Header list of 1hvn.pdb file
Complete list - 23 20 Bytes
HEADER VIRAL PROTEIN/DNA 08-DEC-92 1HVN
TITLE ZINC-AND SEQUENCE-DEPENDENT BINDING TO NUCLEIC ACIDS BY THE N-TERMINAL
TITLE 2 ZINC FINGER DOMAIN OF THE HIV-1 NUCLEOCAPSID PROTEIN: NMR STRUCTURE
TITLE 3 OF THE COMPLEX WITH THE PSI-SITE ANALOG, D/ACGCC
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA (5'-D(P*AP*CP*GP*CP*C)-3');
COMPND 3 CHAIN: D;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: HIV-1 NUCLEOCAPSID ZINC FINGER;
COMPND 7 CHAIN: E;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 MOL_ID: 2;
SOURCE 4 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1;
SOURCE 5 ORGANISM_TAXID: 11676
KEYWDS VIRAL PROTEIN/DNA, VIRAL PROTEIN-DNA COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR T.L.SOUTH,M.F.SUMMERS
REVDAT 4 23-FEB-22 1HVN 1 REMARK LINK
REVDAT 3 24-FEB-09 1HVN 1 VERSN
REVDAT 2 01-APR-03 1HVN 1 JRNL
REVDAT 1 31-JAN-94 1HVN 0
JRNL AUTH T.L.SOUTH,M.F.SUMMERS
JRNL TITL ZINC- AND SEQUENCE-DEPENDENT BINDING TO NUCLEIC ACIDS BY THE
JRNL TITL 2 N-TERMINAL ZINC FINGER OF THE HIV-1 NUCLEOCAPSID PROTEIN:
JRNL TITL 3 NMR STRUCTURE OF THE COMPLEX WITH THE PSI-SITE ANALOG,
JRNL TITL 4 DACGCC.
JRNL REF PROTEIN SCI. V. 2 3 1993
JRNL REFN ISSN 0961-8368
JRNL PMID 8443588
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.F.SUMMERS,L.E.HENDERSON,M.R.CHANCE,J.W.BESS JUNIOR,
REMARK 1 AUTH 2 T.L.SOUTH,P.R.BLAKE,I.SAGI,G.PEREZ-ALVARADO,R.C.SOWDER III,
REMARK 1 AUTH 3 D.R.HARE,L.O.ARTHUR
REMARK 1 TITL NUCLEOCAPSID ZINC FINGERS DETECTED IN RETROVIRUSES: EXAFS
REMARK 1 TITL 2 STUDIES OF INTACT VIRUSES AND THE SOLUTION-STATE STRUCTURE
REMARK 1 TITL 3 OF THE NUCLEOCAPSID PROTEIN FROM HIV-1
REMARK 1 REF PROTEIN SCI. V. 1 563 1992
REMARK 1 REFN ISSN 0961-8368
REMARK 1 REFERENCE 2
REMARK 1 AUTH T.L.SOUTH,P.R.BLAKE,D.R.HARE,M.F.SUMMERS
REMARK 1 TITL THE C-TERMINAL RETROVIRAL-TYPE ZINC FINGER DOMAIN FROM THE
REMARK 1 TITL 2 HIV-1 NUCLEOCAPSID PROTEIN IS STRUCTURALLY SIMILAR TO THE
REMARK 1 TITL 3 N-TERMINAL ZINC FINGER DOMAIN
REMARK 1 REF BIOCHEMISTRY V. 30 6342 1991
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 3
REMARK 1 AUTH T.L.SOUTH,P.R.BLAKE,R.SOWDER III,L.O.ARTHUR,L.E.HENDERSON,
REMARK 1 AUTH 2 M.F.SUMMERS
REMARK 1 TITL THE NUCLEOCAPSID PROTEIN ISOLATED FROM HIV-I PARTICLES BINDS
REMARK 1 TITL 2 ZINC AND FORM RETROVIRAL-TYPE ZINC FINGERS
REMARK 1 REF BIOCHEMISTRY V. 29 7786 1990
REMARK 1 REFN ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NULL
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1HVN 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_1000174051.
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 : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: NULL
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E
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: 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 DA D 1 P DA D 1 OP3 -0.124
REMARK 500 2 DA D 1 P DA D 1 OP3 -0.124
REMARK 500 3 DA D 1 P DA D 1 OP3 -0.123
REMARK 500 4 DA D 1 P DA D 1 OP3 -0.123
REMARK 500 5 DA D 1 P DA D 1 OP3 -0.122
REMARK 500 6 DA D 1 P DA D 1 OP3 -0.123
REMARK 500 7 DA D 1 P DA D 1 OP3 -0.123
REMARK 500 8 DA D 1 P DA D 1 OP3 -0.123
REMARK 500 9 DA D 1 P DA D 1 OP3 -0.123
REMARK 500 10 DA D 1 P DA D 1 OP3 -0.123
REMARK 500 11 DA D 1 P DA D 1 OP3 -0.124
REMARK 500 12 DA D 1 P DA D 1 OP3 -0.123
REMARK 500 13 DA D 1 P DA D 1 OP3 -0.124
REMARK 500 14 DA D 1 P DA D 1 OP3 -0.122
REMARK 500 15 DA D 1 P DA D 1 OP3 -0.123
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 DA D 1 C3' - O3' - P ANGL. DEV. = -11.9 DEGREES
REMARK 500 1 DC D 2 C3' - O3' - P ANGL. DEV. = -12.0 DEGREES
REMARK 500 1 DG D 3 C3' - O3' - P ANGL. DEV. = -11.8 DEGREES
REMARK 500 1 DC D 4 O4' - C1' - N1 ANGL. DEV. = 1.9 DEGREES
REMARK 500 1 DC D 4 C3' - O3' - P ANGL. DEV. = -11.2 DEGREES
REMARK 500 1 DC D 5 O4' - C1' - N1 ANGL. DEV. = 2.0 DEGREES
REMARK 500 2 DA D 1 C3' - O3' - P ANGL. DEV. = -11.9 DEGREES
REMARK 500 2 DC D 2 C3' - O3' - P ANGL. DEV. = -12.0 DEGREES
REMARK 500 2 DG D 3 C3' - O3' - P ANGL. DEV. = -11.9 DEGREES
REMARK 500 2 DC D 4 O4' - C1' - N1 ANGL. DEV. = 1.9 DEGREES
REMARK 500 2 DC D 4 C3' - O3' - P ANGL. DEV. = -11.3 DEGREES
REMARK 500 2 DC D 5 O4' - C1' - N1 ANGL. DEV. = 2.0 DEGREES
REMARK 500 3 DA D 1 C3' - O3' - P ANGL. DEV. = -11.9 DEGREES
REMARK 500 3 DC D 2 C3' - O3' - P ANGL. DEV. = -12.0 DEGREES
REMARK 500 3 DG D 3 C3' - O3' - P ANGL. DEV. = -11.9 DEGREES
REMARK 500 3 DC D 4 O4' - C1' - N1 ANGL. DEV. = 1.9 DEGREES
REMARK 500 3 DC D 4 C3' - O3' - P ANGL. DEV. = -11.2 DEGREES
REMARK 500 3 DC D 5 O4' - C1' - N1 ANGL. DEV. = 2.1 DEGREES
REMARK 500 4 DA D 1 C3' - O3' - P ANGL. DEV. = -11.9 DEGREES
REMARK 500 4 DC D 2 C3' - O3' - P ANGL. DEV. = -12.0 DEGREES
REMARK 500 4 DG D 3 C3' - O3' - P ANGL. DEV. = -11.9 DEGREES
REMARK 500 4 DC D 4 O4' - C1' - N1 ANGL. DEV. = 1.9 DEGREES
REMARK 500 4 DC D 4 C3' - O3' - P ANGL. DEV. = -11.2 DEGREES
REMARK 500 4 DC D 5 O4' - C1' - N1 ANGL. DEV. = 2.0 DEGREES
REMARK 500 5 DA D 1 C3' - O3' - P ANGL. DEV. = -11.9 DEGREES
REMARK 500 5 DC D 2 C3' - O3' - P ANGL. DEV. = -12.0 DEGREES
REMARK 500 5 DG D 3 C3' - O3' - P ANGL. DEV. = -11.9 DEGREES
REMARK 500 5 DC D 4 O4' - C1' - N1 ANGL. DEV. = 1.9 DEGREES
REMARK 500 5 DC D 4 C3' - O3' - P ANGL. DEV. = -11.2 DEGREES
REMARK 500 5 DC D 5 O4' - C1' - N1 ANGL. DEV. = 2.0 DEGREES
REMARK 500 6 DA D 1 C3' - O3' - P ANGL. DEV. = -11.9 DEGREES
REMARK 500 6 DC D 2 C3' - O3' - P ANGL. DEV. = -12.1 DEGREES
REMARK 500 6 DG D 3 C3' - O3' - P ANGL. DEV. = -11.9 DEGREES
REMARK 500 6 DC D 4 O4' - C1' - N1 ANGL. DEV. = 1.9 DEGREES
REMARK 500 6 DC D 4 C3' - O3' - P ANGL. DEV. = -11.2 DEGREES
REMARK 500 6 DC D 5 O4' - C1' - N1 ANGL. DEV. = 2.1 DEGREES
REMARK 500 7 DA D 1 C3' - O3' - P ANGL. DEV. = -11.9 DEGREES
REMARK 500 7 DC D 2 C3' - O3' - P ANGL. DEV. = -12.0 DEGREES
REMARK 500 7 DG D 3 C3' - O3' - P ANGL. DEV. = -11.9 DEGREES
REMARK 500 7 DC D 4 O4' - C1' - N1 ANGL. DEV. = 1.9 DEGREES
REMARK 500 7 DC D 4 C3' - O3' - P ANGL. DEV. = -11.2 DEGREES
REMARK 500 7 DC D 5 O4' - C1' - N1 ANGL. DEV. = 2.1 DEGREES
REMARK 500 8 DA D 1 C3' - O3' - P ANGL. DEV. = -11.9 DEGREES
REMARK 500 8 DC D 2 C3' - O3' - P ANGL. DEV. = -12.0 DEGREES
REMARK 500 8 DG D 3 C3' - O3' - P ANGL. DEV. = -11.9 DEGREES
REMARK 500 8 DC D 4 O4' - C1' - N1 ANGL. DEV. = 1.9 DEGREES
REMARK 500 8 DC D 4 C3' - O3' - P ANGL. DEV. = -11.2 DEGREES
REMARK 500 8 DC D 5 O4' - C1' - N1 ANGL. DEV. = 2.0 DEGREES
REMARK 500 9 DA D 1 C3' - O3' - P ANGL. DEV. = -11.9 DEGREES
REMARK 500 9 DC D 2 C3' - O3' - P ANGL. DEV. = -12.0 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 91 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 1 CYS E 16 -147.94 -65.21
REMARK 500 1 ARG E 17 -38.36 177.65
REMARK 500 2 CYS E 16 -117.70 -78.86
REMARK 500 2 ARG E 17 -73.09 170.71
REMARK 500 3 ARG E 17 29.48 -159.41
REMARK 500 4 ARG E 14 -8.73 -59.89
REMARK 500 7 CYS E 16 -72.00 -72.58
REMARK 500 7 ARG E 17 -54.86 78.30
REMARK 500 10 ARG E 14 -8.19 -59.99
REMARK 500 12 ARG E 14 -9.37 -59.61
REMARK 500 13 ARG E 14 -8.27 -59.68
REMARK 500 14 ARG E 17 28.26 -145.75
REMARK 500 15 ARG E 17 28.40 -148.06
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 1 CYS E 3 -13.76
REMARK 500 1 PHE E 4 -10.95
REMARK 500 1 ILE E 12 -13.16
REMARK 500 2 CYS E 3 -12.83
REMARK 500 2 HIS E 11 11.54
REMARK 500 2 ILE E 12 -14.39
REMARK 500 2 ARG E 17 10.45
REMARK 500 3 CYS E 3 -12.22
REMARK 500 3 PHE E 4 -10.09
REMARK 500 3 HIS E 11 13.00
REMARK 500 3 ILE E 12 -13.84
REMARK 500 4 CYS E 3 -11.75
REMARK 500 4 ILE E 12 -13.80
REMARK 500 5 CYS E 3 -10.93
REMARK 500 5 ILE E 12 -14.01
REMARK 500 6 CYS E 3 -11.92
REMARK 500 6 ILE E 12 -15.55
REMARK 500 7 CYS E 3 -11.22
REMARK 500 7 ILE E 12 -13.93
REMARK 500 7 CYS E 16 13.19
REMARK 500 8 VAL E 1 -12.01
REMARK 500 8 HIS E 11 11.73
REMARK 500 8 ILE E 12 -16.01
REMARK 500 9 CYS E 3 -11.10
REMARK 500 9 ILE E 12 -15.33
REMARK 500 10 CYS E 3 -12.07
REMARK 500 10 HIS E 11 12.37
REMARK 500 10 ILE E 12 -13.94
REMARK 500 11 CYS E 3 -13.08
REMARK 500 11 HIS E 11 10.80
REMARK 500 11 ILE E 12 -15.39
REMARK 500 12 CYS E 3 -13.40
REMARK 500 12 HIS E 11 11.02
REMARK 500 12 ILE E 12 -15.14
REMARK 500 13 CYS E 3 -14.24
REMARK 500 13 ASN E 5 -10.39
REMARK 500 13 HIS E 11 10.38
REMARK 500 13 ILE E 12 -14.70
REMARK 500 14 CYS E 3 -13.66
REMARK 500 14 ILE E 12 -12.77
REMARK 500 15 CYS E 3 -12.49
REMARK 500 15 HIS E 11 11.15
REMARK 500 15 ILE E 12 -15.38
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN E 19 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS E 3 SG
REMARK 620 2 CYS E 6 SG 106.3
REMARK 620 3 HIS E 11 NE2 92.9 109.3
REMARK 620 4 CYS E 16 SG 115.0 108.9 122.7
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 19
DBREF 1HVN E 1 18 UNP Q70622 GAG_HV1LW 389 406
DBREF 1HVN D 1 5 PDB 1HVN 1HVN 1 5
SEQRES 1 D 5 DA DC DG DC DC
SEQRES 1 E 18 VAL LYS CYS PHE ASN CYS GLY LYS GLU GLY HIS ILE ALA
SEQRES 2 E 18 ARG ASN CYS ARG ALA
HET ZN E 19 1
HETNAM ZN ZINC ION
FORMUL 3 ZN ZN 2+
HELIX 1 1 ILE E 12 CYS E 16 5 5
LINK SG CYS E 3 ZN ZN E 19 1555 1555 2.31
LINK SG CYS E 6 ZN ZN E 19 1555 1555 2.30
LINK NE2 HIS E 11 ZN ZN E 19 1555 1555 2.02
LINK SG CYS E 16 ZN ZN E 19 1555 1555 2.30
SITE 1 AC1 4 CYS E 3 CYS E 6 HIS E 11 CYS E 16
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 - 23 20 Bytes