HEADER MEMBRANE PROTEIN 20-SEP-99 1QM1
TITLE HUMAN PRION PROTEIN FRAGMENT 90-230
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PRION PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 90-230;
COMPND 5 SYNONYM: PRP, MAJOR PRION PROTEIN, PRP27-30, PRP33-35C,
COMPND 6 (ASCR).PRP;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 ORGAN: BRAIN;
SOURCE 6 CELLULAR_LOCATION: EXTRACELLULAR;
SOURCE 7 GENE: PRNP;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 10 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 11 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM;
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PRSET A
KEYWDS MEMBRANE PROTEIN, GLYCOPROTEIN, GPI-ANCHOR,
KEYWDS 2 REPEAT, POLYMORPHISM, DISEASE MUTATION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR R.ZAHN,A.LIU,T.LUHRS,K.WUTHRICH
REVDAT 4 07-DEC-11 1QM1 1 HEADER COMPND KEYWDS JRNL
REVDAT 4 2 REMARK VERSN
REVDAT 3 24-FEB-09 1QM1 1 VERSN
REVDAT 2 28-FEB-02 1QM1 1 JRNL REMARK
REVDAT 1 16-DEC-99 1QM1 0
JRNL AUTH R.ZAHN,A.LIU,T.LUHRS,R.RIEK,C.VON SCHROETTER,F.LOPEZ GARCIA,
JRNL AUTH 2 M.BILLETER,L.CALZOLAI,G.WIDER,K.WUTHRICH
JRNL TITL NMR SOLUTION STRUCTURE OF THE HUMAN PRION PROTEIN.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 97 145 2000
JRNL REFN ISSN 0027-8424
JRNL PMID 10618385
JRNL DOI 10.1073/PNAS.97.1.145
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : OPALP
REMARK 3 AUTHORS : KORADI, BILLETER, GUNTERT
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1QM1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-SEP-99.
REMARK 100 THE PDBE ID CODE IS EBI-4130.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 4.5
REMARK 210 IONIC STRENGTH : 0.01
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 90% WATER / 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ
REMARK 210 SPECTROMETER MODEL : DRX750
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 19
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE
REMARK 210 SPECTROSCOPY ON 13C, 15N-LABELED PROTEIN
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-20
REMARK 465 RES C SSSEQI
REMARK 465 GLY A 88
REMARK 465 SER A 89
REMARK 465 GLY A 90
REMARK 465 GLN A 91
REMARK 465 GLY A 92
REMARK 465 GLY A 93
REMARK 465 GLY A 94
REMARK 465 THR A 95
REMARK 465 HIS A 96
REMARK 465 SER A 97
REMARK 465 GLN A 98
REMARK 465 TRP A 99
REMARK 465 ASN A 100
REMARK 465 LYS A 101
REMARK 465 PRO A 102
REMARK 465 SER A 103
REMARK 465 LYS A 104
REMARK 465 PRO A 105
REMARK 465 LYS A 106
REMARK 465 THR A 107
REMARK 465 ASN A 108
REMARK 465 MET A 109
REMARK 465 LYS A 110
REMARK 465 HIS A 111
REMARK 465 MET A 112
REMARK 465 ALA A 113
REMARK 465 GLY A 114
REMARK 465 ALA A 115
REMARK 465 ALA A 116
REMARK 465 ALA A 117
REMARK 465 ALA A 118
REMARK 465 GLY A 119
REMARK 465 ALA A 120
REMARK 465 VAL A 121
REMARK 465 VAL A 122
REMARK 465 GLY A 123
REMARK 465 GLY A 124
REMARK 465 GLY A 229
REMARK 465 SER A 230
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 VAL A 176 CG1 - CB - CG2 ANGL. DEV. = -11.2 DEGREES
REMARK 500 2 VAL A 209 CG1 - CB - CG2 ANGL. DEV. = -9.8 DEGREES
REMARK 500 3 ARG A 151 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 4 VAL A 176 CG1 - CB - CG2 ANGL. DEV. = -10.4 DEGREES
REMARK 500 5 ARG A 164 CD - NE - CZ ANGL. DEV. = 10.8 DEGREES
REMARK 500 5 ARG A 164 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 8 VAL A 176 CG1 - CB - CG2 ANGL. DEV. = -11.6 DEGREES
REMARK 500 8 VAL A 209 CG1 - CB - CG2 ANGL. DEV. = -9.8 DEGREES
REMARK 500 9 VAL A 176 CG1 - CB - CG2 ANGL. DEV. = -10.3 DEGREES
REMARK 500 10 VAL A 176 CG1 - CB - CG2 ANGL. DEV. = -11.6 DEGREES
REMARK 500 11 VAL A 176 CG1 - CB - CG2 ANGL. DEV. = -9.7 DEGREES
REMARK 500 12 VAL A 176 CG1 - CB - CG2 ANGL. DEV. = -10.5 DEGREES
REMARK 500 12 MET A 206 CA - CB - CG ANGL. DEV. = 10.9 DEGREES
REMARK 500 12 CYS A 214 CA - CB - SG ANGL. DEV. = 7.2 DEGREES
REMARK 500 13 ARG A 156 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 13 VAL A 176 CG1 - CB - CG2 ANGL. DEV. = -9.8 DEGREES
REMARK 500 14 VAL A 176 CG1 - CB - CG2 ANGL. DEV. = -11.3 DEGREES
REMARK 500 16 VAL A 176 CG1 - CB - CG2 ANGL. DEV. = -11.2 DEGREES
REMARK 500 17 THR A 188 CA - CB - CG2 ANGL. DEV. = 9.5 DEGREES
REMARK 500 18 ARG A 151 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 18 VAL A 176 CG1 - CB - CG2 ANGL. DEV. = -11.6 DEGREES
REMARK 500 19 ARG A 148 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 20 MET A 134 CG - SD - CE ANGL. DEV. = -9.7 DEGREES
REMARK 500 20 VAL A 176 CA - CB - CG2 ANGL. DEV. = 10.3 DEGREES
REMARK 500 20 VAL A 176 CG1 - CB - CG2 ANGL. DEV. = -11.1 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 PRO A 137 -160.87 -76.15
REMARK 500 1 ARG A 156 -103.41 -102.75
REMARK 500 1 TYR A 157 175.35 52.86
REMARK 500 1 TYR A 163 -158.59 -141.75
REMARK 500 1 ASP A 167 -67.94 -160.87
REMARK 500 1 GLN A 172 -101.96 -76.36
REMARK 500 2 TYR A 128 -103.63 35.44
REMARK 500 2 ILE A 138 91.98 41.20
REMARK 500 2 TYR A 157 162.55 -45.87
REMARK 500 2 ASN A 159 -12.78 -141.20
REMARK 500 2 MET A 166 104.64 -56.30
REMARK 500 2 GLU A 168 94.64 85.27
REMARK 500 2 SER A 170 -81.14 67.31
REMARK 500 2 GLN A 172 -72.65 -50.22
REMARK 500 3 MET A 134 47.97 -157.97
REMARK 500 3 SER A 135 -112.62 35.34
REMARK 500 3 ILE A 138 118.03 61.19
REMARK 500 3 ARG A 156 -104.42 -87.32
REMARK 500 3 TYR A 157 176.01 49.19
REMARK 500 3 MET A 166 91.06 -53.27
REMARK 500 4 TYR A 128 -163.53 -106.26
REMARK 500 4 ILE A 138 86.19 39.14
REMARK 500 4 ARG A 156 -105.33 -100.51
REMARK 500 4 TYR A 157 175.02 49.12
REMARK 500 4 ASN A 159 0.22 -64.87
REMARK 500 4 ASP A 167 -69.62 -149.11
REMARK 500 4 GLU A 168 -30.70 -142.03
REMARK 500 4 GLN A 172 -74.30 -38.19
REMARK 500 5 ILE A 138 88.21 54.13
REMARK 500 5 ASN A 159 -1.31 -145.13
REMARK 500 5 TYR A 163 -162.62 -164.81
REMARK 500 5 PRO A 165 -175.40 -65.49
REMARK 500 5 MET A 166 76.73 -56.24
REMARK 500 5 ASP A 167 -60.70 -124.82
REMARK 500 5 TYR A 169 136.57 75.83
REMARK 500 5 ASN A 171 148.15 85.13
REMARK 500 5 GLN A 172 -93.11 -65.93
REMARK 500 5 ARG A 220 -9.47 -56.07
REMARK 500 6 ILE A 138 82.57 55.80
REMARK 500 6 MET A 166 104.35 -34.94
REMARK 500 6 ASP A 167 -51.96 -142.61
REMARK 500 6 ASN A 171 -155.15 -162.81
REMARK 500 6 GLN A 172 -81.00 -119.88
REMARK 500 7 ILE A 138 70.39 55.49
REMARK 500 7 TYR A 157 175.14 -58.91
REMARK 500 7 ASN A 159 5.64 -64.92
REMARK 500 7 ASP A 167 -84.28 -152.70
REMARK 500 7 GLN A 172 -101.19 -98.57
REMARK 500 7 LYS A 194 23.15 -76.72
REMARK 500 8 ILE A 138 80.61 35.02
REMARK 500
REMARK 500 THIS ENTRY HAS 153 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 ASN A 171 GLN A 172 4 -146.72
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 150 0.07 SIDE CHAIN
REMARK 500 1 ARG A 151 0.09 SIDE CHAIN
REMARK 500 2 ARG A 148 0.10 SIDE CHAIN
REMARK 500 3 TYR A 150 0.07 SIDE CHAIN
REMARK 500 4 ARG A 136 0.09 SIDE CHAIN
REMARK 500 4 TYR A 150 0.07 SIDE CHAIN
REMARK 500 4 PHE A 198 0.08 SIDE CHAIN
REMARK 500 4 ARG A 208 0.12 SIDE CHAIN
REMARK 500 4 TYR A 218 0.07 SIDE CHAIN
REMARK 500 4 TYR A 226 0.09 SIDE CHAIN
REMARK 500 5 TYR A 150 0.11 SIDE CHAIN
REMARK 500 5 ARG A 208 0.07 SIDE CHAIN
REMARK 500 6 ARG A 136 0.09 SIDE CHAIN
REMARK 500 6 ARG A 164 0.09 SIDE CHAIN
REMARK 500 6 TYR A 169 0.10 SIDE CHAIN
REMARK 500 6 PHE A 198 0.08 SIDE CHAIN
REMARK 500 6 TYR A 218 0.07 SIDE CHAIN
REMARK 500 7 ARG A 151 0.09 SIDE CHAIN
REMARK 500 7 TYR A 162 0.08 SIDE CHAIN
REMARK 500 7 ARG A 208 0.09 SIDE CHAIN
REMARK 500 7 ARG A 228 0.10 SIDE CHAIN
REMARK 500 8 TYR A 225 0.08 SIDE CHAIN
REMARK 500 9 TYR A 157 0.08 SIDE CHAIN
REMARK 500 9 TYR A 163 0.09 SIDE CHAIN
REMARK 500 10 ARG A 220 0.09 SIDE CHAIN
REMARK 500 11 ARG A 151 0.08 SIDE CHAIN
REMARK 500 11 ARG A 156 0.11 SIDE CHAIN
REMARK 500 11 TYR A 226 0.10 SIDE CHAIN
REMARK 500 12 TYR A 163 0.07 SIDE CHAIN
REMARK 500 13 TYR A 163 0.08 SIDE CHAIN
REMARK 500 14 ARG A 156 0.11 SIDE CHAIN
REMARK 500 14 TYR A 226 0.07 SIDE CHAIN
REMARK 500 15 ARG A 136 0.09 SIDE CHAIN
REMARK 500 15 TYR A 157 0.09 SIDE CHAIN
REMARK 500 15 TYR A 169 0.08 SIDE CHAIN
REMARK 500 16 ARG A 136 0.09 SIDE CHAIN
REMARK 500 16 TYR A 150 0.11 SIDE CHAIN
REMARK 500 16 ARG A 151 0.08 SIDE CHAIN
REMARK 500 16 ARG A 164 0.08 SIDE CHAIN
REMARK 500 17 ARG A 148 0.09 SIDE CHAIN
REMARK 500 17 ARG A 151 0.13 SIDE CHAIN
REMARK 500 17 TYR A 163 0.09 SIDE CHAIN
REMARK 500 17 ARG A 228 0.08 SIDE CHAIN
REMARK 500 18 TYR A 169 0.09 SIDE CHAIN
REMARK 500 19 TYR A 128 0.11 SIDE CHAIN
REMARK 500 19 ARG A 136 0.08 SIDE CHAIN
REMARK 500 19 TYR A 150 0.09 SIDE CHAIN
REMARK 500 19 ARG A 164 0.20 SIDE CHAIN
REMARK 500 20 TYR A 169 0.07 SIDE CHAIN
REMARK 500 20 TYR A 226 0.11 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1AG2 RELATED DB: PDB
REMARK 900 PRION PROTEIN DOMAIN PRP(121-231) FROM MOUSE, NMR,
REMARK 900 MINIMIZED AVERAGE STRUCTURE
REMARK 900 RELATED ID: 1QLZ RELATED DB: PDB
REMARK 900 HUMAN PRION PROTEIN NMR, 20 STRUCTURES, RESIDUES 23-230
REMARK 900 RELATED ID: 1QLX RELATED DB: PDB
REMARK 900 HUMAN PRION PROTEIN, NMR, REPRESENTATIVE STRUCTURE
REMARK 900 RESIDUES 23-230
REMARK 900 RELATED ID: 1QM0 RELATED DB: PDB
REMARK 900 HUMAN PRION PROTEIN FRAGMENT 90-230, NMR, REPRESENTATIVE
REMARK 900 STRUCTURE
REMARK 900 RELATED ID: 1QM2 RELATED DB: PDB
REMARK 900 HUMAN PRION PROTEIN FRAGMENT 121-230, NMR, REPRESENTATIVE
REMARK 900 STRUCTURE
REMARK 900 RELATED ID: 1QM3 RELATED DB: PDB
REMARK 900 HUMAN PRION PROTEIN FRAGMENT 121-230, NMR, 20 STRUCTURES
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 2 RESIDUES (GLY SER) INSERTED AT THE N-TERMINUS
DBREF 1QM1 A 90 230 UNP P04156 PRIO_HUMAN 90 230
SEQADV 1QM1 GLY A 88 UNP P04156 CLONING ARTIFACT
SEQADV 1QM1 SER A 89 UNP P04156 CLONING ARTIFACT
SEQRES 1 A 143 GLY SER GLY GLN GLY GLY GLY THR HIS SER GLN TRP ASN
SEQRES 2 A 143 LYS PRO SER LYS PRO LYS THR ASN MET LYS HIS MET ALA
SEQRES 3 A 143 GLY ALA ALA ALA ALA GLY ALA VAL VAL GLY GLY LEU GLY
SEQRES 4 A 143 GLY TYR MET LEU GLY SER ALA MET SER ARG PRO ILE ILE
SEQRES 5 A 143 HIS PHE GLY SER ASP TYR GLU ASP ARG TYR TYR ARG GLU
SEQRES 6 A 143 ASN MET HIS ARG TYR PRO ASN GLN VAL TYR TYR ARG PRO
SEQRES 7 A 143 MET ASP GLU TYR SER ASN GLN ASN ASN PHE VAL HIS ASP
SEQRES 8 A 143 CYS VAL ASN ILE THR ILE LYS GLN HIS THR VAL THR THR
SEQRES 9 A 143 THR THR LYS GLY GLU ASN PHE THR GLU THR ASP VAL LYS
SEQRES 10 A 143 MET MET GLU ARG VAL VAL GLU GLN MET CYS ILE THR GLN
SEQRES 11 A 143 TYR GLU ARG GLU SER GLN ALA TYR TYR GLN ARG GLY SER
HELIX 1 H1 ASP A 144 MET A 154 1 11
HELIX 2 H2 ASN A 173 LYS A 194 1 22
HELIX 3 H3 GLU A 200 ARG A 228 1 29
SHEET 1 S1 2 TYR A 128 GLY A 131 0
SHEET 2 S1 2 VAL A 161 ARG A 164 -1 N TYR A 128 O VAL A 161
SSBOND 1 CYS A 179 CYS A 214 1555 1555 2.06
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
