Header list of 1fhb.pdb file
Complete list - b 23 2 Bytes
HEADER ELECTRON TRANSPORT 16-JUN-95 1FHB TITLE THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE CYANIDE ADDUCT OF A TITLE 2 MET80ALA VARIANT OF SACCHAROMYCES CEREVISIAE ISO-1-CYTOCHROME C. TITLE 3 IDENTIFICATION OF LIGAND-RESIDUE INTERACTIONS IN THE DISTAL HEME TITLE 4 CAVITY COMPND MOL_ID: 1; COMPND 2 MOLECULE: FERRICYTOCHROME C; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: MET80ALA-ISO-1-FERRICYTOCHROME C (ISOZYME 1); COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES; COMPND 7 OTHER_DETAILS: CYANIDE ADDUCT OF ALA 80, ISOZYME 1, OXIDIZED FORM SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE; SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST; SOURCE 4 ORGANISM_TAXID: 4932; SOURCE 5 STRAIN: GM3C2; SOURCE 6 VARIANT: H39Q, M80A, C102S; SOURCE 7 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE; SOURCE 8 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST; SOURCE 9 EXPRESSION_SYSTEM_TAXID: 4932; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: YEP213-LEU58HISCYC1; SOURCE 11 EXPRESSION_SYSTEM_GENE: YEAST ISO-1-CYTOCHROME C (CYC1) KEYWDS ELECTRON TRANSPORT EXPDTA SOLUTION NMR NUMMDL 17 AUTHOR L.BANCI,I.BERTINI,K.L.BREN,H.B.GRAY,P.SOMPORNPISUT,P.TURANO REVDAT 3 23-FEB-22 1FHB 1 REMARK SEQADV LINK REVDAT 2 24-FEB-09 1FHB 1 VERSN REVDAT 1 15-SEP-95 1FHB 0 JRNL AUTH L.BANCI,I.BERTINI,K.L.BREN,H.B.GRAY,P.SOMPORNPISUT,P.TURANO JRNL TITL THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE CYANIDE ADDUCT JRNL TITL 2 OF A MET80ALA VARIANT OF SACCHAROMYCES CEREVISIAE JRNL TITL 3 ISO-1-CYTOCHROME C. IDENTIFICATION OF LIGAND-RESIDUE JRNL TITL 4 INTERACTIONS IN THE DISTAL HEME CAVITY JRNL REF BIOCHEMISTRY V. 34 11385 1995 JRNL REFN ISSN 0006-2960 JRNL PMID 7547866 JRNL DOI 10.1021/BI00036A011 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH K.L.BREN,H.B.GRAY,L.BANCI,I.BERTINI,P.TURANO REMARK 1 TITL PARAMAGNETIC 1H NMR SPECTROSCOPY OF THE CYANIDE DERIVATIVE REMARK 1 TITL 2 OF MET80ALA-ISO-1-CYTOCHROME C REMARK 1 REF TO BE PUBLISHED REMARK 1 REFN REMARK 1 REFERENCE 2 REMARK 1 AUTH Y.LU,D.R.CASIMILO,K.L.BREN,J.H.RICHARDS,H.B.GRAY REMARK 1 TITL STRUCTURALLY ENGINEERED CYTOCHROMES WITH UNUSUAL REMARK 1 TITL 2 LIGAND-BINDING PROPERTIES: EXPRESSION OF SACCHAROMYCES REMARK 1 TITL 3 CEREVISIAE MET80-->ALA ISO-1-CYTOCHROME C REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 90 11456 1993 REMARK 1 REFN ISSN 0027-8424 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DIANA, AMBER 4.0 REMARK 3 AUTHORS : GUENTERT,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 1FHB 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_1000173286. 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 : 17 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 SG CYS A 14 CAB HEM A 104 1.82 REMARK 500 SG CYS A 17 CAC HEM A 104 1.82 REMARK 500 C CYN A 105 FE HEM A 104 1.86 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 2 TYR A 48 CB - CG - CD2 ANGL. DEV. = -5.5 DEGREES REMARK 500 3 TYR A 48 CB - CG - CD2 ANGL. DEV. = -5.9 DEGREES REMARK 500 4 TYR A 48 CB - CG - CD2 ANGL. DEV. = -4.0 DEGREES REMARK 500 5 TYR A 48 CB - CG - CD2 ANGL. DEV. = -4.7 DEGREES REMARK 500 6 TYR A 48 CB - CG - CD2 ANGL. DEV. = -5.3 DEGREES REMARK 500 7 TYR A 48 CB - CG - CD2 ANGL. DEV. = -6.4 DEGREES REMARK 500 10 TYR A 48 CB - CG - CD2 ANGL. DEV. = -6.3 DEGREES REMARK 500 11 TYR A 48 CB - CG - CD2 ANGL. DEV. = -4.9 DEGREES REMARK 500 11 GLU A 103 CA - C - O ANGL. DEV. = -38.6 DEGREES REMARK 500 12 TYR A 48 CB - CG - CD2 ANGL. DEV. = -4.8 DEGREES REMARK 500 13 TYR A 48 CB - CG - CD2 ANGL. DEV. = -5.0 DEGREES REMARK 500 15 TYR A 48 CB - CG - CD2 ANGL. DEV. = -5.0 DEGREES REMARK 500 16 TYR A 48 CB - CG - CD2 ANGL. DEV. = -6.1 DEGREES REMARK 500 17 TYR A 48 CB - CG - CD2 ANGL. DEV. = -6.2 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 LYS A 5 -54.86 76.32 REMARK 500 1 LYS A 27 -84.13 -58.79 REMARK 500 1 PRO A 30 -177.31 -66.93 REMARK 500 1 SER A 47 82.31 -69.49 REMARK 500 1 ASN A 56 106.10 -28.46 REMARK 500 1 ASN A 70 63.99 -159.42 REMARK 500 1 ALA A 80 77.44 -66.56 REMARK 500 1 LEU A 85 90.68 -65.73 REMARK 500 1 GLU A 88 -47.13 81.93 REMARK 500 2 LYS A 5 -54.95 76.71 REMARK 500 2 ARG A 13 -71.62 -142.04 REMARK 500 2 LYS A 27 -110.59 -89.11 REMARK 500 2 PHE A 36 86.90 -67.28 REMARK 500 2 LYS A 55 44.36 -103.70 REMARK 500 2 ASN A 56 107.45 -41.28 REMARK 500 2 TRP A 59 63.83 60.93 REMARK 500 2 ALA A 80 88.26 -61.51 REMARK 500 2 LEU A 85 54.30 -118.26 REMARK 500 2 GLU A 88 -39.30 77.16 REMARK 500 3 ALA A 3 -60.60 64.85 REMARK 500 3 LYS A 4 -175.17 -69.56 REMARK 500 3 LYS A 5 -60.96 73.64 REMARK 500 3 ARG A 13 -76.54 -140.57 REMARK 500 3 LYS A 27 -98.18 -76.32 REMARK 500 3 PHE A 36 98.95 -66.06 REMARK 500 3 GLU A 44 162.77 -49.00 REMARK 500 3 LYS A 55 49.29 -89.18 REMARK 500 3 ASN A 56 74.23 -55.18 REMARK 500 3 ASN A 70 80.47 -164.43 REMARK 500 3 ALA A 80 86.94 -68.57 REMARK 500 3 GLU A 88 -44.59 84.34 REMARK 500 4 LYS A 5 -53.21 72.61 REMARK 500 4 LYS A 27 -94.11 -62.77 REMARK 500 4 LEU A 32 42.11 -87.99 REMARK 500 4 PHE A 36 107.62 -58.29 REMARK 500 4 ARG A 38 -110.17 -86.75 REMARK 500 4 GLU A 44 -120.90 -89.97 REMARK 500 4 LYS A 55 35.14 -96.08 REMARK 500 4 ASN A 56 102.07 -39.47 REMARK 500 4 TRP A 59 76.14 67.11 REMARK 500 4 ASN A 70 87.52 -170.13 REMARK 500 4 ALA A 81 103.29 -164.08 REMARK 500 4 LYS A 87 -58.73 -11.07 REMARK 500 4 GLU A 88 -44.31 80.54 REMARK 500 5 PHE A -3 87.58 -67.21 REMARK 500 5 SER A 2 -163.08 -79.40 REMARK 500 5 LYS A 5 -61.89 94.89 REMARK 500 5 ARG A 13 -58.00 -133.57 REMARK 500 5 LYS A 27 -82.26 -54.58 REMARK 500 5 GLU A 44 -73.97 -105.97 REMARK 500 REMARK 500 THIS ENTRY HAS 190 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 TYR A 48 0.17 SIDE CHAIN REMARK 500 1 TYR A 67 0.09 SIDE CHAIN REMARK 500 1 PHE A 82 0.10 SIDE CHAIN REMARK 500 2 HIS A 33 0.10 SIDE CHAIN REMARK 500 2 TYR A 67 0.12 SIDE CHAIN REMARK 500 2 TYR A 74 0.09 SIDE CHAIN REMARK 500 2 PHE A 82 0.09 SIDE CHAIN REMARK 500 2 ARG A 91 0.11 SIDE CHAIN REMARK 500 2 TYR A 97 0.07 SIDE CHAIN REMARK 500 3 TYR A 48 0.16 SIDE CHAIN REMARK 500 3 TYR A 67 0.10 SIDE CHAIN REMARK 500 3 TYR A 97 0.06 SIDE CHAIN REMARK 500 4 ARG A 13 0.08 SIDE CHAIN REMARK 500 4 PHE A 36 0.09 SIDE CHAIN REMARK 500 4 TYR A 67 0.10 SIDE CHAIN REMARK 500 5 TYR A 67 0.10 SIDE CHAIN REMARK 500 5 TYR A 74 0.18 SIDE CHAIN REMARK 500 6 TYR A 48 0.15 SIDE CHAIN REMARK 500 6 TYR A 67 0.12 SIDE CHAIN REMARK 500 6 TYR A 74 0.07 SIDE CHAIN REMARK 500 6 ARG A 91 0.12 SIDE CHAIN REMARK 500 7 PHE A 10 0.08 SIDE CHAIN REMARK 500 7 TYR A 48 0.18 SIDE CHAIN REMARK 500 7 TYR A 67 0.13 SIDE CHAIN REMARK 500 8 TYR A 48 0.18 SIDE CHAIN REMARK 500 8 TYR A 67 0.09 SIDE CHAIN REMARK 500 8 PHE A 82 0.10 SIDE CHAIN REMARK 500 9 TYR A 48 0.16 SIDE CHAIN REMARK 500 9 TYR A 67 0.11 SIDE CHAIN REMARK 500 10 ARG A 38 0.08 SIDE CHAIN REMARK 500 10 TYR A 48 0.12 SIDE CHAIN REMARK 500 10 TYR A 67 0.10 SIDE CHAIN REMARK 500 10 TYR A 74 0.07 SIDE CHAIN REMARK 500 10 PHE A 82 0.13 SIDE CHAIN REMARK 500 11 PHE A 36 0.08 SIDE CHAIN REMARK 500 11 TYR A 48 0.10 SIDE CHAIN REMARK 500 11 TYR A 67 0.09 SIDE CHAIN REMARK 500 12 PHE A 10 0.08 SIDE CHAIN REMARK 500 12 TYR A 48 0.16 SIDE CHAIN REMARK 500 12 TYR A 67 0.08 SIDE CHAIN REMARK 500 12 TYR A 74 0.07 SIDE CHAIN REMARK 500 13 TYR A 48 0.13 SIDE CHAIN REMARK 500 13 TYR A 67 0.11 SIDE CHAIN REMARK 500 13 TYR A 74 0.09 SIDE CHAIN REMARK 500 13 ARG A 91 0.10 SIDE CHAIN REMARK 500 14 TYR A 48 0.17 SIDE CHAIN REMARK 500 14 TYR A 67 0.09 SIDE CHAIN REMARK 500 15 PHE A -3 0.08 SIDE CHAIN REMARK 500 15 ARG A 13 0.09 SIDE CHAIN REMARK 500 15 ARG A 38 0.09 SIDE CHAIN REMARK 500 REMARK 500 THIS ENTRY HAS 60 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 HEM A 104 FE REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS A 18 NE2 REMARK 620 2 HEM A 104 NA 89.7 REMARK 620 3 HEM A 104 NB 88.7 90.7 REMARK 620 4 HEM A 104 NC 92.2 177.7 90.5 REMARK 620 5 HEM A 104 ND 89.7 89.0 178.4 89.8 REMARK 620 N 1 2 3 4 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CYN A 105 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 104 DBREF 1FHB A -5 103 UNP P00044 CYC1_YEAST 1 108 SEQADV 1FHB GLN A 39 UNP P00044 HIS 44 CONFLICT SEQADV 1FHB ALA A 80 UNP P00044 MET 85 CONFLICT SEQADV 1FHB SER A 102 UNP P00044 CYS 107 CONFLICT SEQRES 1 A 108 THR GLU PHE LYS ALA GLY SER ALA LYS LYS GLY ALA THR SEQRES 2 A 108 LEU PHE LYS THR ARG CYS LEU GLN CYS HIS THR VAL GLU SEQRES 3 A 108 LYS GLY GLY PRO HIS LYS VAL GLY PRO ASN LEU HIS GLY SEQRES 4 A 108 ILE PHE GLY ARG GLN SER GLY GLN ALA GLU GLY TYR SER SEQRES 5 A 108 TYR THR ASP ALA ASN ILE LYS LYS ASN VAL LEU TRP ASP SEQRES 6 A 108 GLU ASN ASN MET SER GLU TYR LEU THR ASN PRO M3L LYS SEQRES 7 A 108 TYR ILE PRO GLY THR LYS ALA ALA PHE GLY GLY LEU LYS SEQRES 8 A 108 LYS GLU LYS ASP ARG ASN ASP LEU ILE THR TYR LEU LYS SEQRES 9 A 108 LYS ALA SER GLU MODRES 1FHB M3L A 72 LYS N-TRIMETHYLLYSINE HET M3L A 72 12 HET CYN A 105 2 HET HEM A 104 43 HETNAM M3L N-TRIMETHYLLYSINE HETNAM CYN CYANIDE ION HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE HETSYN HEM HEME FORMUL 1 M3L C9 H21 N2 O2 1+ FORMUL 2 CYN C N 1- FORMUL 3 HEM C34 H32 FE N4 O4 HELIX 1 1 GLY A 6 ARG A 13 1 8 HELIX 2 2 ASP A 50 LYS A 54 1 5 HELIX 3 3 GLU A 61 THR A 69 1 9 HELIX 4 4 PRO A 71 TYR A 74 1 4 HELIX 5 5 LYS A 89 ALA A 101 1 13 LINK C PRO A 71 N M3L A 72 1555 1555 1.33 LINK C M3L A 72 N LYS A 73 1555 1555 1.34 LINK NE2 HIS A 18 FE HEM A 104 1555 1555 1.96 SITE 1 AC1 4 TYR A 67 PRO A 71 ALA A 80 HEM A 104 SITE 1 AC2 27 ARG A 13 CYS A 14 GLN A 16 CYS A 17 SITE 2 AC2 27 HIS A 18 VAL A 28 GLY A 29 PRO A 30 SITE 3 AC2 27 LEU A 32 ILE A 35 SER A 40 GLY A 41 SITE 4 AC2 27 TYR A 46 THR A 49 ASN A 52 TRP A 59 SITE 5 AC2 27 MET A 64 TYR A 67 LEU A 68 GLY A 77 SITE 6 AC2 27 THR A 78 ALA A 80 PHE A 82 LEU A 85 SITE 7 AC2 27 LEU A 94 LEU A 98 CYN A 105 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 - b 23 2 Bytes