Header list of 1pih.pdb file
Complete list - 23 20 Bytes
HEADER ELECTRON TRANSFER(IRON-SULFUR PROTEIN) 03-AUG-94 1PIH TITLE THE THREE DIMENSIONAL STRUCTURE OF THE PARAMAGNETIC PROTEIN HIPIP I TITLE 2 FROM E.HALOPHILA THROUGH NUCLEAR MAGNETIC RESONANCE COMPND MOL_ID: 1; COMPND 2 MOLECULE: HIGH POTENTIAL IRON SULFUR PROTEIN; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HALORHODOSPIRA HALOPHILA; SOURCE 3 ORGANISM_TAXID: 1053; SOURCE 4 GENE: POTENTIAL KEYWDS ELECTRON TRANSFER(IRON-SULFUR PROTEIN) EXPDTA SOLUTION NMR NUMMDL 15 AUTHOR L.BANCI,I.BERTINI,L.D.ELTIS,I.FELLI,D.H.W.KASTRAU,C.LUCHINAT, AUTHOR 2 M.PICCIOLI,R.PIERATTELLI,M.SMITH REVDAT 6 23-FEB-22 1PIH 1 REMARK REVDAT 5 24-MAR-09 1PIH 1 ATOM CONECT REVDAT 4 24-FEB-09 1PIH 1 VERSN REVDAT 3 01-APR-03 1PIH 1 JRNL REVDAT 2 08-MAR-95 1PIH 1 JRNL REMARK REVDAT 1 20-DEC-94 1PIH 0 JRNL AUTH L.BANCI,I.BERTINI,L.D.ELTIS,I.C.FELLI,D.H.KASTRAU, JRNL AUTH 2 C.LUCHINAT,M.PICCIOLI,R.PIERATTELLI,M.SMITH JRNL TITL THE THREE-DIMENSIONAL STRUCTURE IN SOLUTION OF THE JRNL TITL 2 PARAMAGNETIC HIGH-POTENTIAL IRON-SULFUR PROTEIN I FROM JRNL TITL 3 ECTOTHIORHODOSPIRA HALOPHILA THROUGH NUCLEAR MAGNETIC JRNL TITL 4 RESONANCE. JRNL REF EUR.J.BIOCHEM. V. 225 715 1994 JRNL REFN ISSN 0014-2956 JRNL PMID 7957187 JRNL DOI 10.1111/J.1432-1033.1994.00715.X REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH I.BERTINI,I.FELLI,D.H.W.KASTRAU,C.LUCHINAT,M.PICCIOLI, REMARK 1 AUTH 2 M.S.VIEZZOLI REMARK 1 TITL SEQUENCE SPECIFIC ASSIGNMENT OF THE 1H AND 15N NUCLEAR REMARK 1 TITL 2 MAGNETIC RESONANCE SPECTRA OF THE REDUCED RECOMBINANT HIGH REMARK 1 TITL 3 POTENTIAL IRON SULFUR PROTEIN (HIPIP) I FROM REMARK 1 TITL 4 ECTOTHIORHODOSPIRA HALOPHILA REMARK 1 REF EUR.J.BIOCHEM. V. 225 703 1994 REMARK 1 REFN ISSN 0014-2956 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : AMBER REMARK 3 AUTHORS : GUNTERT,BRAUN,WUTHRICH (DIANA), REMARK 3 PEARLMAN,CASE,CALDWELL,SIEBEL,SINGH,WEINER,KOLLMAN REMARK 3 (AMBER) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1PIH 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_1000175695. 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: 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 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 VAL A 68 CA - CB - CG2 ANGL. DEV. = 10.1 DEGREES REMARK 500 3 VAL A 68 CA - CB - CG2 ANGL. DEV. = 9.9 DEGREES REMARK 500 4 PHE A 55 CB - CG - CD1 ANGL. DEV. = -4.4 DEGREES REMARK 500 5 GLU A 3 OE1 - CD - OE2 ANGL. DEV. = -8.5 DEGREES REMARK 500 5 VAL A 68 CA - CB - CG2 ANGL. DEV. = 10.7 DEGREES REMARK 500 6 ARG A 49 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES REMARK 500 7 VAL A 68 CA - CB - CG2 ANGL. DEV. = 9.6 DEGREES REMARK 500 8 ARG A 49 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES REMARK 500 8 ARG A 49 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES REMARK 500 8 VAL A 68 CA - CB - CG2 ANGL. DEV. = 10.2 DEGREES REMARK 500 12 VAL A 68 CA - CB - CG2 ANGL. DEV. = 9.6 DEGREES REMARK 500 14 GLU A 3 OE1 - CD - OE2 ANGL. DEV. = -8.9 DEGREES REMARK 500 14 VAL A 68 CA - CB - CG2 ANGL. DEV. = 11.3 DEGREES REMARK 500 15 ARG A 49 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES REMARK 500 15 ARG A 49 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES REMARK 500 15 VAL A 68 CA - CB - CG2 ANGL. DEV. = 11.3 DEGREES 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 GLN A 44 -138.98 -151.43 REMARK 500 1 ASP A 45 66.83 -69.19 REMARK 500 1 ASP A 54 47.14 -70.10 REMARK 500 1 PHE A 55 -55.40 -172.71 REMARK 500 1 ALA A 72 34.84 -97.40 REMARK 500 2 ARG A 26 -41.32 127.18 REMARK 500 2 GLN A 44 -128.59 -152.07 REMARK 500 2 HIS A 52 136.80 95.72 REMARK 500 2 ASP A 54 -13.49 98.28 REMARK 500 2 TYR A 69 113.01 -27.06 REMARK 500 2 ALA A 72 35.41 -98.76 REMARK 500 3 SER A 2 -158.48 -57.31 REMARK 500 3 GLU A 3 154.34 -45.53 REMARK 500 3 ARG A 26 -37.62 124.96 REMARK 500 3 GLU A 34 31.35 -76.92 REMARK 500 3 ASN A 35 30.31 -143.11 REMARK 500 3 GLN A 44 -152.85 -147.67 REMARK 500 3 ASP A 45 68.45 -56.54 REMARK 500 3 HIS A 52 117.59 96.41 REMARK 500 3 ASP A 54 -20.33 100.08 REMARK 500 3 VAL A 68 -70.35 -67.74 REMARK 500 3 TYR A 69 -85.34 58.72 REMARK 500 3 ALA A 70 124.95 62.68 REMARK 500 3 ALA A 72 48.66 -91.93 REMARK 500 4 SER A 2 38.11 -94.13 REMARK 500 4 HIS A 12 50.07 37.11 REMARK 500 4 ARG A 26 -35.81 143.16 REMARK 500 4 ASP A 45 71.12 -56.40 REMARK 500 4 ASP A 54 -40.19 122.01 REMARK 500 4 ALA A 72 35.43 -98.96 REMARK 500 5 HIS A 12 48.13 39.97 REMARK 500 5 ARG A 26 -38.60 127.58 REMARK 500 5 GLU A 34 23.96 -75.10 REMARK 500 5 ASP A 54 -29.20 120.80 REMARK 500 5 ALA A 72 33.59 -99.33 REMARK 500 6 SER A 2 47.49 -153.75 REMARK 500 6 ARG A 26 -44.19 141.10 REMARK 500 6 VAL A 43 -50.72 -123.82 REMARK 500 6 GLN A 44 -138.64 -140.73 REMARK 500 6 ASP A 45 64.18 -68.51 REMARK 500 6 THR A 51 -29.44 71.44 REMARK 500 6 PHE A 55 -42.29 -179.46 REMARK 500 6 ALA A 72 33.07 -96.73 REMARK 500 7 SER A 2 55.92 -162.09 REMARK 500 7 HIS A 12 50.52 39.02 REMARK 500 7 ARG A 26 -36.27 -178.06 REMARK 500 7 GLN A 44 -155.44 -151.71 REMARK 500 7 ASP A 45 70.52 -56.96 REMARK 500 7 HIS A 52 163.26 82.52 REMARK 500 7 ASP A 54 -171.50 63.43 REMARK 500 REMARK 500 THIS ENTRY HAS 116 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 GLN A 44 ASP A 45 5 148.94 REMARK 500 ARG A 49 CYS A 50 8 141.06 REMARK 500 SER A 2 GLU A 3 9 -148.89 REMARK 500 PRO A 71 ALA A 72 11 142.48 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 5 0.16 SIDE CHAIN REMARK 500 1 PHE A 55 0.09 SIDE CHAIN REMARK 500 2 ARG A 5 0.16 SIDE CHAIN REMARK 500 2 TYR A 27 0.17 SIDE CHAIN REMARK 500 2 PHE A 55 0.09 SIDE CHAIN REMARK 500 2 TYR A 69 0.07 SIDE CHAIN REMARK 500 3 ARG A 5 0.15 SIDE CHAIN REMARK 500 3 HIS A 12 0.09 SIDE CHAIN REMARK 500 3 TYR A 27 0.17 SIDE CHAIN REMARK 500 3 PHE A 55 0.10 SIDE CHAIN REMARK 500 4 ARG A 5 0.12 SIDE CHAIN REMARK 500 4 ARG A 26 0.12 SIDE CHAIN REMARK 500 4 PHE A 55 0.15 SIDE CHAIN REMARK 500 4 TYR A 69 0.06 SIDE CHAIN REMARK 500 5 ARG A 5 0.20 SIDE CHAIN REMARK 500 5 TYR A 27 0.14 SIDE CHAIN REMARK 500 5 PHE A 55 0.08 SIDE CHAIN REMARK 500 6 ARG A 49 0.15 SIDE CHAIN REMARK 500 6 PHE A 55 0.13 SIDE CHAIN REMARK 500 7 ARG A 5 0.14 SIDE CHAIN REMARK 500 7 PHE A 55 0.09 SIDE CHAIN REMARK 500 8 ARG A 5 0.12 SIDE CHAIN REMARK 500 8 HIS A 12 0.10 SIDE CHAIN REMARK 500 8 ARG A 26 0.12 SIDE CHAIN REMARK 500 8 TYR A 27 0.16 SIDE CHAIN REMARK 500 8 ARG A 49 0.12 SIDE CHAIN REMARK 500 9 ARG A 5 0.12 SIDE CHAIN REMARK 500 9 TYR A 27 0.07 SIDE CHAIN REMARK 500 9 ARG A 49 0.15 SIDE CHAIN REMARK 500 9 PHE A 55 0.10 SIDE CHAIN REMARK 500 9 TYR A 69 0.07 SIDE CHAIN REMARK 500 10 ARG A 5 0.18 SIDE CHAIN REMARK 500 10 ARG A 26 0.08 SIDE CHAIN REMARK 500 11 ARG A 5 0.20 SIDE CHAIN REMARK 500 11 ARG A 26 0.15 SIDE CHAIN REMARK 500 11 TYR A 27 0.21 SIDE CHAIN REMARK 500 12 ARG A 5 0.11 SIDE CHAIN REMARK 500 12 TYR A 27 0.18 SIDE CHAIN REMARK 500 12 ARG A 49 0.09 SIDE CHAIN REMARK 500 13 ARG A 5 0.12 SIDE CHAIN REMARK 500 13 HIS A 12 0.11 SIDE CHAIN REMARK 500 13 TYR A 27 0.12 SIDE CHAIN REMARK 500 13 PHE A 55 0.09 SIDE CHAIN REMARK 500 14 ARG A 5 0.10 SIDE CHAIN REMARK 500 14 HIS A 12 0.09 SIDE CHAIN REMARK 500 14 TYR A 27 0.15 SIDE CHAIN REMARK 500 14 ARG A 49 0.07 SIDE CHAIN REMARK 500 14 HIS A 52 0.09 SIDE CHAIN REMARK 500 15 ARG A 5 0.21 SIDE CHAIN REMARK 500 15 HIS A 12 0.10 SIDE CHAIN REMARK 500 REMARK 500 THIS ENTRY HAS 52 PLANE DEVIATIONS. 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 SF4 A 74 FE1 REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 33 SG REMARK 620 2 SF4 A 74 S2 111.6 REMARK 620 3 SF4 A 74 S3 110.7 105.8 REMARK 620 4 SF4 A 74 S4 116.3 105.5 106.3 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 SF4 A 74 FE2 REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 36 SG REMARK 620 2 SF4 A 74 S1 110.1 REMARK 620 3 SF4 A 74 S3 113.5 106.4 REMARK 620 4 SF4 A 74 S4 112.6 107.3 106.6 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 SF4 A 74 FE3 REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 50 SG REMARK 620 2 SF4 A 74 S1 108.3 REMARK 620 3 SF4 A 74 S2 115.7 106.8 REMARK 620 4 SF4 A 74 S4 112.8 106.7 106.1 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 SF4 A 74 FE4 REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 66 SG REMARK 620 2 SF4 A 74 S1 109.2 REMARK 620 3 SF4 A 74 S2 114.3 106.6 REMARK 620 4 SF4 A 74 S3 113.0 105.8 107.3 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 SF4 A 74 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1PIJ RELATED DB: PDB DBREF 1PIH A 3 73 UNP P04168 HIP1_ECTHA 1 71 SEQRES 1 A 73 ALA SER GLU PRO ARG ALA GLU ASP GLY HIS ALA HIS ASP SEQRES 2 A 73 TYR VAL ASN GLU ALA ALA ASP ALA SER GLY HIS PRO ARG SEQRES 3 A 73 TYR GLN GLU GLY GLN LEU CYS GLU ASN CYS ALA PHE TRP SEQRES 4 A 73 GLY GLU ALA VAL GLN ASP GLY TRP GLY ARG CYS THR HIS SEQRES 5 A 73 PRO ASP PHE ASP GLU VAL LEU VAL LYS ALA GLU GLY TRP SEQRES 6 A 73 CYS SER VAL TYR ALA PRO ALA SER HET SF4 A 74 8 HETNAM SF4 IRON/SULFUR CLUSTER FORMUL 2 SF4 FE4 S4 HELIX 1 1 GLU A 17 HIS A 24 5 8 HELIX 2 2 LEU A 32 ASN A 35 5 4 HELIX 3 3 HIS A 52 GLU A 57 1 6 SHEET 1 A 3 TRP A 39 GLN A 44 0 SHEET 2 A 3 TRP A 47 CYS A 50 -1 O TRP A 47 N VAL A 43 SHEET 3 A 3 VAL A 60 LYS A 61 -1 O VAL A 60 N GLY A 48 LINK SG CYS A 33 FE1 SF4 A 74 1555 1555 2.06 LINK SG CYS A 36 FE2 SF4 A 74 1555 1555 2.03 LINK SG CYS A 50 FE3 SF4 A 74 1555 1555 2.02 LINK SG CYS A 66 FE4 SF4 A 74 1555 1555 2.03 SITE 1 AC1 6 CYS A 33 CYS A 36 CYS A 50 CYS A 66 SITE 2 AC1 6 VAL A 68 TYR A 69 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