Header list of 1pzq.pdb file
Complete list - r 2 2 Bytes
HEADER TRANSFERASE 14-JUL-03 1PZQ
TITLE STRUCTURE OF FUSED DOCKING DOMAINS FROM THE ERYTHROMYCIN POLYKETIDE
TITLE 2 SYNTHASE (DEBS), A MODEL FOR THE INTERACTION BETWEEN DEBS 2 AND DEBS
TITLE 3 3: THE A DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ERYTHRONOLIDE SYNTHASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: C-TERMINAL FRAGMENT;
COMPND 5 SYNONYM: ORF 2, 6-DEOXYERYTHRONOLIDE B SYNTHASE II, DEBS 2;
COMPND 6 EC: 2.3.1.94;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
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 8
AUTHOR R.W.BROADHURST,D.NIETLISPACH,M.P.WHEATCROFT,P.F.LEADLAY,K.J.WEISSMAN
REVDAT 3 02-MAR-22 1PZQ 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1PZQ 1 VERSN
REVDAT 1 24-FEB-04 1PZQ 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 : ANSIG 3.3, CNS 1.0
REMARK 3 AUTHORS : KRAULIS (ANSIG), BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 1811 RESTRAINTS: 1709 NOE-
REMARK 3 DERIVED
REMARK 3 DISTANCE CONSTRAINTS, 60 DIHEDRAL ANGLE RESTRAINTS, 42 DISTANCE
REMARK 3 RESTRAINTS
REMARK 3 FROM HYDROGEN BONDS.
REMARK 4
REMARK 4 1PZQ 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_1000019734.
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 : CNS 1.0
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 40
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 8
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 O ASP A 9 H GLY A 11 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 ALA A 4 -139.57 -172.99
REMARK 500 1 SER A 5 128.19 64.50
REMARK 500 1 PRO A 6 -167.39 -71.38
REMARK 500 1 ILE A 10 -50.28 55.40
REMARK 500 1 SER A 25 84.18 -47.21
REMARK 500 1 ASP A 28 52.21 -162.30
REMARK 500 1 HIS A 30 44.60 -75.45
REMARK 500 1 ASP A 50 84.19 -67.25
REMARK 500 1 THR A 54 -41.15 -165.60
REMARK 500 1 SER A 55 -49.42 -163.10
REMARK 500 1 ALA B 4 -139.78 -174.01
REMARK 500 1 SER B 5 127.02 63.59
REMARK 500 1 PRO B 6 -159.01 -68.70
REMARK 500 1 ASP B 9 -12.87 76.94
REMARK 500 1 ILE B 10 -40.82 69.58
REMARK 500 1 SER B 25 86.60 -54.75
REMARK 500 1 ASP B 28 60.83 -159.09
REMARK 500 1 HIS B 30 37.65 -74.46
REMARK 500 1 ASP B 50 93.47 -62.16
REMARK 500 1 ALA B 51 134.16 -172.32
REMARK 500 1 THR B 54 -41.27 -164.87
REMARK 500 1 SER B 55 -49.54 -162.90
REMARK 500 2 SER A 2 43.94 -79.05
REMARK 500 2 SER A 5 57.35 -174.80
REMARK 500 2 ILE A 10 -59.61 45.93
REMARK 500 2 SER A 25 84.06 -46.54
REMARK 500 2 ASP A 28 52.08 -162.60
REMARK 500 2 HIS A 30 44.96 -75.18
REMARK 500 2 ALA A 51 132.76 -177.68
REMARK 500 2 SER A 53 -140.24 -177.13
REMARK 500 2 THR A 54 136.32 -175.55
REMARK 500 2 ALA A 56 -138.28 -176.35
REMARK 500 2 ILE A 57 136.27 -174.14
REMARK 500 2 SER A 58 -44.92 -173.39
REMARK 500 2 GLU A 59 135.79 -172.45
REMARK 500 2 SER B 2 43.10 -78.89
REMARK 500 2 SER B 5 53.85 -171.14
REMARK 500 2 ASP B 9 -0.88 69.19
REMARK 500 2 ILE B 10 -58.36 60.95
REMARK 500 2 SER B 25 86.47 -53.10
REMARK 500 2 ASP B 28 60.30 -162.49
REMARK 500 2 HIS B 30 41.07 -75.40
REMARK 500 2 ALA B 51 130.74 -179.40
REMARK 500 2 SER B 53 -140.31 -176.48
REMARK 500 2 THR B 54 136.81 -175.40
REMARK 500 2 ALA B 56 -138.84 -176.60
REMARK 500 2 ILE B 57 136.59 -175.54
REMARK 500 2 SER B 58 -43.16 -172.92
REMARK 500 2 GLU B 59 136.90 -172.36
REMARK 500 3 SER A 2 134.96 64.56
REMARK 500
REMARK 500 THIS ENTRY HAS 199 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1PZR 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 B DOMAIN
DBREF 1PZQ A 3 60 UNP Q03132 ERYA2_SACER 3490 3547
DBREF 1PZQ B 3 60 UNP Q03132 ERYA2_SACER 3490 3547
SEQADV 1PZQ GLY A 1 UNP Q03132 CLONING ARTIFACT
SEQADV 1PZQ SER A 2 UNP Q03132 CLONING ARTIFACT
SEQADV 1PZQ GLY B 1 UNP Q03132 CLONING ARTIFACT
SEQADV 1PZQ SER B 2 UNP Q03132 CLONING ARTIFACT
SEQRES 1 A 60 GLY SER ALA ALA SER PRO ALA VAL ASP ILE GLY ASP ARG
SEQRES 2 A 60 LEU ASP GLU LEU GLU LYS ALA LEU GLU ALA LEU SER ALA
SEQRES 3 A 60 GLU ASP GLY HIS ASP ASP VAL GLY GLN ARG LEU GLU SER
SEQRES 4 A 60 LEU LEU ARG ARG TRP ASN SER ARG ARG ALA ASP ALA PRO
SEQRES 5 A 60 SER THR SER ALA ILE SER GLU ASP
SEQRES 1 B 60 GLY SER ALA ALA SER PRO ALA VAL ASP ILE GLY ASP ARG
SEQRES 2 B 60 LEU ASP GLU LEU GLU LYS ALA LEU GLU ALA LEU SER ALA
SEQRES 3 B 60 GLU ASP GLY HIS ASP ASP VAL GLY GLN ARG LEU GLU SER
SEQRES 4 B 60 LEU LEU ARG ARG TRP ASN SER ARG ARG ALA ASP ALA PRO
SEQRES 5 B 60 SER THR SER ALA ILE SER GLU ASP
HELIX 1 1 ILE A 10 SER A 25 1 16
HELIX 2 2 HIS A 30 ASP A 50 1 21
HELIX 3 3 ILE B 10 SER B 25 1 16
HELIX 4 4 HIS B 30 ASP B 50 1 21
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