HEADER ELECTRON TRANSPORT 15-JUN-15 2N3Y
TITLE NMR STRUCTURE OF THE Y48PCMF VARIANT OF HUMAN CYTOCHROME C IN ITS
TITLE 2 REDUCED STATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME C;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: CYCS, CYC;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PCCY48AMBER
KEYWDS CYTOCHROME C, HEMEPROTEIN, MITOCHONDRIA, APOPTOSIS, PHOSPHORYLATION,
KEYWDS 2 ELECTRON TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR B.MORENO-BELTRAN,R.DEL CONTE,A.DIAZ-QUINTANA,M.A.DE LA ROSA,P.TURANO,
AUTHOR 2 I.DIAZ-MORENO
REVDAT 4 26-APR-17 2N3Y 1 JRNL
REVDAT 3 19-APR-17 2N3Y 1 JRNL
REVDAT 2 29-MAR-17 2N3Y 1 JRNL
REVDAT 1 14-DEC-16 2N3Y 0
JRNL AUTH B.MORENO-BELTRAN,A.GUERRA-CASTELLANO,A.DIAZ-QUINTANA,
JRNL AUTH 2 R.DEL CONTE,S.M.GARCIA-MAURINO,S.DIAZ-MORENO,
JRNL AUTH 3 K.GONZALEZ-ARZOLA,C.SANTOS-OCANA,A.VELAZQUEZ-CAMPOY,
JRNL AUTH 4 M.A.DE LA ROSA,P.TURANO,I.DIAZ-MORENO
JRNL TITL STRUCTURAL BASIS OF MITOCHONDRIAL DYSFUNCTION IN RESPONSE TO
JRNL TITL 2 CYTOCHROME C PHOSPHORYLATION AT TYROSINE 48.
JRNL REF PROC. NATL. ACAD. SCI. V. 114 E3041 2017
JRNL REF 2 U.S.A.
JRNL REFN ESSN 1091-6490
JRNL PMID 28348229
JRNL DOI 10.1073/PNAS.1618008114
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CYANA 2.1, AMBER, CYANA
REMARK 3 AUTHORS : GUNTERT, MUMENTHALER AND WUTHRICH (CYANA), CASE,
REMARK 3 DARDEN, CHEATHAM, III, SIMMERLING, WANG, DUKE, LUO,
REMARK 3 ... AND KOLLMAN (AMBER), GUNTERT, MUMENTHALER AND
REMARK 3 WUTHRICH (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: MOLECULAR DYNAMICS PERFORMED IN SOLVENT
REMARK 4
REMARK 4 2N3Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-JUN-15.
REMARK 100 THE DEPOSITION ID IS D_1000104391.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.3
REMARK 210 IONIC STRENGTH : 0.05
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.7 MM [U-99% 13C; U-99% 15N]
REMARK 210 CYTOCHROME C, 90% H2O/10% D2O;
REMARK 210 0.7 MM [U-99% 15N] CYTOCHROME C,
REMARK 210 90% H2O/10% D2O; 0.6 MM
REMARK 210 CYTOCHROME C, 90% H2O/10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC; 3D 1H-15N NOESY;
REMARK 210 2D 1H-13C HSQC; 2D 1H-1H NOESY;
REMARK 210 3D CBCA(CO)NH; 3D HNCO; 3D HNCA;
REMARK 210 3D HN(CO)CA; 3D HBHA(CO)NH; 3D
REMARK 210 HCCH-TOCSY; 2D 1H-1H COSY; 2D 1H-
REMARK 210 13C HSQC AROMATIC; 3D HNCACB; 3D
REMARK 210 1H-13C NOESY ALIPHATIC
REMARK 210 SPECTROMETER FIELD STRENGTH : 950 MHZ; 700 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : TOPSPIN, TALOS, CARA, XEASY
REMARK 210 METHOD USED : DISTANCE GEOMETRY, MOLECULAR
REMARK 210 DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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 ARG A 38 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 1 ARG A 91 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 2 ARG A 91 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 3 ARG A 91 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 5 ARG A 38 NE - CZ - NH1 ANGL. DEV. = 5.1 DEGREES
REMARK 500 5 ARG A 91 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 6 ARG A 38 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 6 ARG A 91 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 7 ARG A 38 NE - CZ - NH1 ANGL. DEV. = 5.2 DEGREES
REMARK 500 7 ARG A 91 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 8 ARG A 91 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 9 ARG A 38 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 9 ARG A 91 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 10 ARG A 38 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 10 ARG A 91 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 12 ARG A 38 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 12 ARG A 91 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 13 ARG A 38 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 14 ARG A 91 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 15 ARG A 91 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 16 ARG A 91 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 17 ARG A 38 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 17 ARG A 91 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 18 ARG A 38 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 19 ARG A 38 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 20 ARG A 91 NE - CZ - NH1 ANGL. DEV. = 4.4 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 CYS A 14 -41.01 -131.38
REMARK 500 1 THR A 40 -135.72 -111.56
REMARK 500 1 GLN A 42 -16.70 -157.29
REMARK 500 1 SER A 47 75.62 58.20
REMARK 500 1 ASN A 70 94.47 -161.47
REMARK 500 1 MET A 80 91.60 -66.05
REMARK 500 2 LEU A 32 -7.34 67.88
REMARK 500 2 THR A 40 -126.92 -123.72
REMARK 500 2 GLN A 42 -21.75 -152.56
REMARK 500 2 TYR A 46 -43.05 -131.25
REMARK 500 2 1PA A 48 -52.12 -133.13
REMARK 500 2 THR A 63 -36.94 -134.42
REMARK 500 2 ASN A 70 95.75 -163.83
REMARK 500 3 CYS A 14 -43.77 -131.47
REMARK 500 3 LYS A 27 -153.56 -144.09
REMARK 500 3 LEU A 32 -4.07 67.16
REMARK 500 3 THR A 40 -162.08 -125.81
REMARK 500 3 GLN A 42 -27.25 -151.04
REMARK 500 3 THR A 49 116.79 -162.01
REMARK 500 3 ASN A 70 90.06 -164.89
REMARK 500 3 MET A 80 96.61 -62.35
REMARK 500 4 LYS A 27 -164.38 -160.41
REMARK 500 4 THR A 40 -167.73 -128.17
REMARK 500 4 GLN A 42 -12.48 -152.84
REMARK 500 4 SER A 47 167.54 59.85
REMARK 500 4 ASN A 70 83.39 -157.68
REMARK 500 5 CYS A 17 -52.16 -133.38
REMARK 500 5 LYS A 27 -162.30 -167.60
REMARK 500 5 THR A 40 -127.77 -128.94
REMARK 500 5 GLN A 42 -12.46 -158.24
REMARK 500 5 SER A 47 168.58 58.09
REMARK 500 5 1PA A 48 -57.24 -133.82
REMARK 500 5 ASN A 70 92.62 -164.72
REMARK 500 6 THR A 40 -162.77 -109.55
REMARK 500 6 GLN A 42 -25.05 -153.84
REMARK 500 6 ASN A 70 86.83 -169.15
REMARK 500 6 MET A 80 91.72 -58.16
REMARK 500 7 CYS A 17 -55.68 -121.99
REMARK 500 7 VAL A 20 45.75 -141.07
REMARK 500 7 LEU A 32 -4.22 67.86
REMARK 500 7 ASN A 70 94.22 -162.54
REMARK 500 8 CYS A 17 -52.75 -131.73
REMARK 500 8 VAL A 20 57.53 -140.97
REMARK 500 8 LEU A 32 -2.93 68.24
REMARK 500 8 1PA A 48 -83.28 -126.65
REMARK 500 8 ASN A 54 33.47 -93.79
REMARK 500 8 TRP A 59 95.37 -61.03
REMARK 500 8 ASN A 70 91.74 -165.41
REMARK 500 9 LEU A 32 -1.14 67.28
REMARK 500 9 1PA A 48 -64.48 -143.50
REMARK 500
REMARK 500 THIS ENTRY HAS 133 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 HIS A 18 THR A 19 6 149.39
REMARK 500 ASN A 103 GLU A 104 6 -146.45
REMARK 500 ARG A 38 LYS A 39 7 144.79
REMARK 500 ARG A 38 LYS A 39 10 148.32
REMARK 500 LYS A 79 MET A 80 10 149.03
REMARK 500 LYS A 79 MET A 80 19 149.22
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 6 TYR A 67 0.09 SIDE CHAIN
REMARK 500 7 ARG A 91 0.11 SIDE CHAIN
REMARK 500 8 ARG A 38 0.09 SIDE CHAIN
REMARK 500 10 TYR A 67 0.08 SIDE CHAIN
REMARK 500 12 TYR A 67 0.09 SIDE CHAIN
REMARK 500 18 HIS A 26 0.10 SIDE CHAIN
REMARK 500 18 TYR A 46 0.08 SIDE CHAIN
REMARK 500 18 TYR A 74 0.07 SIDE CHAIN
REMARK 500 19 ARG A 91 0.10 SIDE CHAIN
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 MH0 A 201 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 18 NE2
REMARK 620 2 MH0 A 201 NB 88.4
REMARK 620 3 MH0 A 201 NC 87.7 91.2
REMARK 620 4 MH0 A 201 NA 90.9 92.9 175.6
REMARK 620 5 MH0 A 201 ND 89.4 177.0 86.7 89.1
REMARK 620 6 MET A 80 SD 173.8 89.2 86.7 94.9 92.8
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MH0 A 201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 18828 RELATED DB: BMRB
REMARK 900 NMR ASSIGNMENT OF ARABIDOPSIS THALIANA REDUCED CYTOCHROME C
REMARK 900 RELATED ID: 26578 RELATED DB: BMRB
REMARK 900 NMR ASSIGNMENT OF HOMO SAPIENS OXIDIZED CYTOCHROME C
REMARK 900 RELATED ID: 25660 RELATED DB: BMRB
DBREF 2N3Y A 1 104 UNP P99999 CYC_HUMAN 2 105
SEQADV 2N3Y 1PA A 48 UNP P99999 TYR 49 ENGINEERED MUTATION
SEQRES 1 A 104 GLY ASP VAL GLU LYS GLY LYS LYS ILE PHE ILE MET LYS
SEQRES 2 A 104 CYS SER GLN CYS HIS THR VAL GLU LYS GLY GLY LYS HIS
SEQRES 3 A 104 LYS THR GLY PRO ASN LEU HIS GLY LEU PHE GLY ARG LYS
SEQRES 4 A 104 THR GLY GLN ALA PRO GLY TYR SER 1PA THR ALA ALA ASN
SEQRES 5 A 104 LYS ASN LYS GLY ILE ILE TRP GLY GLU ASP THR LEU MET
SEQRES 6 A 104 GLU TYR LEU GLU ASN PRO LYS LYS TYR ILE PRO GLY THR
SEQRES 7 A 104 LYS MET ILE PHE VAL GLY ILE LYS LYS LYS GLU GLU ARG
SEQRES 8 A 104 ALA ASP LEU ILE ALA TYR LEU LYS LYS ALA THR ASN GLU
MODRES 2N3Y 1PA A 48 PHE 4-(CARBOXYMETHYL)-L-PHENYLALANINE
HET 1PA A 48 25
HET MH0 A 201 75
HETNAM 1PA 4-(CARBOXYMETHYL)-L-PHENYLALANINE
HETNAM MH0 MESOHEME
HETSYN 1PA P-(CARBOXYMETHYL)PHENYLALANINE
FORMUL 1 1PA C11 H13 N O4
FORMUL 2 MH0 C34 H36 FE N4 O4
HELIX 1 1 ASP A 2 CYS A 14 1 13
HELIX 2 2 ALA A 50 LYS A 55 1 6
HELIX 3 3 THR A 63 ASN A 70 1 8
HELIX 4 4 ASN A 70 ILE A 75 1 6
HELIX 5 5 LYS A 87 THR A 102 1 16
LINK C SER A 47 N 1PA A 48 1555 1555 1.34
LINK C 1PA A 48 N THR A 49 1555 1555 1.34
LINK NE2 HIS A 18 FE MH0 A 201 1555 1555 2.02
LINK SD MET A 80 FE MH0 A 201 1555 1555 2.48
LINK SG CYS A 14 CAB MH0 A 201 1555 1555 1.81
LINK SG CYS A 17 CAC MH0 A 201 1555 1555 1.82
SITE 1 AC1 15 LYS A 13 CYS A 14 CYS A 17 HIS A 18
SITE 2 AC1 15 THR A 28 PRO A 30 THR A 40 SER A 47
SITE 3 AC1 15 1PA A 48 THR A 49 TYR A 67 LYS A 79
SITE 4 AC1 15 MET A 80 ILE A 85 LEU A 94
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
(ATOM LINES ARE NOT SHOWN.)
END
