Header list of 4ull.pdb file
Complete list - 11 20 Bytes
HEADER TOXIN 17-DEC-96 4ULL
TITLE SOLUTION NMR STRUCTURE OF VEROTOXIN-1 B-SUBUNIT FROM E. COLI, 5
TITLE 2 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SHIGA TOXIN 1B;
COMPND 3 CHAIN: A
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562
KEYWDS TOXIN
EXPDTA SOLUTION NMR
NUMMDL 5
AUTHOR J.M.RICHARDSON,P.D.EVANS,S.W.HOMANS,A.DONOHUE-ROLFE
REVDAT 3 11-DEC-19 4ULL 1 COMPND SOURCE REMARK DBREF
REVDAT 2 24-FEB-09 4ULL 1 VERSN
REVDAT 1 01-APR-97 4ULL 0
JRNL AUTH J.M.RICHARDSON,P.D.EVANS,S.W.HOMANS,A.DONOHUE-ROLFE
JRNL TITL SOLUTION STRUCTURE OF THE CARBOHYDRATE-BINDING B-SUBUNIT
JRNL TITL 2 HOMOPENTAMER OF VEROTOXIN VT-1 FROM E. COLI.
JRNL REF NAT.STRUCT.BIOL. V. 4 190 1997
JRNL REFN ISSN 1072-8368
JRNL PMID 9164458
JRNL DOI 10.1038/NSB0397-190
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4ULL COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000179445.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 318
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : ASSIGNMENT HNCO; HCACO; HNCOCA;
REMARK 210 3D TOCSY. 1H-1H DISTANCE
REMARK 210 DERIVATION; 3D-NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500.3 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XPLOR 3.1
REMARK 210 METHOD USED : SIMULATED ANNEALING/ MOLECULAR
REMARK 210 DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 40
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 5
REMARK 210 CONFORMERS, SELECTION CRITERIA : NO RESTRAINT VIOLATIONS ABOVE
REMARK 210 0.7 ANGSTROM
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED BY TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY ON UNIFORMLY 13C, 15N-LABELED VEROTOXIN-1. IONIC_
REMARK 210 STRENGTH: 200 MM PRESSURE: ATMOSPHERIC SOLVENT SYSTEM: H20
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 HZ3 LYS A 13 OG1 THR A 21 1.30
REMARK 500 OG1 THR A 6 HZ1 LYS A 8 1.31
REMARK 500 HZ2 LYS A 13 OD1 ASN A 15 1.36
REMARK 500 O ASP A 26 HZ1 LYS A 27 1.37
REMARK 500 HZ3 LYS A 53 OE1 GLU A 65 1.41
REMARK 500 OD1 ASP A 3 HZ1 LYS A 53 1.42
REMARK 500 O SER A 38 HG SER A 42 1.43
REMARK 500 O GLU A 10 HZ3 LYS A 23 1.44
REMARK 500 O LYS A 53 HG1 THR A 54 1.45
REMARK 500 HZ2 LYS A 8 O GLY A 25 1.46
REMARK 500 O ALA A 43 H GLY A 47 1.47
REMARK 500 O SER A 42 HG1 THR A 46 1.52
REMARK 500 HG1 THR A 6 OD2 ASP A 26 1.52
REMARK 500 HE ARG A 33 OG SER A 64 1.52
REMARK 500 HG1 THR A 1 OD2 ASP A 3 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 ASP A 3 -146.98 -88.02
REMARK 500 1 CYS A 4 -86.86 -171.42
REMARK 500 1 LYS A 8 -146.30 -72.69
REMARK 500 1 VAL A 9 66.71 -158.04
REMARK 500 1 GLU A 10 59.13 -101.29
REMARK 500 1 TYR A 11 103.80 124.05
REMARK 500 1 ASN A 15 -40.70 -165.85
REMARK 500 1 ASP A 17 -41.41 171.54
REMARK 500 1 ASP A 18 -36.64 -145.70
REMARK 500 1 THR A 19 -78.18 -48.93
REMARK 500 1 PHE A 20 176.28 69.74
REMARK 500 1 LYS A 23 72.04 -109.13
REMARK 500 1 ARG A 33 -55.15 -161.69
REMARK 500 1 TRP A 34 -26.65 178.28
REMARK 500 1 ASN A 35 69.16 179.53
REMARK 500 1 MET A 48 60.37 142.20
REMARK 500 1 THR A 49 67.55 -176.90
REMARK 500 1 VAL A 50 -151.15 -77.52
REMARK 500 1 THR A 54 161.74 67.76
REMARK 500 1 ALA A 56 -57.08 75.07
REMARK 500 1 ASN A 59 81.94 58.03
REMARK 500 1 PHE A 63 -82.75 -98.07
REMARK 500 2 ASP A 3 -146.97 -88.47
REMARK 500 2 CYS A 4 -86.45 -171.63
REMARK 500 2 LYS A 8 -145.67 -72.83
REMARK 500 2 VAL A 9 67.08 -158.23
REMARK 500 2 GLU A 10 58.12 -101.48
REMARK 500 2 TYR A 11 103.98 125.27
REMARK 500 2 ASN A 15 -40.22 -166.62
REMARK 500 2 ASP A 17 -41.04 171.22
REMARK 500 2 ASP A 18 -37.04 -145.96
REMARK 500 2 THR A 19 -78.29 -48.48
REMARK 500 2 PHE A 20 176.39 69.77
REMARK 500 2 LYS A 23 72.91 -108.42
REMARK 500 2 ARG A 33 -55.29 -161.79
REMARK 500 2 TRP A 34 -25.86 178.09
REMARK 500 2 ASN A 35 68.34 178.58
REMARK 500 2 MET A 48 60.24 141.93
REMARK 500 2 THR A 49 67.01 -177.00
REMARK 500 2 VAL A 50 -151.93 -77.57
REMARK 500 2 THR A 54 161.74 67.70
REMARK 500 2 ALA A 56 -56.92 75.16
REMARK 500 2 ASN A 59 81.81 58.13
REMARK 500 2 PHE A 63 -82.02 -97.94
REMARK 500 3 ASP A 3 -147.66 -88.10
REMARK 500 3 CYS A 4 -86.64 -170.77
REMARK 500 3 LYS A 8 -145.92 -72.84
REMARK 500 3 VAL A 9 67.19 -158.17
REMARK 500 3 GLU A 10 58.55 -101.21
REMARK 500 3 TYR A 11 103.36 124.88
REMARK 500
REMARK 500 THIS ENTRY HAS 110 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 1 ARG A 69 0.25 SIDE CHAIN
REMARK 500 2 ARG A 69 0.25 SIDE CHAIN
REMARK 500 3 ARG A 69 0.25 SIDE CHAIN
REMARK 500 4 ARG A 69 0.25 SIDE CHAIN
REMARK 500 5 ARG A 69 0.25 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 4ULL A 1 69 UNP Q8G8Y6 Q8G8Y6_ECOLX 17 85
SEQRES 1 A 69 THR PRO ASP CYS VAL THR GLY LYS VAL GLU TYR THR LYS
SEQRES 2 A 69 TYR ASN ASP ASP ASP THR PHE THR VAL LYS VAL GLY ASP
SEQRES 3 A 69 LYS GLU LEU PHE THR ASN ARG TRP ASN LEU GLN SER LEU
SEQRES 4 A 69 LEU LEU SER ALA GLN ILE THR GLY MET THR VAL THR ILE
SEQRES 5 A 69 LYS THR ASN ALA CYS HIS ASN GLY GLY GLY PHE SER GLU
SEQRES 6 A 69 VAL ILE PHE ARG
HELIX 1 1 LEU A 36 THR A 46 1 11
SHEET 1 A 3 VAL A 5 GLY A 7 0
SHEET 2 A 3 VAL A 50 LYS A 53 -1 N ILE A 52 O VAL A 5
SHEET 3 A 3 GLU A 65 ILE A 67 -1 N ILE A 67 O THR A 51
SHEET 1 B 2 THR A 21 VAL A 24 0
SHEET 2 B 2 LYS A 27 PHE A 30 -1 N LEU A 29 O VAL A 22
SSBOND 1 CYS A 4 CYS A 57 1555 1555 2.02
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 - 11 20 Bytes