Header list of 1hzl.pdb file
Complete list - g 9 2 Bytes
HEADER ANTIBIOTIC 25-JAN-01 1HZL
TITLE SOLUTION STRUCTURES OF C-1027 APOPROTEIN AND ITS COMPLEX WITH THE
TITLE 2 AROMATIZED CHROMOPHORE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: C-1027 APOPROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ANTITUMOR ANTIBIOTIC C-1027 APOPROTEIN
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES GLOBISPORUS;
SOURCE 3 ORGANISM_TAXID: 1908;
SOURCE 4 STRAIN: C-1027
KEYWDS CHROMOPROTEIN, C-1027, APOPROTEIN, AROMATIZED CHROMOPHORE, ANTIBIOTIC
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR T.TANAKA,S.FUKUDA-ISHISAKA,M.HIRAMA,T.OTANI
REVDAT 4 14-JUN-23 1HZL 1 REMARK SSBOND
REVDAT 3 05-FEB-20 1HZL 1 REMARK ATOM
REVDAT 2 24-FEB-09 1HZL 1 VERSN
REVDAT 1 23-MAY-01 1HZL 0
JRNL AUTH T.TANAKA,S.FUKUDA-ISHISAKA,M.HIRAMA,T.OTANI
JRNL TITL SOLUTION STRUCTURES OF C-1027 APOPROTEIN AND ITS COMPLEX
JRNL TITL 2 WITH THE AROMATIZED CHROMOPHORE.
JRNL REF J.MOL.BIOL. V. 309 267 2001
JRNL REFN ISSN 0022-2836
JRNL PMID 11491295
JRNL DOI 10.1006/JMBI.2001.4621
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1, X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER, A.T. (X-PLOR), BRUNGER, A.T. (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 1539 RESTRAINTS: 1378 NOE-DERIVED DISTANCE RESTRAINTS, 95
REMARK 3 DIHEDRAL ANGLE RESTRAINTS, 60 DISTANCE RESTRAINTS FROM HYDROGEN
REMARK 3 BONDS, AND 6 DISTANCE RESTRAINTS FROM DISULFIDE BONDS.
REMARK 4
REMARK 4 1HZL COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-JAN-01.
REMARK 100 THE DEPOSITION ID IS D_1000012720.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 5.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : SAMPLE 1: 8.3-8.6MM C-1027
REMARK 210 APOPROTEIN COMPLEXED WITH THE
REMARK 210 AROMATIZED CHROMOPHORE; 99.996%
REMARK 210 D2O; SAMPLE 2: 8.3-8.6MM C-1027
REMARK 210 APOPROTEIN COMPLEXED WITH THE
REMARK 210 AROMATIZED CHROMOPHORE; 90% H2O,
REMARK 210 10% D2O; 8.3-8.6MM C-1027
REMARK 210 APOPROTEIN COMPLEXED WITH THE
REMARK 210 AROMATIZED CHROMOPHORE; 90% H2O,
REMARK 210 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; COSY; HOHAHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AM
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
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: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR TECHNIQUES.
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: 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 PHE A 4 113.80 -162.53
REMARK 500 1 SER A 7 -85.23 -56.26
REMARK 500 1 ALA A 9 25.06 -168.31
REMARK 500 1 LEU A 12 -160.01 -79.67
REMARK 500 1 ALA A 25 -142.83 -73.16
REMARK 500 1 ALA A 37 119.56 -171.06
REMARK 500 1 GLN A 42 -161.14 -119.56
REMARK 500 1 ALA A 50 78.35 -112.09
REMARK 500 1 ASP A 56 -164.31 -102.31
REMARK 500 1 SER A 62 120.27 -175.30
REMARK 500 1 TYR A 71 139.35 -171.40
REMARK 500 1 SER A 74 113.24 177.37
REMARK 500 1 THR A 88 13.63 -145.30
REMARK 500 1 ASN A 97 -156.86 -138.12
REMARK 500 1 LEU A 102 -92.75 -77.20
REMARK 500 1 THR A 108 103.43 -161.81
REMARK 500 2 PRO A 2 -167.32 -73.32
REMARK 500 2 SER A 7 -78.08 -59.81
REMARK 500 2 ALA A 9 20.65 -161.92
REMARK 500 2 LEU A 12 -155.84 -68.99
REMARK 500 2 SER A 21 118.87 -160.09
REMARK 500 2 ALA A 25 -154.37 -65.36
REMARK 500 2 ALA A 37 130.28 -175.12
REMARK 500 2 GLN A 42 -166.18 -113.54
REMARK 500 2 ALA A 50 99.15 -163.52
REMARK 500 2 TYR A 71 138.30 -178.46
REMARK 500 2 SER A 74 -155.43 -161.66
REMARK 500 2 VAL A 81 -47.71 -131.79
REMARK 500 2 THR A 88 -30.72 177.96
REMARK 500 2 ALA A 89 175.03 -59.52
REMARK 500 2 LEU A 100 128.18 -38.05
REMARK 500 2 LEU A 102 -89.85 -121.02
REMARK 500 3 SER A 7 -72.90 -66.65
REMARK 500 3 ALA A 9 31.51 -179.37
REMARK 500 3 GLN A 16 156.29 -44.18
REMARK 500 3 ALA A 25 -139.47 -60.04
REMARK 500 3 ALA A 26 139.68 -170.79
REMARK 500 3 SER A 74 116.20 -179.15
REMARK 500 3 GLU A 77 -70.98 -79.20
REMARK 500 3 VAL A 81 -30.78 -134.92
REMARK 500 3 CYS A 86 25.17 -79.87
REMARK 500 3 SER A 98 -45.43 -28.06
REMARK 500 3 LEU A 100 108.73 -44.49
REMARK 500 3 LEU A 102 -101.34 -69.25
REMARK 500 4 PRO A 2 -168.28 -69.74
REMARK 500 4 PRO A 8 -157.49 -77.22
REMARK 500 4 ALA A 9 -23.38 164.76
REMARK 500 4 SER A 21 112.99 -166.75
REMARK 500 4 ALA A 25 -124.64 -62.41
REMARK 500 4 ALA A 26 130.57 -175.39
REMARK 500
REMARK 500 THIS ENTRY HAS 437 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 68 0.31 SIDE CHAIN
REMARK 500 2 ARG A 68 0.28 SIDE CHAIN
REMARK 500 3 ARG A 68 0.20 SIDE CHAIN
REMARK 500 4 ARG A 68 0.26 SIDE CHAIN
REMARK 500 5 ARG A 68 0.25 SIDE CHAIN
REMARK 500 6 ARG A 68 0.25 SIDE CHAIN
REMARK 500 7 ARG A 68 0.19 SIDE CHAIN
REMARK 500 8 ARG A 68 0.31 SIDE CHAIN
REMARK 500 9 ARG A 68 0.31 SIDE CHAIN
REMARK 500 10 ARG A 68 0.24 SIDE CHAIN
REMARK 500 11 ARG A 68 0.25 SIDE CHAIN
REMARK 500 12 ARG A 68 0.15 SIDE CHAIN
REMARK 500 13 ARG A 68 0.23 SIDE CHAIN
REMARK 500 14 ARG A 68 0.30 SIDE CHAIN
REMARK 500 15 ARG A 68 0.29 SIDE CHAIN
REMARK 500 16 ARG A 68 0.29 SIDE CHAIN
REMARK 500 17 ARG A 68 0.32 SIDE CHAIN
REMARK 500 18 ARG A 68 0.30 SIDE CHAIN
REMARK 500 19 ARG A 68 0.28 SIDE CHAIN
REMARK 500 20 ARG A 68 0.20 SIDE CHAIN
REMARK 500 21 ARG A 68 0.23 SIDE CHAIN
REMARK 500 22 ARG A 68 0.26 SIDE CHAIN
REMARK 500 23 ARG A 68 0.28 SIDE CHAIN
REMARK 500 24 ARG A 68 0.24 SIDE CHAIN
REMARK 500 25 ARG A 68 0.26 SIDE CHAIN
REMARK 500 26 ARG A 68 0.31 SIDE CHAIN
REMARK 500 27 ARG A 68 0.32 SIDE CHAIN
REMARK 500 28 ARG A 68 0.24 SIDE CHAIN
REMARK 500 29 ARG A 68 0.30 SIDE CHAIN
REMARK 500 30 ARG A 68 0.21 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ROM A 111
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4947 RELATED DB: BMRB
REMARK 900 4947 CONTAINS 1H RESONANCE ASSIGNMENTS OF C-1027 APOPROTEIN
REMARK 900 COMPLEXED WITH THE AROMATIZED CHROMOPHORE
REMARK 900 RELATED ID: 1HZK RELATED DB: PDB
REMARK 900 1HZK IS C-1027 APOPROTEIN
DBREF 1HZL A 1 110 UNP Q06110 CAGA_STRGL 34 143
SEQRES 1 A 110 ALA PRO ALA PHE SER VAL SER PRO ALA SER GLY LEU SER
SEQRES 2 A 110 ASP GLY GLN SER VAL SER VAL SER VAL SER GLY ALA ALA
SEQRES 3 A 110 ALA GLY GLU THR TYR TYR ILE ALA GLN CYS ALA PRO VAL
SEQRES 4 A 110 GLY GLY GLN ASP ALA CYS ASN PRO ALA THR ALA THR SER
SEQRES 5 A 110 PHE THR THR ASP ALA SER GLY ALA ALA SER PHE SER PHE
SEQRES 6 A 110 VAL VAL ARG LYS SER TYR THR GLY SER THR PRO GLU GLY
SEQRES 7 A 110 THR PRO VAL GLY SER VAL ASP CYS ALA THR ALA ALA CYS
SEQRES 8 A 110 ASN LEU GLY ALA GLY ASN SER GLY LEU ASP LEU GLY HIS
SEQRES 9 A 110 VAL ALA LEU THR PHE GLY
HET ROM A 111 105
HETNAM ROM C-1027 AROMATIZED CHROMOPHORE
FORMUL 2 ROM C43 H45 CL N3 O13 1+
SHEET 1 A 3 ALA A 3 VAL A 6 0
SHEET 2 A 3 SER A 17 SER A 23 -1 N SER A 21 O SER A 5
SHEET 3 A 3 ALA A 61 VAL A 66 -1 N ALA A 61 O VAL A 22
SHEET 1 B 4 ASP A 43 THR A 54 0
SHEET 2 B 4 THR A 30 PRO A 38 -1 O TYR A 31 N PHE A 53
SHEET 3 B 4 ASN A 92 GLY A 96 -1 O ASN A 92 N CYS A 36
SHEET 4 B 4 ASP A 101 ALA A 106 -1 N LEU A 102 O ALA A 95
SHEET 1 C 2 SER A 70 THR A 75 0
SHEET 2 C 2 THR A 79 ASP A 85 -1 O THR A 79 N THR A 75
SSBOND 1 CYS A 36 CYS A 45 1555 1555 2.02
SSBOND 2 CYS A 86 CYS A 91 1555 1555 2.02
SITE 1 AC1 10 TYR A 32 ALA A 34 CYS A 36 CYS A 45
SITE 2 AC1 10 PRO A 47 THR A 75 PRO A 76 GLY A 96
SITE 3 AC1 10 ASN A 97 SER A 98
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 - g 9 2 Bytes