Header list of 1f7w.pdb file
Complete list - 23 20 Bytes
HEADER CELL CYCLE 28-JUN-00 1F7W
TITLE SOLUTION STRUCTURE OF C-TERMINAL DOMAIN ZIPA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CELL DIVISION PROTEIN ZIPA;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL DOMAIN, RESIDUES 185-328;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PEG041
KEYWDS ALPHA-BETA FOLD, CELL DIVISION, SEPTATION, TRANSMEMBRANE, CELL CYCLE
EXPDTA SOLUTION NMR
AUTHOR F.J.MOY,E.GLASFELD,L.MOSYAK,R.POWERS
REVDAT 3 23-FEB-22 1F7W 1 REMARK
REVDAT 2 24-FEB-09 1F7W 1 VERSN
REVDAT 1 28-JUN-01 1F7W 0
JRNL AUTH F.J.MOY,E.GLASFELD,L.MOSYAK,R.POWERS
JRNL TITL SOLUTION STRUCTURE OF ZIPA, A CRUCIAL COMPONENT OF
JRNL TITL 2 ESCHERICHIA COLI CELL DIVISION.
JRNL REF BIOCHEMISTRY V. 39 9146 2000
JRNL REFN ISSN 0006-2960
JRNL PMID 10924108
JRNL DOI 10.1021/BI0009690
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH F.J.MOY,E.GLASFELD,R.POWERS
REMARK 1 TITL 1H, 15N, 13C, AND 13CO ASSIGNMENTS AND SECONDARY STRUCTURE
REMARK 1 TITL 2 DETERMINATION OF ZIPA
REMARK 1 REF TO BE PUBLISHED
REMARK 1 REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR V3.840, X-PLOR V3.840
REMARK 3 AUTHORS : BRUNGER (X-PLOR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 2758 RESTRAINTS, 2038 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 377
REMARK 3 DIHEDRAL ANGLE RESTRAINTS, 84 DISTANCE RESTRAINTS FROM HYDROGEN
REMARK 3 BONDS, 113 3JNHA COUPLING RESTRAINTS, 230 SECONDARY CA/CB
REMARK 3 CHEMICAL SHIFT RESTRAINTS, AND A CONFORMATIONAL DATABASE. THE
REMARK 3 COORDINATES IN THIS ENTRY CORROSPOND TO THE REFINED MINIMIZED
REMARK 3 AVERAGE STRUCTURE DETERMINED FROM AN ENSEMBLE OF 30 STRUCTURES
REMARK 4
REMARK 4 1F7W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-JUL-00.
REMARK 100 THE DEPOSITION ID IS D_1000011351.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298; 298; 298
REMARK 210 PH : 5.5; 5.5; 5.5
REMARK 210 IONIC STRENGTH : 50 MM KCL; 50 MM KCL; 50 MM KCL
REMARK 210 PRESSURE : AMBIENT; AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 1 MM ZIPA U-15N,13C; 50MM
REMARK 210 PHOSPHATE BUFFER; 2 MM NAN3; 50
REMARK 210 MM KCL; 90% H2O, 10% D2O; PH 5.5;
REMARK 210 1 MM ZIPA U-15N,13C; 50MM
REMARK 210 PHOSPHATE BUFFER; 2 MM NAN3; 50
REMARK 210 MM KCL; 100% D2O; PH 5.5; 1 MM
REMARK 210 ZIPA U-15N; 50MM PHOSPHATE
REMARK 210 BUFFER; 2 MM NAN3; 50 MM KCL; 90%
REMARK 210 H2O, 10% D2O; PH 5.5
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; HNHA; 2D_15N_
REMARK 210 HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 1.7, PIPP 4.2.8, XWINNMR
REMARK 210 2.0
REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK:
REMARK 210 THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY.
REMARK 210 REFINEMENT PROGRAM: X-PLOR V3.840, AUTHORS: BRUNGER
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 OD2 ASP A 118 HZ1 LYS A 128 1.45
REMARK 500 O ALA A 62 H THR A 83 1.52
REMARK 500 OD1 ASP A 118 H ARG A 122 1.53
REMARK 500 O LYS A 140 H ALA A 144 1.55
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 PRO A 4 69.15 -64.53
REMARK 500 LYS A 5 11.96 -68.93
REMARK 500 ALA A 17 -168.91 -74.69
REMARK 500 PHE A 39 103.83 -59.99
REMARK 500 ASP A 41 -162.68 -64.54
REMARK 500 ASP A 76 73.41 -152.59
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1F7W A 1 144 UNP P77173 ZIPA_ECOLI 185 328
SEQRES 1 A 144 MET ASP LYS PRO LYS ARG LYS GLU ALA VAL ILE ILE MET
SEQRES 2 A 144 ASN VAL ALA ALA HIS HIS GLY SER GLU LEU ASN GLY GLU
SEQRES 3 A 144 LEU LEU LEU ASN SER ILE GLN GLN ALA GLY PHE ILE PHE
SEQRES 4 A 144 GLY ASP MET ASN ILE TYR HIS ARG HIS LEU SER PRO ASP
SEQRES 5 A 144 GLY SER GLY PRO ALA LEU PHE SER LEU ALA ASN MET VAL
SEQRES 6 A 144 LYS PRO GLY THR PHE ASP PRO GLU MET LYS ASP PHE THR
SEQRES 7 A 144 THR PRO GLY VAL THR ILE PHE MET GLN VAL PRO SER TYR
SEQRES 8 A 144 GLY ASP GLU LEU GLN ASN PHE LYS LEU MET LEU GLN SER
SEQRES 9 A 144 ALA GLN HIS ILE ALA ASP GLU VAL GLY GLY VAL VAL LEU
SEQRES 10 A 144 ASP ASP GLN ARG ARG MET MET THR PRO GLN LYS LEU ARG
SEQRES 11 A 144 GLU TYR GLN ASP ILE ILE ARG GLU VAL LYS ASP ALA ASN
SEQRES 12 A 144 ALA
HELIX 1 1 GLY A 25 ALA A 35 1 11
HELIX 2 2 ASP A 93 GLY A 113 1 21
HELIX 3 3 THR A 125 ALA A 144 1 20
SHEET 1 A 6 ILE A 38 GLY A 40 0
SHEET 2 A 6 ILE A 44 HIS A 48 -1 O ILE A 44 N GLY A 40
SHEET 3 A 6 ALA A 57 ASN A 63 -1 N LEU A 58 O ARG A 47
SHEET 4 A 6 GLY A 81 GLN A 87 -1 N THR A 83 O ALA A 62
SHEET 5 A 6 VAL A 10 ALA A 16 -1 O ILE A 11 N MET A 86
SHEET 6 A 6 VAL A 115 LEU A 117 -1 O VAL A 115 N ALA A 16
SHEET 1 B 2 LEU A 23 ASN A 24 0
SHEET 2 B 2 THR A 78 THR A 79 -1 O THR A 79 N LEU A 23
CISPEP 1 LYS A 66 PRO A 67 0 -0.29
CISPEP 2 VAL A 88 PRO A 89 0 0.10
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
Complete list - 23 20 Bytes