Header list of 185d.pdb file
Complete list - 1 20 Bytes
HEADER DNA/ANTIBIOTIC 10-AUG-94 185D
TITLE SEQUENCE SPECIFICITY OF QUINOXALINE ANTIBIOTICS. 1. SOLUTION STRUCTURE
TITLE 2 OF A 1:1 COMPLEX BETWEEN TRIOSTIN A AND [D(GACGTC)]2 AND COMPARISON
TITLE 3 WITH THE SOLUTION STRUCTURE OF THE [N-MECYS3, N-MECYS7]TANDEM-
TITLE 4 [D(GATATC)]2 COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRIOSTIN A;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: DNA (5'-D(*GP*AP*CP*GP*TP*C)-3');
COMPND 7 CHAIN: C, D;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 ORGANISM_SCIENTIFIC: STREPTOMYCINEAE;
SOURCE 4 ORGANISM_TAXID: 1931;
SOURCE 5 MOL_ID: 2;
SOURCE 6 SYNTHETIC: YES
KEYWDS BISINTERCALATOR, DEPSIPEPTIDE, QUINOXALINE, ANTIBIOTIC, ANTITUMOR,
KEYWDS 2 DNA-ANTIBIOTIC COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 5
AUTHOR K.J.ADDESS,J.FEIGON
REVDAT 5 01-NOV-17 185D 1 REMARK
REVDAT 4 27-JUL-11 185D 1 DBREF HETATM REMARK
REVDAT 3 13-JUL-11 185D 1 VERSN
REVDAT 2 24-FEB-09 185D 1 VERSN
REVDAT 1 07-FEB-95 185D 0
JRNL AUTH K.J.ADDESS,J.FEIGON
JRNL TITL SEQUENCE SPECIFICITY OF QUINOXALINE ANTIBIOTICS. 1. SOLUTION
JRNL TITL 2 STRUCTURE OF A 1:1 COMPLEX BETWEEN TRIOSTIN A AND
JRNL TITL 3 [D(GACGTC)]2 AND COMPARISON WITH THE SOLUTION STRUCTURE OF
JRNL TITL 4 THE [N-MECYS3,N-MECYS7]TANDEM-[D(GATATC)]2 COMPLEX.
JRNL REF BIOCHEMISTRY V. 33 12386 1994
JRNL REFN ISSN 0006-2960
JRNL PMID 7918461
JRNL DOI 10.1021/BI00207A005
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH K.J.ADDESS,J.S.SINSHEIMER,J.FEIGON
REMARK 1 TITL SOLUTION STRUCTURE OF A COMPLEX BETWEEN
REMARK 1 TITL 2 [N-MECYS3,N-MECYS7]TANDEM AND [D(GATATC)]2
REMARK 1 REF BIOCHEMISTRY V. 32 2498 1993
REMARK 1 REFN ISSN 0006-2960
REMARK 1 PMID 8448108
REMARK 1 DOI 10.1021/BI00061A006
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: NUMBER OF ATOMS PRESENT IN ENTRY.
REMARK 3 NUMBER OF PROTEIN ATOMS 328 NUMBER OF NUCLEIC ACID ATOMS 48
REMARK 3 NUMBER OF SOLVENT ATOMS 240 NUMBER OF HETEROGEN ATOMS 40 AVERAGE
REMARK 3 PAIRWISE RMSD BOND DISTANCES FOR HEAVY ATOM POSITIONS FOR 5
REMARK 3 STRUCTURES: 1.37 ANGSTROMS.
REMARK 4
REMARK 4 185D 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_1000170189.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : DISTANCE GEOMETRY, MOLECULAR
REMARK 210 DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 5
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: TRIOSTIN A CONTAINS TWO PLANAR AROMATIC QUINOXALINE RINGS
REMARK 210 THAT ARE COVALENTLY ATTACHED TO A CYCLIC OCTADEPSIPEPTIDE RING
REMARK 210 REPRESENTED BY CHAINS A AND B IN THIS ENTRY. THERE IS A
REMARK 210 DISULFIDE BRIDGE LINKING CYS A 4 TO CYS B 9. BOTH CYS AND VAL
REMARK 210 RESIDUES CONTAIN METHYLATED AMIDE NITROGENS; THE TWO D-SER
REMARK 210 RESIDUES ARE AMIDE BONDED TO THE TWO QUINOXALINE RINGS.
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2080 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 2840 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -3.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, D
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 400
REMARK 400 COMPOUND
REMARK 400 TRIOSTIN IS A BICYCLIC OCTADEPSIPEPTIDE, A MEMBER
REMARK 400 OF THE QUINOXALINE CLASS OF ANTIBIOTICS.
REMARK 400 HERE, TRIOSTIN IS REPRESENTED BY GROUPING TOGETHER THE
REMARK 400 SEQUENCE (SEQRES) AND THE TWO LIGANDS (HET) QUI
REMARK 400
REMARK 400 THE TRIOSTIN A IS CYCLIC DEPSIPEPTIDE, A MEMBER OF ANTICANCER CLASS.
REMARK 400
REMARK 400 GROUP: 1
REMARK 400 NAME: TRIOSTIN A
REMARK 400 CHAIN: A
REMARK 400 COMPONENT_1: PEPTIDE LIKE POLYMER
REMARK 400 COMPONENT_2: RESIDUE QUI, 2 COPIES
REMARK 400 DESCRIPTION: TRIOSTIN IS A BICYCLIC OCTADEPSIPEPTIDE.
REMARK 400 BICYCLIZATION IS ACHIEVED BY LINKING THE N- AND THE
REMARK 400 C- TERMINI, AND A DISULPHIDE BOND BETWEEN RESIDUES 3
REMARK 400 AND 7. THE TWO QUINOXALINE CHROMOPHORES ARE LINKED
REMARK 400 TO THE D-SERINE RESIDUES, RESIDUES 1 AND 5.
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 1 DT C 15 C5 DT C 15 C7 0.039
REMARK 500 1 DT D 21 C5 DT D 21 C7 0.043
REMARK 500 2 DT C 15 C5 DT C 15 C7 0.042
REMARK 500 3 DT C 15 C5 DT C 15 C7 0.038
REMARK 500 4 DT C 15 C5 DT C 15 C7 0.036
REMARK 500 4 DT D 21 C5 DT D 21 C7 0.036
REMARK 500 5 DT C 15 C5 DT C 15 C7 0.040
REMARK 500 5 DT D 21 C5 DT D 21 C7 0.037
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 1 DG C 11 O4' - C1' - N9 ANGL. DEV. = 1.9 DEGREES
REMARK 500 1 DG C 11 N7 - C8 - N9 ANGL. DEV. = 3.3 DEGREES
REMARK 500 1 DC C 13 C1' - O4' - C4' ANGL. DEV. = -6.2 DEGREES
REMARK 500 1 DC C 13 N1 - C2 - O2 ANGL. DEV. = 3.8 DEGREES
REMARK 500 1 DG C 14 O4' - C1' - C2' ANGL. DEV. = -5.5 DEGREES
REMARK 500 1 DG C 14 N7 - C8 - N9 ANGL. DEV. = 3.2 DEGREES
REMARK 500 1 DG D 17 C1' - O4' - C4' ANGL. DEV. = -6.5 DEGREES
REMARK 500 1 DG D 17 N7 - C8 - N9 ANGL. DEV. = 3.3 DEGREES
REMARK 500 1 DC D 19 C1' - O4' - C4' ANGL. DEV. = -6.8 DEGREES
REMARK 500 1 DC D 19 O4' - C1' - N1 ANGL. DEV. = 2.7 DEGREES
REMARK 500 1 DC D 19 N1 - C2 - O2 ANGL. DEV. = 3.7 DEGREES
REMARK 500 1 DG D 20 N7 - C8 - N9 ANGL. DEV. = 3.1 DEGREES
REMARK 500 1 DT D 21 O4' - C1' - C2' ANGL. DEV. = -4.9 DEGREES
REMARK 500 1 DC D 22 O4' - C1' - N1 ANGL. DEV. = 2.8 DEGREES
REMARK 500 2 DG C 11 O4' - C1' - C2' ANGL. DEV. = -5.3 DEGREES
REMARK 500 2 DG C 11 O4' - C1' - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 2 DG C 11 N7 - C8 - N9 ANGL. DEV. = 3.1 DEGREES
REMARK 500 2 DC C 13 O4' - C1' - N1 ANGL. DEV. = 1.8 DEGREES
REMARK 500 2 DG C 14 O4' - C1' - C2' ANGL. DEV. = -5.9 DEGREES
REMARK 500 2 DG C 14 O4' - C1' - N9 ANGL. DEV. = 3.9 DEGREES
REMARK 500 2 DG C 14 N7 - C8 - N9 ANGL. DEV. = 3.3 DEGREES
REMARK 500 2 DC C 16 O4' - C1' - N1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 2 DG D 17 N7 - C8 - N9 ANGL. DEV. = 3.5 DEGREES
REMARK 500 2 DG D 20 C1' - O4' - C4' ANGL. DEV. = -6.2 DEGREES
REMARK 500 2 DG D 20 O4' - C1' - C2' ANGL. DEV. = -6.8 DEGREES
REMARK 500 2 DG D 20 O4' - C1' - N9 ANGL. DEV. = 4.4 DEGREES
REMARK 500 2 DG D 20 N7 - C8 - N9 ANGL. DEV. = 3.3 DEGREES
REMARK 500 3 DG C 11 O4' - C1' - N9 ANGL. DEV. = 2.0 DEGREES
REMARK 500 3 DG C 11 N7 - C8 - N9 ANGL. DEV. = 3.4 DEGREES
REMARK 500 3 DA C 12 O4' - C1' - N9 ANGL. DEV. = 2.5 DEGREES
REMARK 500 3 DC C 13 O4' - C1' - N1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 3 DG C 14 O4' - C1' - N9 ANGL. DEV. = 2.2 DEGREES
REMARK 500 3 DG C 14 N7 - C8 - N9 ANGL. DEV. = 3.2 DEGREES
REMARK 500 3 DT C 15 O4' - C1' - C2' ANGL. DEV. = -6.8 DEGREES
REMARK 500 3 DC C 16 O4' - C1' - N1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 3 DG D 17 N7 - C8 - N9 ANGL. DEV. = 3.4 DEGREES
REMARK 500 3 DG D 17 C3' - O3' - P ANGL. DEV. = 9.2 DEGREES
REMARK 500 3 DA D 18 O4' - C1' - C2' ANGL. DEV. = -4.9 DEGREES
REMARK 500 3 DC D 19 C4' - C3' - C2' ANGL. DEV. = -4.6 DEGREES
REMARK 500 3 DC D 19 O4' - C1' - N1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 3 DG D 20 O4' - C1' - C2' ANGL. DEV. = -5.5 DEGREES
REMARK 500 3 DG D 20 O4' - C1' - N9 ANGL. DEV. = 3.6 DEGREES
REMARK 500 3 DG D 20 N7 - C8 - N9 ANGL. DEV. = 3.2 DEGREES
REMARK 500 3 DC D 22 O4' - C1' - N1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 4 DG C 11 O4' - C1' - C2' ANGL. DEV. = -5.4 DEGREES
REMARK 500 4 DG C 11 O4' - C1' - N9 ANGL. DEV. = 4.4 DEGREES
REMARK 500 4 DG C 11 N7 - C8 - N9 ANGL. DEV. = 3.3 DEGREES
REMARK 500 4 DC C 13 C4' - C3' - C2' ANGL. DEV. = -5.2 DEGREES
REMARK 500 4 DC C 13 O4' - C1' - N1 ANGL. DEV. = 5.2 DEGREES
REMARK 500 4 DG C 14 O4' - C1' - C2' ANGL. DEV. = -5.4 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 73 ANGLE DEVIATIONS.
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 5 NCY A 3 -61.43 -98.73
REMARK 500 5 NCY A 7 -62.43 -90.57
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 CHAIN A OF TRIOSTIN A
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 193D RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF D(ACACGTGT) COMPLEXED WITH QUINOMYCIN UK-6305
REMARK 900 RELATED ID: 1PFE RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF D(GCGTACG) COMPLEXED WITH ECHINOMYCIN - SPACE
REMARK 900 GROUP P6322
REMARK 900 RELATED ID: 1VS2 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF D(GCGTACGC) COMPLEXED WITH TRIOSIN A
REMARK 900 RELATED ID: 1XVK RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF D(GCGTACGC) COMPLEXED WITH ECHINOMYCIN - SPACE
REMARK 900 GROUP P632
REMARK 900 RELATED ID: 1XVN RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF D(ACGTACGT) COMPLEXED WITH ECHINOMYCIN - SPACE
REMARK 900 GROUP P632
REMARK 900 RELATED ID: 1XVR RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF D(CGTACG) COMPLEXED WITH ECHINOMYCIN - SPACE
REMARK 900 GROUP C21
REMARK 900 RELATED ID: 2ADW RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF D(ACGTACGT) COMPLEXED WITH ECHINOMYCIN - SPACE
REMARK 900 GROUP P42212
REMARK 900 RELATED ID: 2DA8 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF D(GATATC) COMPLEXED WITH A MODIFIED TRIOSTIN
REMARK 900 A AT POSITIONS 4 AND 8
REMARK 900 RELATED ID: 3GO3 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF D(ACGTACGT) COMPLEXED WITH ECHINOMYCIN - SPACE
REMARK 900 GROUP P41212
DBREF 185D A 1 8 NOR NOR01129 NOR01129 1 8
DBREF 185D C 11 16 PDB 185D 185D 1 6
DBREF 185D D 17 22 PDB 185D 185D 1 6
SEQRES 1 A 8 DSN ALA NCY MVA DSN ALA NCY MVA
SEQRES 1 C 6 DG DA DC DG DT DC
SEQRES 1 D 6 DG DA DC DG DT DC
HET DSN A 1 10
HET NCY A 3 13
HET MVA A 4 19
HET DSN A 5 10
HET NCY A 7 13
HET MVA A 8 19
HET QUI A 0 17
HET QUI A 9 17
HETNAM DSN D-SERINE
HETNAM NCY N-METHYLCYSTEINE
HETNAM MVA N-METHYLVALINE
HETNAM QUI 2-CARBOXYQUINOXALINE
FORMUL 1 DSN 2(C3 H7 N O3)
FORMUL 1 NCY 2(C4 H9 N O2 S)
FORMUL 1 MVA 2(C6 H13 N O2)
FORMUL 4 QUI 2(C9 H6 N2 O2)
SSBOND 1 NCY A 3 NCY A 7 1555 1555 2.02
LINK C QUI A 0 N DSN A 1 1555 1555 1.33
LINK C DSN A 1 N ALA A 2 1555 1555 1.31
LINK OG DSN A 1 C MVA A 8 1555 1555 1.33
LINK C ALA A 2 N NCY A 3 1555 1555 1.32
LINK C NCY A 3 N MVA A 4 1555 1555 1.33
LINK C MVA A 4 OG DSN A 5 1555 1555 1.33
LINK C DSN A 5 N ALA A 6 1555 1555 1.30
LINK N DSN A 5 C QUI A 9 1555 1555 1.33
LINK C ALA A 6 N NCY A 7 1555 1555 1.33
LINK C NCY A 7 N MVA A 8 1555 1555 1.33
SITE 1 AC1 8 DA C 12 DC C 13 DG C 14 DT C 15
SITE 2 AC1 8 DA D 18 DC D 19 DG D 20 DT D 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 - 1 20 Bytes