HEADER ELECTRON TRANSPORT 10-FEB-03 1NX7
TITLE SOLUTION STRUCTURE OF OXIDIZED BOVINE MICROSOMAL CYTOCHROME B5
CAVEAT 1NX7 CHIRALITY ERROR AT THE CA CENTER OF ALA A 3
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME B5;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 3-84;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: JM83;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PUC19
KEYWDS FIVE HELIX, FIVE SHEET, HEME RING, ELECTRON TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR H.WU,Q.ZANG
REVDAT 4 23-FEB-22 1NX7 1 REMARK LINK
REVDAT 3 24-FEB-09 1NX7 1 VERSN
REVDAT 2 01-FEB-05 1NX7 1 JRNL
REVDAT 1 15-JUN-04 1NX7 0
JRNL AUTH Q.ZHANG,C.CAO,Z.Q.WANG,Y.H.WANG,H.WU,Z.X.HUANG
JRNL TITL THE COMPARATIVE STUDY ON THE SOLUTION STRUCTURES OF THE
JRNL TITL 2 OXIDIZED BOVINE MICROSOMAL CYTOCHROME B5 AND MUTANT V45H
JRNL REF PROTEIN SCI. V. 13 2161 2004
JRNL REFN ISSN 0961-8368
JRNL PMID 15273310
JRNL DOI 10.1110/PS.04721104
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA 1.5, AMBER 6.0
REMARK 3 AUTHORS : PETER GUNTERT (DYANA), PETER KOLLMAN (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURE ARE BASED ON A TOTAL OF
REMARK 3 1698 RESTRAINS, 1489 ARE NOE-DERIVED DISTANCE CONSTRAINTS AND
REMARK 3 209 PSEUDOCONTACT SHIFT CONSTRAINTS
REMARK 4
REMARK 4 1NX7 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-FEB-03.
REMARK 100 THE DEPOSITION ID IS D_1000018308.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300; 298
REMARK 210 PH : 7.00; 7.00
REMARK 210 IONIC STRENGTH : 25MM PHOSPHATE BUFFER; 25MM
REMARK 210 PHOSPHATE BUFFER
REMARK 210 PRESSURE : 1 ATM; 1 ATM
REMARK 210 SAMPLE CONTENTS : 3.0MM; 3.0MM
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D TOCSY, DQF-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : VNMR 6.1B, XEASY 1994
REMARK 210 METHOD USED : DISTANCE GEOMITRY
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (RES=RESIDUE NAME;
REMARK 470 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 470 MODELS 1-30
REMARK 470 RES CSSEQI ATOMS
REMARK 470 ARG A 84 C O
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 ASN A 16 N - CA - CB ANGL. DEV. = -13.2 DEGREES
REMARK 500 1 ARG A 84 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 1 ARG A 84 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 3 ASN A 16 N - CA - CB ANGL. DEV. = -11.5 DEGREES
REMARK 500 4 ARG A 68 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 5 ASN A 16 N - CA - CB ANGL. DEV. = -11.2 DEGREES
REMARK 500 5 ARG A 68 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 6 TYR A 27 CB - CG - CD2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 9 ASN A 16 N - CA - CB ANGL. DEV. = -11.4 DEGREES
REMARK 500 10 ASN A 16 N - CA - CB ANGL. DEV. = -11.2 DEGREES
REMARK 500 10 ARG A 68 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 12 ARG A 68 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 13 ASN A 16 N - CA - CB ANGL. DEV. = -11.5 DEGREES
REMARK 500 14 ARG A 47 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 16 LEU A 25 CB - CG - CD2 ANGL. DEV. = 11.2 DEGREES
REMARK 500 17 ASN A 16 N - CA - CB ANGL. DEV. = -11.9 DEGREES
REMARK 500 18 ASN A 16 N - CA - CB ANGL. DEV. = -11.5 DEGREES
REMARK 500 19 ASN A 16 N - CA - CB ANGL. DEV. = -11.8 DEGREES
REMARK 500 20 LEU A 25 CB - CG - CD1 ANGL. DEV. = 10.2 DEGREES
REMARK 500 20 ARG A 84 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 21 LEU A 25 CB - CG - CD1 ANGL. DEV. = 10.8 DEGREES
REMARK 500 21 ARG A 68 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 21 ARG A 68 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 23 ARG A 68 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 24 ASN A 16 N - CA - CB ANGL. DEV. = -11.6 DEGREES
REMARK 500 25 ASN A 16 N - CA - CB ANGL. DEV. = -11.0 DEGREES
REMARK 500 26 ARG A 47 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 28 ARG A 68 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 29 ARG A 68 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 30 ASN A 16 N - CA - CB ANGL. DEV. = -11.5 DEGREES
REMARK 500 30 ARG A 47 NE - CZ - NH1 ANGL. DEV. = 3.2 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 SER A 20 94.72 -40.54
REMARK 500 1 HIS A 26 69.61 63.50
REMARK 500 1 TYR A 27 -27.24 68.11
REMARK 500 1 LEU A 36 -55.58 -28.47
REMARK 500 1 GLU A 56 -75.10 -37.03
REMARK 500 1 HIS A 63 -110.66 64.09
REMARK 500 1 PRO A 81 -9.28 -58.22
REMARK 500 2 HIS A 15 69.45 -110.36
REMARK 500 2 ASN A 16 7.98 -162.50
REMARK 500 2 SER A 18 -65.58 -171.16
REMARK 500 2 HIS A 26 76.32 60.11
REMARK 500 2 TYR A 27 -38.80 75.99
REMARK 500 2 HIS A 80 131.33 -37.72
REMARK 500 2 PRO A 81 1.67 -64.27
REMARK 500 3 ASN A 16 11.19 -162.46
REMARK 500 3 SER A 18 -63.48 -173.19
REMARK 500 3 SER A 20 106.62 -52.24
REMARK 500 3 HIS A 26 78.76 60.64
REMARK 500 3 TYR A 27 24.48 48.31
REMARK 500 3 HIS A 63 -83.91 -147.29
REMARK 500 3 HIS A 80 134.23 -36.46
REMARK 500 3 PRO A 81 -5.50 -56.51
REMARK 500 4 HIS A 15 70.74 -109.05
REMARK 500 4 ASN A 16 30.96 -159.09
REMARK 500 4 SER A 18 -74.06 55.22
REMARK 500 4 SER A 20 100.05 -43.70
REMARK 500 4 TYR A 27 -26.87 67.42
REMARK 500 4 GLU A 56 -72.51 -37.79
REMARK 500 4 HIS A 63 130.62 -35.86
REMARK 500 4 HIS A 80 138.05 -39.01
REMARK 500 5 ASN A 16 25.99 -152.80
REMARK 500 5 LYS A 19 -71.63 168.59
REMARK 500 5 HIS A 26 72.72 60.04
REMARK 500 5 TYR A 27 -31.42 74.30
REMARK 500 5 VAL A 61 44.28 -88.13
REMARK 500 5 PRO A 81 2.34 -63.50
REMARK 500 6 HIS A 15 77.63 -100.60
REMARK 500 6 ASN A 16 21.70 -155.13
REMARK 500 6 LYS A 19 -52.67 -129.84
REMARK 500 6 TYR A 27 -24.86 67.33
REMARK 500 6 ASP A 31 57.28 -94.46
REMARK 500 6 LEU A 32 9.41 -68.67
REMARK 500 6 GLU A 56 -72.08 -36.62
REMARK 500 6 HIS A 80 130.79 -37.58
REMARK 500 7 HIS A 15 59.18 -100.56
REMARK 500 7 ASN A 17 -104.39 -148.33
REMARK 500 7 SER A 18 -72.26 -65.73
REMARK 500 7 SER A 20 108.51 -40.67
REMARK 500 7 HIS A 26 62.11 73.50
REMARK 500 7 TYR A 27 -25.30 66.22
REMARK 500
REMARK 500 THIS ENTRY HAS 226 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 7 0.12 SIDE CHAIN
REMARK 500 1 ARG A 84 0.13 SIDE CHAIN
REMARK 500 2 TYR A 6 0.13 SIDE CHAIN
REMARK 500 2 TYR A 7 0.07 SIDE CHAIN
REMARK 500 2 TYR A 27 0.11 SIDE CHAIN
REMARK 500 2 ARG A 47 0.11 SIDE CHAIN
REMARK 500 3 TYR A 6 0.17 SIDE CHAIN
REMARK 500 3 TYR A 7 0.09 SIDE CHAIN
REMARK 500 3 TYR A 30 0.09 SIDE CHAIN
REMARK 500 3 PHE A 58 0.10 SIDE CHAIN
REMARK 500 4 TYR A 7 0.10 SIDE CHAIN
REMARK 500 4 TYR A 27 0.11 SIDE CHAIN
REMARK 500 4 PHE A 58 0.13 SIDE CHAIN
REMARK 500 4 ARG A 68 0.08 SIDE CHAIN
REMARK 500 4 ARG A 84 0.11 SIDE CHAIN
REMARK 500 5 TYR A 7 0.12 SIDE CHAIN
REMARK 500 5 TYR A 27 0.09 SIDE CHAIN
REMARK 500 5 PHE A 58 0.14 SIDE CHAIN
REMARK 500 5 ARG A 68 0.09 SIDE CHAIN
REMARK 500 6 TYR A 7 0.09 SIDE CHAIN
REMARK 500 6 TYR A 30 0.13 SIDE CHAIN
REMARK 500 7 TYR A 7 0.09 SIDE CHAIN
REMARK 500 7 TYR A 27 0.14 SIDE CHAIN
REMARK 500 7 TYR A 30 0.09 SIDE CHAIN
REMARK 500 7 ARG A 47 0.13 SIDE CHAIN
REMARK 500 7 PHE A 58 0.15 SIDE CHAIN
REMARK 500 8 TYR A 7 0.10 SIDE CHAIN
REMARK 500 8 TYR A 30 0.10 SIDE CHAIN
REMARK 500 8 PHE A 58 0.08 SIDE CHAIN
REMARK 500 8 ARG A 84 0.08 SIDE CHAIN
REMARK 500 9 TYR A 7 0.09 SIDE CHAIN
REMARK 500 9 TYR A 27 0.08 SIDE CHAIN
REMARK 500 9 TYR A 30 0.09 SIDE CHAIN
REMARK 500 9 PHE A 58 0.11 SIDE CHAIN
REMARK 500 10 TYR A 6 0.14 SIDE CHAIN
REMARK 500 10 TYR A 7 0.09 SIDE CHAIN
REMARK 500 10 TYR A 27 0.12 SIDE CHAIN
REMARK 500 10 ARG A 68 0.11 SIDE CHAIN
REMARK 500 10 ARG A 84 0.14 SIDE CHAIN
REMARK 500 11 TYR A 7 0.09 SIDE CHAIN
REMARK 500 11 TYR A 30 0.13 SIDE CHAIN
REMARK 500 11 PHE A 58 0.14 SIDE CHAIN
REMARK 500 12 TYR A 6 0.11 SIDE CHAIN
REMARK 500 12 TYR A 7 0.10 SIDE CHAIN
REMARK 500 12 TYR A 27 0.08 SIDE CHAIN
REMARK 500 12 PHE A 58 0.10 SIDE CHAIN
REMARK 500 12 ARG A 84 0.10 SIDE CHAIN
REMARK 500 13 TYR A 6 0.15 SIDE CHAIN
REMARK 500 13 TYR A 7 0.10 SIDE CHAIN
REMARK 500 13 TYR A 27 0.09 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 111 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 201 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 39 NE2
REMARK 620 2 HEM A 201 NA 91.3
REMARK 620 3 HEM A 201 NB 92.1 90.2
REMARK 620 4 HEM A 201 NC 89.6 179.0 89.3
REMARK 620 5 HEM A 201 ND 88.1 91.3 178.5 89.2
REMARK 620 6 HIS A 63 NE2 176.2 89.6 91.6 89.5 88.2
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 HEM A 201
DBREF 1NX7 A 3 84 UNP P00171 CYB5_BOVIN 7 88
SEQRES 1 A 82 ALA VAL LYS TYR TYR THR LEU GLU GLU ILE GLN LYS HIS
SEQRES 2 A 82 ASN ASN SER LYS SER THR TRP LEU ILE LEU HIS TYR LYS
SEQRES 3 A 82 VAL TYR ASP LEU THR LYS PHE LEU GLU GLU HIS PRO GLY
SEQRES 4 A 82 GLY GLU GLU VAL LEU ARG GLU GLN ALA GLY GLY ASP ALA
SEQRES 5 A 82 THR GLU ASN PHE GLU ASP VAL GLY HIS SER THR ASP ALA
SEQRES 6 A 82 ARG GLU LEU SER LYS THR PHE ILE ILE GLY GLU LEU HIS
SEQRES 7 A 82 PRO ASP ASP ARG
HET HEM A 201 73
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETSYN HEM HEME
FORMUL 2 HEM C34 H32 FE N4 O4
HELIX 1 1 THR A 8 LYS A 14 1 7
HELIX 2 2 LYS A 34 HIS A 39 1 6
HELIX 3 3 GLU A 43 GLN A 49 1 7
HELIX 4 4 ALA A 54 GLY A 62 1 9
HELIX 5 5 SER A 64 LYS A 72 1 9
SHEET 1 A 5 LYS A 5 TYR A 7 0
SHEET 2 A 5 ILE A 75 LEU A 79 1 O GLU A 78 N TYR A 7
SHEET 3 A 5 LYS A 28 TYR A 30 -1 N VAL A 29 O ILE A 76
SHEET 4 A 5 LEU A 23 LEU A 25 -1 N LEU A 23 O TYR A 30
SHEET 5 A 5 GLY A 52 ASP A 53 1 O GLY A 52 N ILE A 24
LINK NE2 HIS A 39 FE HEM A 201 1555 1555 1.99
LINK NE2 HIS A 63 FE HEM A 201 1555 1555 2.00
SITE 1 AC1 15 LEU A 23 LEU A 32 PHE A 35 HIS A 39
SITE 2 AC1 15 PRO A 40 GLY A 41 VAL A 45 LEU A 46
SITE 3 AC1 15 GLN A 49 ASN A 57 PHE A 58 HIS A 63
SITE 4 AC1 15 SER A 64 ALA A 67 SER A 71
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
