COCKTAIL AND
REMARK 210 TSP 1H SHIFT REFERENCE: 90% H2O,
REMARK 210 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 3D_13C_15N_X-FILTERED_13C-SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : ANSIG 3.3, CNS 1.0
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 7
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY. INTERMOLECULAR CONTACTS WERE OBTAINED FROM AN X-
REMARK 210 FILTERED NOESY EXPERIMENT ON A MIXED-LABELED SAMPLE.
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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
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 GLU A 78 -151.80 -170.62
REMARK 500 1 ASP A 79 -49.77 -152.11
REMARK 500 1 SER A 83 -153.13 56.84
REMARK 500 1 ASP A 85 49.66 -169.99
REMARK 500 1 MET A 88 -152.98 -153.69
REMARK 500 1 HIS A 116 -77.15 -67.85
REMARK 500 1 ALA A 118 -139.07 60.51
REMARK 500 1 GLU B 78 -151.99 -169.38
REMARK 500 1 ASP B 79 -47.42 -149.41
REMARK 500 1 SER B 83 -147.92 58.06
REMARK 500 1 ASP B 85 42.98 -171.11
REMARK 500 1 MET B 88 -149.51 -153.06
REMARK 500 1 ALA B 118 -142.22 62.56
REMARK 500 2 GLU A 78 -72.31 66.70
REMARK 500 2 LEU A 81 -139.15 -70.80
REMARK 500 2 MET A 82 -41.25 -175.49
REMARK 500 2 ASP A 85 53.10 -168.70
REMARK 500 2 GLU A 115 -113.36 -71.15
REMARK 500 2 HIS A 116 93.32 52.54
REMARK 500 2 GLU B 78 -60.35 70.67
REMARK 500 2 LEU B 81 -139.88 -69.89
REMARK 500 2 MET B 82 -42.22 -173.75
REMARK 500 2 ASP B 85 49.84 -170.52
REMARK 500 2 GLU B 115 -120.57 -74.19
REMARK 500 2 HIS B 116 103.64 59.63
REMARK 500 3 GLU A 78 158.12 56.48
REMARK 500 3 ASP A 79 -65.78 175.20
REMARK 500 3 MET A 82 -50.65 -164.46
REMARK 500 3 SER A 83 142.69 65.82
REMARK 500 3 ASP A 85 53.36 -150.20
REMARK 500 3 SER A 106 -60.68 -90.33
REMARK 500 3 GLU A 115 -107.31 -67.55
REMARK 500 3 ARG A 117 -27.17 177.20
REMARK 500 3 ALA A 118 -135.61 59.67
REMARK 500 3 GLU B 78 140.86 62.77
REMARK 500 3 ASP B 79 -52.95 -171.58
REMARK 500 3 MET B 82 -47.31 -170.13
REMARK 500 3 SER B 83 143.93 62.62
REMARK 500 3 GLU B 115 -118.90 -75.18
REMARK 500 3 ARG B 117 -32.79 177.14
REMARK 500 3 ALA B 118 -139.45 61.40
REMARK 500 4 ASP A 79 -68.19 174.08
REMARK 500 4 LEU A 80 140.93 64.83
REMARK 500 4 MET A 82 -45.01 75.38
REMARK 500 4 ASP A 85 46.12 -172.90
REMARK 500 4 ASN A 86 -153.44 -149.18
REMARK 500 4 MET A 88 -150.70 -152.66
REMARK 500 4 HIS A 116 -86.34 -59.43
REMARK 500 4 ASP B 79 -57.05 -172.31
REMARK 500 4 LEU B 80 136.25 60.53
REMARK 500
REMARK 500 THIS ENTRY HAS 100 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1PZQ RELATED DB: PDB
REMARK 900 STRUCTURE OF FUSED DOCKING DOMAINS FROM THE ERYTHROMYCIN POLYKETIDE
REMARK 900 SYNTHASE (DEBS), A MODEL FOR THE INTERACTION BETWEEN DEBS 2 AND
REMARK 900 DEBS 3: THE A DOMAIN
REMARK 999
REMARK 999 SEQUENCE LEU 81 AND MET 82 FORM A LINKER BETWEEN THE C-TERMINAL
REMARK 999 FRAGMENT OF DEBS2 AND THE N-TERMINAL FRAGMENT OF DEBS3
DBREF 1PZR A 61 80 UNP Q03132 ERY2_SACER 3548 3567
DBREF 1PZR A 83 120 UNP Q03133 ERY3_SACER 2 39
DBREF 1PZR B 61 80 UNP Q03132 ERY2_SACER 3548 3567
DBREF 1PZR B 83 120 UNP Q03133 ERY3_SACER 2 39
SEQADV 1PZR LEU A 81 Q03132 SEE REMARK 999
SEQADV 1PZR MET A 82 Q03132 SEE REMARK 999
SEQADV 1PZR LEU B 81 Q03132 SEE REMARK 999
SEQADV 1PZR MET B 82 Q03132 SEE REMARK 999
SEQRES 1 A 60 ALA SER ASP ASP GLU LEU PHE SER MET LEU ASP GLN ARG
SEQRES 2 A 60 PHE GLY GLY GLY GLU ASP LEU LEU MET SER GLY ASP ASN
SEQRES 3 A 60 GLY MET THR GLU GLU LYS LEU ARG ARG TYR LEU LYS ARG
SEQRES 4 A 60 THR VAL THR GLU LEU ASP SER VAL THR ALA ARG LEU ARG
SEQRES 5 A 60 GLU VAL GLU HIS ARG ALA GLY GLU
SEQRES 1 B 60 ALA SER ASP ASP GLU LEU PHE SER MET LEU ASP GLN ARG
SEQRES 2 B 60 PHE GLY GLY GLY GLU ASP LEU LEU MET SER GLY ASP ASN
SEQRES 3 B 60 GLY MET THR GLU GLU LYS LEU ARG ARG TYR LEU LYS ARG
SEQRES 4 B 60 THR VAL THR GLU LEU ASP SER VAL THR ALA ARG LEU ARG
SEQRES 5 B 60 GLU VAL GLU HIS ARG ALA GLY GLU
HELIX 1 1 SER A 62 GLY A 76 1 15
HELIX 2 2 MET A 88 ALA A 118 1 31
HELIX 3 3 SER B 62 GLY B 76 1 15
HELIX 4 4 MET B 88 ALA B 118 1 31
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