Header list of 1f7x.pdb file
Complete list - b 23 2 Bytes
HEADER CELL CYCLE 28-JUN-00 1F7X
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;
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, INNER
KEYWDS 2 MEMBRANE, CELL CYCLE
EXPDTA SOLUTION NMR
NUMMDL 30
MDLTYP MINIMIZED AVERAGE
AUTHOR F.J.MOY,E.GLASFELD,L.MOSYAK,R.POWERS
REVDAT 3 23-FEB-22 1F7X 1 JRNL REMARK
REVDAT 2 24-FEB-09 1F7X 1 VERSN
REVDAT 1 28-JUN-01 1F7X 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 LETTER TO THE EDITOR: 1H, 15N, 13C, AND 13CO ASSIGNMENTS AND
REMARK 1 TITL 2 SECONDARY STRUCTURE DETERMINATION OF ZIPA.
REMARK 1 REF J. BIOMOL. NMR V. 17 275 2000
REMARK 1 REFN ISSN 0925-2738
REMARK 1 PMID 10959637
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.
REMARK 4
REMARK 4 1F7X COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-JUL-00.
REMARK 100 THE DEPOSITION ID IS D_1000011352.
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; 50; 50
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 : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY,STRUCTURES
REMARK 210 WITH FAVORABLE NON-BOND ENERGY,
REMARK 210 STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS,STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1F7W
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY.
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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (RES=RESIDUE NAME;
REMARK 470 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 470 MODELS 1-30
REMARK 470 RES CSSEQI ATOMS
REMARK 470 ALA A 144 O
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 OD1 ASP A 118 H ARG A 122 1.45
REMARK 500 HD1 HIS A 48 O GLY A 55 1.49
REMARK 500 O ALA A 62 H THR A 83 1.53
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 LYS A 5 32.28 -78.77
REMARK 500 1 ALA A 17 -165.46 -71.91
REMARK 500 1 ASP A 41 -163.97 -61.79
REMARK 500 1 PRO A 72 -13.96 -46.08
REMARK 500 1 ASP A 76 69.34 -152.15
REMARK 500 2 PRO A 4 158.24 -35.71
REMARK 500 2 ALA A 17 -165.80 -71.02
REMARK 500 2 PHE A 39 102.99 -59.98
REMARK 500 2 ASP A 41 -162.97 -60.53
REMARK 500 2 PRO A 72 -11.28 -47.56
REMARK 500 2 ASP A 76 74.78 -151.23
REMARK 500 3 ALA A 9 -163.80 -165.70
REMARK 500 3 ASP A 41 -163.19 -63.78
REMARK 500 3 MET A 42 19.81 57.19
REMARK 500 4 LYS A 5 31.04 -80.00
REMARK 500 4 ASP A 41 -163.78 -64.31
REMARK 500 4 PRO A 56 -176.68 -69.61
REMARK 500 4 PRO A 72 -12.64 -45.19
REMARK 500 4 ASP A 76 75.66 -150.16
REMARK 500 5 ASP A 2 42.24 -91.66
REMARK 500 5 PRO A 4 37.60 -65.70
REMARK 500 5 ALA A 17 -166.30 -72.11
REMARK 500 5 ASP A 41 -161.96 -60.76
REMARK 500 5 PRO A 72 -6.45 -50.68
REMARK 500 5 ASP A 76 79.35 -150.76
REMARK 500 6 LYS A 5 33.03 -80.89
REMARK 500 6 ASP A 41 -165.69 -65.45
REMARK 500 6 PRO A 72 -8.88 -46.66
REMARK 500 6 ASP A 76 78.01 -150.10
REMARK 500 7 ALA A 9 -166.66 -162.30
REMARK 500 7 ALA A 17 -169.91 -71.82
REMARK 500 7 PHE A 39 107.41 -58.62
REMARK 500 7 ASP A 41 -166.37 -66.43
REMARK 500 8 ASP A 41 -163.35 -65.56
REMARK 500 8 MET A 42 19.96 58.70
REMARK 500 8 PRO A 72 -14.37 -44.05
REMARK 500 8 ASP A 76 78.31 -150.03
REMARK 500 9 ASP A 41 -164.45 -62.59
REMARK 500 9 PRO A 72 -15.53 -42.89
REMARK 500 10 ALA A 9 -166.22 -168.17
REMARK 500 10 ASP A 41 -161.97 -65.36
REMARK 500 10 MET A 42 -99.71 58.18
REMARK 500 10 ASN A 43 28.47 -164.81
REMARK 500 10 PRO A 72 -13.37 -49.86
REMARK 500 11 PRO A 4 -145.05 -56.91
REMARK 500 11 LYS A 5 36.46 -76.34
REMARK 500 11 ASP A 41 -169.84 -69.34
REMARK 500 11 PRO A 72 -8.17 -48.98
REMARK 500 11 ASP A 76 77.80 -154.80
REMARK 500 12 PRO A 4 9.70 -67.69
REMARK 500
REMARK 500 THIS ENTRY HAS 136 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1F7W RELATED DB: PDB
REMARK 900 1F7W IS THE RESTRAINED MINIMIZED AVERAGE STRUCTURE OF ZIPA FOR THIS
REMARK 900 ENSEMBLE.
DBREF 1F7X 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 71 ASP A 76 5 6
HELIX 3 3 ASP A 93 GLY A 113 1 21
HELIX 4 4 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 N ILE A 11 O 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 1 -0.08
CISPEP 2 VAL A 88 PRO A 89 1 -1.15
CISPEP 3 LYS A 66 PRO A 67 2 -1.24
CISPEP 4 VAL A 88 PRO A 89 2 0.61
CISPEP 5 LYS A 66 PRO A 67 3 -0.28
CISPEP 6 VAL A 88 PRO A 89 3 0.06
CISPEP 7 LYS A 66 PRO A 67 4 -0.02
CISPEP 8 VAL A 88 PRO A 89 4 0.28
CISPEP 9 LYS A 66 PRO A 67 5 -0.73
CISPEP 10 VAL A 88 PRO A 89 5 -1.17
CISPEP 11 LYS A 66 PRO A 67 6 -0.43
CISPEP 12 VAL A 88 PRO A 89 6 0.37
CISPEP 13 LYS A 66 PRO A 67 7 -0.48
CISPEP 14 VAL A 88 PRO A 89 7 0.19
CISPEP 15 LYS A 66 PRO A 67 8 -0.48
CISPEP 16 VAL A 88 PRO A 89 8 0.01
CISPEP 17 LYS A 66 PRO A 67 9 -0.59
CISPEP 18 VAL A 88 PRO A 89 9 -0.93
CISPEP 19 LYS A 66 PRO A 67 10 -0.29
CISPEP 20 VAL A 88 PRO A 89 10 -0.44
CISPEP 21 LYS A 66 PRO A 67 11 -0.73
CISPEP 22 VAL A 88 PRO A 89 11 -1.38
CISPEP 23 LYS A 66 PRO A 67 12 -0.25
CISPEP 24 VAL A 88 PRO A 89 12 -1.60
CISPEP 25 LYS A 66 PRO A 67 13 -0.08
CISPEP 26 VAL A 88 PRO A 89 13 0.14
CISPEP 27 LYS A 66 PRO A 67 14 -0.77
CISPEP 28 VAL A 88 PRO A 89 14 0.48
CISPEP 29 LYS A 66 PRO A 67 15 0.34
CISPEP 30 VAL A 88 PRO A 89 15 -0.07
CISPEP 31 LYS A 66 PRO A 67 16 -1.22
CISPEP 32 VAL A 88 PRO A 89 16 0.27
CISPEP 33 LYS A 66 PRO A 67 17 -0.97
CISPEP 34 VAL A 88 PRO A 89 17 -0.35
CISPEP 35 LYS A 66 PRO A 67 18 -0.71
CISPEP 36 VAL A 88 PRO A 89 18 0.11
CISPEP 37 LYS A 66 PRO A 67 19 -1.07
CISPEP 38 VAL A 88 PRO A 89 19 -0.46
CISPEP 39 LYS A 66 PRO A 67 20 -0.12
CISPEP 40 VAL A 88 PRO A 89 20 0.00
CISPEP 41 LYS A 66 PRO A 67 21 -0.83
CISPEP 42 VAL A 88 PRO A 89 21 -0.33
CISPEP 43 LYS A 66 PRO A 67 22 -0.59
CISPEP 44 VAL A 88 PRO A 89 22 0.16
CISPEP 45 LYS A 66 PRO A 67 23 -0.57
CISPEP 46 VAL A 88 PRO A 89 23 -0.07
CISPEP 47 LYS A 66 PRO A 67 24 0.18
CISPEP 48 VAL A 88 PRO A 89 24 -0.43
CISPEP 49 LYS A 66 PRO A 67 25 -0.69
CISPEP 50 VAL A 88 PRO A 89 25 0.27
CISPEP 51 LYS A 66 PRO A 67 26 -0.45
CISPEP 52 VAL A 88 PRO A 89 26 -2.06
CISPEP 53 LYS A 66 PRO A 67 27 0.10
CISPEP 54 VAL A 88 PRO A 89 27 -0.66
CISPEP 55 LYS A 66 PRO A 67 28 0.22
CISPEP 56 VAL A 88 PRO A 89 28 -0.27
CISPEP 57 LYS A 66 PRO A 67 29 -0.84
CISPEP 58 VAL A 88 PRO A 89 29 -0.18
CISPEP 59 LYS A 66 PRO A 67 30 -0.19
CISPEP 60 VAL A 88 PRO A 89 30 0.25
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