HEADER OXIDOREDUCTASE(SUPEROXIDE ACCEPTOR) 14-JUN-91 1SDY
TITLE STRUCTURE SOLUTION AND MOLECULAR DYNAMICS REFINEMENT OF THE YEAST CU,
TITLE 2 ZN ENZYME SUPEROXIDE DISMUTASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COPPER,ZINC SUPEROXIDE DISMUTASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 1.15.1.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932
KEYWDS OXIDOREDUCTASE(SUPEROXIDE ACCEPTOR)
EXPDTA X-RAY DIFFRACTION
AUTHOR K.DJINOVIC,G.GATTI,A.CODA,L.ANTOLINI,G.PELOSI,A.DESIDERI,M.FALCONI,
AUTHOR 2 F.MARMOCCHI,G.ROTILIO,M.BOLOGNESI
REVDAT 4 29-NOV-17 1SDY 1 REMARK HELIX
REVDAT 3 24-FEB-09 1SDY 1 VERSN
REVDAT 2 01-APR-03 1SDY 1 JRNL
REVDAT 1 31-JAN-94 1SDY 0
JRNL AUTH K.DJINOVIC,G.GATTI,A.CODA,L.ANTOLINI,G.PELOSI,A.DESIDERI,
JRNL AUTH 2 M.FALCONI,F.MARMOCCHI,G.ROLILIO,M.BOLOGNESI
JRNL TITL STRUCTURE SOLUTION AND MOLECULAR DYNAMICS REFINEMENT OF THE
JRNL TITL 2 YEAST CU,ZN ENZYME SUPEROXIDE DISMUTASE.
JRNL REF ACTA CRYSTALLOGR.,SECT.B V. 47 918 1991
JRNL REFN ISSN 0108-7681
JRNL PMID 1772629
JRNL DOI 10.1107/S0108768191004949
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH E.D.GETZOFF,J.A.TAINER,M.M.STEMPIEN,G.I.BELL,R.A.HALLEWELL
REMARK 1 TITL EVOLUTION OF CUZN SUPEROXIDE DISMUTASE AND THE GREEK KEY
REMARK 1 TITL 2 BETA-BARREL STRUCTURAL MOTIF
REMARK 1 REF PROTEINS V. 5 322 1989
REMARK 1 REFN ISSN 0887-3585
REMARK 1 REFERENCE 2
REMARK 1 AUTH A.DESIDERI,M.FALCONI,V.PARISI,G.ROTILIO
REMARK 1 TITL CONSERVATION OF LOCAL ELECTRIC FIELDS IN THE EVOLUTION OF
REMARK 1 TITL 2 CU,ZN SUPEROXIDE DISMUTASE
REMARK 1 REF FEBS LETT. V. 250 45 1989
REMARK 1 REFN ISSN 0014-5793
REMARK 1 REFERENCE 3
REMARK 1 AUTH F.FRIGERIO,M.FALCONI,G.GATTI,M.BOLOGNESI,A.DESIDERI,
REMARK 1 AUTH 2 F.MARMOCCHI,G.ROTILIO
REMARK 1 TITL CRYSTALLOGRAPHIC CHARACTERIZATION AND THREE-DIMENSIONAL
REMARK 1 TITL 2 MODEL OF YEAST CU,ZN SUPEROXIDE DISMUTASE
REMARK 1 REF BIOCHEM.BIOPHYS.RES.COMMUN. V. 160 677 1989
REMARK 1 REFN ISSN 0006-291X
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : TNT
REMARK 3 AUTHORS : TRONRUD,TEN EYCK,MATTHEWS
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : NULL
REMARK 3
REMARK 3 USING DATA ABOVE SIGMA CUTOFF.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : 0.158
REMARK 3 R VALUE (WORKING SET) : NULL
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 USING ALL DATA, NO SIGMA CUTOFF.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4424
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 8
REMARK 3 SOLVENT ATOMS : 513
REMARK 3
REMARK 3 WILSON B VALUE (FROM FCALC, A**2) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. RMS WEIGHT COUNT
REMARK 3 BOND LENGTHS (A) : 0.016 ; NULL ; NULL
REMARK 3 BOND ANGLES (DEGREES) : 2.912 ; NULL ; NULL
REMARK 3 TORSION ANGLES (DEGREES) : 27.160; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 TRIGONAL CARBON PLANES (A) : 0.019 ; NULL ; NULL
REMARK 3 GENERAL PLANES (A) : 0.020 ; NULL ; NULL
REMARK 3 ISOTROPIC THERMAL FACTORS (A**2) : NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS (A) : 0.098 ; NULL ; NULL
REMARK 3
REMARK 3 INCORRECT CHIRAL-CENTERS (COUNT) : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 RESTRAINT LIBRARIES.
REMARK 3 STEREOCHEMISTRY : NULL
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1SDY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000176336.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 66.85
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.71
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 52.65000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 71.50000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 52.65000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 71.50000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
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 300 REMARK: THE TRANSFORMATION PRESENTED ON *MTRIX 1* RECORDS BELOW
REMARK 300 WILL YIELD APPROXIMATE COORDINATES FOR CHAIN *A* WHEN
REMARK 300 APPLIED TO CHAIN *B*. THE TRANSFORMATION PRESENTED ON
REMARK 300 *MTRIX 2* RECORDS BELOW WILL YIELD APPROXIMATE COORDINATES
REMARK 300 FOR CHAIN *C* WHEN APPLIED TO CHAIN *D*.
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLN A 3 OE1
REMARK 480 ALA A 23 CB
REMARK 480 SER A 25A CB OG
REMARK 480 GLU A 75 CD OE1 OE2
REMARK 480 ASP A 128 CB CG OD1 OD2
REMARK 480 THR A 129 N CA CB OG1 CG2
REMARK 480 GLU A 130 OE1 OE2
REMARK 480 LYS A 134 CD CE NZ
REMARK 480 LYS B 19 CD CE NZ
REMARK 480 GLU B 21 CD OE1 OE2
REMARK 480 GLU B 25 CG
REMARK 480 LYS B 66 CE NZ
REMARK 480 GLU B 89 CB CG CD OE1 OE2
REMARK 480 ASN B 90 CB
REMARK 480 LYS B 98 NZ
REMARK 480 ASN B 151 O OXT
REMARK 480 LYS C 66 NZ
REMARK 480 GLU C 75 CB CG CD OE1 OE2
REMARK 480 LYS C 86 CD
REMARK 480 SER C 96 OG
REMARK 480 LYS C 126 CE NZ
REMARK 480 ASP C 128 O CB CG OD1 OD2
REMARK 480 THR C 129 N CG2
REMARK 480 GLU C 130 CG
REMARK 480 LYS D 19 CD
REMARK 480 GLU D 25B OE2
REMARK 480 GLU D 75 CB CG CD OE1 OE2
REMARK 480 LYS D 86 CD CE NZ
REMARK 480 SER D 96 OG
REMARK 480 GLU D 130 CD OE1
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 VAL D 2 C GLN D 3 N 0.153
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 ARG A 41 NE - CZ - NH1 ANGL. DEV. = 7.0 DEGREES
REMARK 500 ARG A 41 NE - CZ - NH2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 ARG A 77 NE - CZ - NH2 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG A 141 NE - CZ - NH1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ARG A 141 NE - CZ - NH2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 ASN A 151 N - CA - CB ANGL. DEV. = 12.4 DEGREES
REMARK 500 THR B 28 CA - CB - CG2 ANGL. DEV. = -8.5 DEGREES
REMARK 500 ARG B 113 CD - NE - CZ ANGL. DEV. = 8.4 DEGREES
REMARK 500 ARG B 113 NE - CZ - NH1 ANGL. DEV. = 7.3 DEGREES
REMARK 500 ARG B 113 NE - CZ - NH2 ANGL. DEV. = -5.3 DEGREES
REMARK 500 SER B 114 CB - CA - C ANGL. DEV. = -11.9 DEGREES
REMARK 500 VAL C 17 CG1 - CB - CG2 ANGL. DEV. = -14.5 DEGREES
REMARK 500 ARG C 41 CD - NE - CZ ANGL. DEV. = 11.9 DEGREES
REMARK 500 ARG C 41 NE - CZ - NH1 ANGL. DEV. = 11.0 DEGREES
REMARK 500 ARG C 41 NE - CZ - NH2 ANGL. DEV. = -12.7 DEGREES
REMARK 500 ARG C 77 NE - CZ - NH2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 THR C 87 CA - CB - CG2 ANGL. DEV. = -9.0 DEGREES
REMARK 500 LEU C 101 CB - CG - CD2 ANGL. DEV. = -10.8 DEGREES
REMARK 500 PRO C 107 C - N - CA ANGL. DEV. = 11.3 DEGREES
REMARK 500 ARG C 141 NE - CZ - NH1 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ARG C 141 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 VAL D 2 O - C - N ANGL. DEV. = -19.3 DEGREES
REMARK 500 VAL D 17 CA - CB - CG1 ANGL. DEV. = 11.0 DEGREES
REMARK 500 ARG D 41 NE - CZ - NH1 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ARG D 41 NE - CZ - NH2 ANGL. DEV. = -6.5 DEGREES
REMARK 500 ARG D 77 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ARG D 77 NE - CZ - NH2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 ASP D 88 CB - CG - OD1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ARG D 113 NE - CZ - NH1 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG D 141 NE - CZ - NH1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 ARG D 141 NE - CZ - NH2 ANGL. DEV. = -4.2 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 LYS A 126 30.63 -99.62
REMARK 500 LYS B 67 -169.02 -111.48
REMARK 500 LEU B 124 22.99 44.91
REMARK 500 PRO B 140 -179.87 -64.63
REMARK 500 ARG B 141 78.97 -118.19
REMARK 500 ASN C 63 68.81 -151.62
REMARK 500 LYS C 66 41.99 38.87
REMARK 500 LEU C 124 16.06 55.19
REMARK 500 PRO C 140 174.02 -58.20
REMARK 500 PRO D 140 177.60 -56.40
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 VAL D 2 GLN D 3 149.77
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 VAL D 2 -18.48
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 CU A 152 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 154 O
REMARK 620 2 HIS A 44 ND1 120.3
REMARK 620 3 HIS A 61 NE2 73.3 78.7
REMARK 620 4 HIS A 46 NE2 88.0 148.2 98.0
REMARK 620 5 HIS A 118 NE2 83.2 90.4 143.7 108.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 153 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 78 ND1
REMARK 620 2 HIS A 61 ND1 104.4
REMARK 620 3 HIS A 69 ND1 129.3 112.8
REMARK 620 4 ASP A 81 OD1 110.7 104.0 92.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU B 152 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 61 NE2
REMARK 620 2 HIS B 46 NE2 95.5
REMARK 620 3 HIS B 44 ND1 84.1 143.0
REMARK 620 4 HIS B 118 NE2 155.8 104.0 88.8
REMARK 620 5 HOH B 154 O 76.0 103.8 111.8 85.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 153 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 78 ND1
REMARK 620 2 HIS B 69 ND1 121.3
REMARK 620 3 HIS B 61 ND1 107.0 103.7
REMARK 620 4 ASP B 81 OD1 115.0 96.0 113.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU C 152 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 44 ND1
REMARK 620 2 HIS C 46 NE2 139.5
REMARK 620 3 HOH C 154 O 124.0 89.6
REMARK 620 4 HIS C 118 NE2 98.7 101.3 93.3
REMARK 620 5 HIS C 61 NE2 79.0 90.0 75.6 164.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 153 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 61 ND1
REMARK 620 2 HIS C 78 ND1 111.1
REMARK 620 3 HIS C 69 ND1 110.7 126.2
REMARK 620 4 ASP C 81 OD1 102.3 107.8 94.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU D 152 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 46 NE2
REMARK 620 2 HIS D 118 NE2 109.6
REMARK 620 3 HOH D 154 O 103.7 77.0
REMARK 620 4 HIS D 61 NE2 93.4 149.9 78.9
REMARK 620 5 HIS D 44 ND1 140.0 96.3 111.6 76.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 153 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 78 ND1
REMARK 620 2 ASP D 81 OD1 103.6
REMARK 620 3 HIS D 61 ND1 115.0 110.2
REMARK 620 4 HIS D 69 ND1 124.7 91.6 108.2
REMARK 620 N 1 2 3
REMARK 650
REMARK 650 HELIX
REMARK 650 THE HELIX EXTENDS TO RESIDUE 129 AND TO RESIDUES 136, 137
REMARK 650 AND 138 WITH BETA-TURNS.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: A
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: B
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: C
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: D
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU A 152
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 153
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU B 152
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 153
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU C 152
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 153
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU D 152
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 153
DBREF 1SDY A 2 151 UNP P00445 SODC_YEAST 1 153
DBREF 1SDY B 2 151 UNP P00445 SODC_YEAST 1 153
DBREF 1SDY C 2 151 UNP P00445 SODC_YEAST 1 153
DBREF 1SDY D 2 151 UNP P00445 SODC_YEAST 1 153
SEQRES 1 A 153 VAL GLN ALA VAL ALA VAL LEU LYS GLY ASP ALA GLY VAL
SEQRES 2 A 153 SER GLY VAL VAL LYS PHE GLU GLN ALA SER GLU SER GLU
SEQRES 3 A 153 PRO THR THR VAL SER TYR GLU ILE ALA GLY ASN SER PRO
SEQRES 4 A 153 ASN ALA GLU ARG GLY PHE HIS ILE HIS GLU PHE GLY ASP
SEQRES 5 A 153 ALA THR ASN GLY CYS VAL SER ALA GLY PRO HIS PHE ASN
SEQRES 6 A 153 PRO PHE LYS LYS THR HIS GLY ALA PRO THR ASP GLU VAL
SEQRES 7 A 153 ARG HIS VAL GLY ASP MET GLY ASN VAL LYS THR ASP GLU
SEQRES 8 A 153 ASN GLY VAL ALA LYS GLY SER PHE LYS ASP SER LEU ILE
SEQRES 9 A 153 LYS LEU ILE GLY PRO THR SER VAL VAL GLY ARG SER VAL
SEQRES 10 A 153 VAL ILE HIS ALA GLY GLN ASP ASP LEU GLY LYS GLY ASP
SEQRES 11 A 153 THR GLU GLU SER LEU LYS THR GLY ASN ALA GLY PRO ARG
SEQRES 12 A 153 PRO ALA CYS GLY VAL ILE GLY LEU THR ASN
SEQRES 1 B 153 VAL GLN ALA VAL ALA VAL LEU LYS GLY ASP ALA GLY VAL
SEQRES 2 B 153 SER GLY VAL VAL LYS PHE GLU GLN ALA SER GLU SER GLU
SEQRES 3 B 153 PRO THR THR VAL SER TYR GLU ILE ALA GLY ASN SER PRO
SEQRES 4 B 153 ASN ALA GLU ARG GLY PHE HIS ILE HIS GLU PHE GLY ASP
SEQRES 5 B 153 ALA THR ASN GLY CYS VAL SER ALA GLY PRO HIS PHE ASN
SEQRES 6 B 153 PRO PHE LYS LYS THR HIS GLY ALA PRO THR ASP GLU VAL
SEQRES 7 B 153 ARG HIS VAL GLY ASP MET GLY ASN VAL LYS THR ASP GLU
SEQRES 8 B 153 ASN GLY VAL ALA LYS GLY SER PHE LYS ASP SER LEU ILE
SEQRES 9 B 153 LYS LEU ILE GLY PRO THR SER VAL VAL GLY ARG SER VAL
SEQRES 10 B 153 VAL ILE HIS ALA GLY GLN ASP ASP LEU GLY LYS GLY ASP
SEQRES 11 B 153 THR GLU GLU SER LEU LYS THR GLY ASN ALA GLY PRO ARG
SEQRES 12 B 153 PRO ALA CYS GLY VAL ILE GLY LEU THR ASN
SEQRES 1 C 153 VAL GLN ALA VAL ALA VAL LEU LYS GLY ASP ALA GLY VAL
SEQRES 2 C 153 SER GLY VAL VAL LYS PHE GLU GLN ALA SER GLU SER GLU
SEQRES 3 C 153 PRO THR THR VAL SER TYR GLU ILE ALA GLY ASN SER PRO
SEQRES 4 C 153 ASN ALA GLU ARG GLY PHE HIS ILE HIS GLU PHE GLY ASP
SEQRES 5 C 153 ALA THR ASN GLY CYS VAL SER ALA GLY PRO HIS PHE ASN
SEQRES 6 C 153 PRO PHE LYS LYS THR HIS GLY ALA PRO THR ASP GLU VAL
SEQRES 7 C 153 ARG HIS VAL GLY ASP MET GLY ASN VAL LYS THR ASP GLU
SEQRES 8 C 153 ASN GLY VAL ALA LYS GLY SER PHE LYS ASP SER LEU ILE
SEQRES 9 C 153 LYS LEU ILE GLY PRO THR SER VAL VAL GLY ARG SER VAL
SEQRES 10 C 153 VAL ILE HIS ALA GLY GLN ASP ASP LEU GLY LYS GLY ASP
SEQRES 11 C 153 THR GLU GLU SER LEU LYS THR GLY ASN ALA GLY PRO ARG
SEQRES 12 C 153 PRO ALA CYS GLY VAL ILE GLY LEU THR ASN
SEQRES 1 D 153 VAL GLN ALA VAL ALA VAL LEU LYS GLY ASP ALA GLY VAL
SEQRES 2 D 153 SER GLY VAL VAL LYS PHE GLU GLN ALA SER GLU SER GLU
SEQRES 3 D 153 PRO THR THR VAL SER TYR GLU ILE ALA GLY ASN SER PRO
SEQRES 4 D 153 ASN ALA GLU ARG GLY PHE HIS ILE HIS GLU PHE GLY ASP
SEQRES 5 D 153 ALA THR ASN GLY CYS VAL SER ALA GLY PRO HIS PHE ASN
SEQRES 6 D 153 PRO PHE LYS LYS THR HIS GLY ALA PRO THR ASP GLU VAL
SEQRES 7 D 153 ARG HIS VAL GLY ASP MET GLY ASN VAL LYS THR ASP GLU
SEQRES 8 D 153 ASN GLY VAL ALA LYS GLY SER PHE LYS ASP SER LEU ILE
SEQRES 9 D 153 LYS LEU ILE GLY PRO THR SER VAL VAL GLY ARG SER VAL
SEQRES 10 D 153 VAL ILE HIS ALA GLY GLN ASP ASP LEU GLY LYS GLY ASP
SEQRES 11 D 153 THR GLU GLU SER LEU LYS THR GLY ASN ALA GLY PRO ARG
SEQRES 12 D 153 PRO ALA CYS GLY VAL ILE GLY LEU THR ASN
HET CU A 152 1
HET ZN A 153 1
HET CU B 152 1
HET ZN B 153 1
HET CU C 152 1
HET ZN C 153 1
HET CU D 152 1
HET ZN D 153 1
HETNAM CU COPPER (II) ION
HETNAM ZN ZINC ION
FORMUL 5 CU 4(CU 2+)
FORMUL 6 ZN 4(ZN 2+)
FORMUL 13 HOH *513(H2 O)
HELIX 1 HAA GLU A 130 THR A 135 1SEE REMARK 5 6
HELIX 2 HAB GLU B 130 THR B 135 1SEE REMARK 5 6
HELIX 3 HAC GLU C 130 THR C 135 1SEE REMARK 5 6
HELIX 4 HAD GLU D 130 THR D 135 1SEE REMARK 5 6
SHEET 1 BGA 4 GLN A 3 LEU A 8 0
SHEET 2 BGA 4 SER A 15 GLU A 21 -1 O PHE A 20 N ALA A 4
SHEET 3 BGA 4 THR A 27 GLY A 35 -1 O THR A 28 N GLU A 21
SHEET 4 BGA 4 ALA A 93 ASP A 99 -1 O PHE A 97 N VAL A 29
SHEET 1 SMA 5 ASP A 81 LYS A 86 0
SHEET 2 SMA 5 GLU A 40 HIS A 46 -1 O ARG A 41 N VAL A 85
SHEET 3 SMA 5 SER A 114 ILE A 117 -1 O VAL A 116 N HIS A 44
SHEET 4 SMA 5 ALA A 143 LEU A 149 -1 O GLY A 145 N VAL A 115
SHEET 5 SMA 5 GLN A 3 LEU A 8 -1 O VAL A 5 N GLY A 148
SHEET 1 BGB 4 GLN B 3 LEU B 8 0
SHEET 2 BGB 4 SER B 15 GLU B 21 -1 O PHE B 20 N ALA B 4
SHEET 3 BGB 4 THR B 27 GLY B 35 -1 O THR B 28 N GLU B 21
SHEET 4 BGB 4 ALA B 93 ASP B 99 -1 O PHE B 97 N VAL B 29
SHEET 1 SMB 5 ASP B 81 LYS B 86 0
SHEET 2 SMB 5 GLU B 40 HIS B 46 -1 O ARG B 41 N VAL B 85
SHEET 3 SMB 5 SER B 114 ILE B 117 -1 O VAL B 116 N HIS B 44
SHEET 4 SMB 5 ALA B 143 LEU B 149 -1 O GLY B 145 N VAL B 115
SHEET 5 SMB 5 GLN B 3 LEU B 8 -1 O VAL B 5 N GLY B 148
SHEET 1 BGC 4 GLN C 3 LEU C 8 0
SHEET 2 BGC 4 SER C 15 GLU C 21 -1 O PHE C 20 N ALA C 4
SHEET 3 BGC 4 THR C 27 GLY C 35 -1 O THR C 28 N GLU C 21
SHEET 4 BGC 4 ALA C 93 ASP C 99 -1 O PHE C 97 N VAL C 29
SHEET 1 SMC 5 ASP C 81 LYS C 86 0
SHEET 2 SMC 5 GLU C 40 HIS C 46 -1 O ARG C 41 N VAL C 85
SHEET 3 SMC 5 SER C 114 ILE C 117 -1 O VAL C 116 N HIS C 44
SHEET 4 SMC 5 ALA C 143 LEU C 149 -1 O GLY C 145 N VAL C 115
SHEET 5 SMC 5 GLN C 3 LEU C 8 -1 O VAL C 5 N GLY C 148
SHEET 1 BGD 4 GLN D 3 LEU D 8 0
SHEET 2 BGD 4 SER D 15 GLU D 21 -1 O PHE D 20 N ALA D 4
SHEET 3 BGD 4 THR D 27 GLY D 35 -1 O THR D 28 N GLU D 21
SHEET 4 BGD 4 ALA D 93 ASP D 99 -1 O PHE D 97 N VAL D 29
SHEET 1 SMD 5 ASP D 81 LYS D 86 0
SHEET 2 SMD 5 GLU D 40 HIS D 46 -1 O ARG D 41 N VAL D 85
SHEET 3 SMD 5 SER D 114 ILE D 117 -1 O VAL D 116 N HIS D 44
SHEET 4 SMD 5 ALA D 143 LEU D 149 -1 O GLY D 145 N VAL D 115
SHEET 5 SMD 5 GLN D 3 LEU D 8 -1 O VAL D 5 N GLY D 148
SSBOND 1 CYS A 55 CYS A 144 1555 1555 2.03
SSBOND 2 CYS B 55 CYS B 144 1555 1555 2.04
SSBOND 3 CYS C 55 CYS C 144 1555 1555 2.08
SSBOND 4 CYS D 55 CYS D 144 1555 1555 2.04
LINK CU CU A 152 O HOH A 154 1555 1555 1.86
LINK CU CU A 152 ND1 HIS A 44 1555 1555 1.85
LINK CU CU A 152 NE2 HIS A 61 1555 1555 2.44
LINK CU CU A 152 NE2 HIS A 46 1555 1555 2.17
LINK CU CU A 152 NE2 HIS A 118 1555 1555 2.24
LINK ZN ZN A 153 ND1 HIS A 78 1555 1555 2.03
LINK ZN ZN A 153 ND1 HIS A 61 1555 1555 1.94
LINK ZN ZN A 153 ND1 HIS A 69 1555 1555 1.90
LINK ZN ZN A 153 OD1 ASP A 81 1555 1555 1.85
LINK CU CU B 152 NE2 HIS B 61 1555 1555 2.08
LINK CU CU B 152 NE2 HIS B 46 1555 1555 2.28
LINK CU CU B 152 ND1 HIS B 44 1555 1555 1.87
LINK CU CU B 152 NE2 HIS B 118 1555 1555 2.01
LINK CU CU B 152 O HOH B 154 1555 1555 2.06
LINK ZN ZN B 153 ND1 HIS B 78 1555 1555 2.03
LINK ZN ZN B 153 ND1 HIS B 69 1555 1555 1.92
LINK ZN ZN B 153 ND1 HIS B 61 1555 1555 2.03
LINK ZN ZN B 153 OD1 ASP B 81 1555 1555 2.02
LINK CU CU C 152 ND1 HIS C 44 1555 1555 1.91
LINK CU CU C 152 NE2 HIS C 46 1555 1555 2.30
LINK CU CU C 152 O HOH C 154 1555 1555 1.83
LINK CU CU C 152 NE2 HIS C 118 1555 1555 2.14
LINK CU CU C 152 NE2 HIS C 61 1555 1555 2.00
LINK ZN ZN C 153 ND1 HIS C 61 1555 1555 2.20
LINK ZN ZN C 153 ND1 HIS C 78 1555 1555 1.91
LINK ZN ZN C 153 ND1 HIS C 69 1555 1555 1.93
LINK ZN ZN C 153 OD1 ASP C 81 1555 1555 2.06
LINK CU CU D 152 NE2 HIS D 46 1555 1555 2.14
LINK CU CU D 152 NE2 HIS D 118 1555 1555 2.26
LINK CU CU D 152 O HOH D 154 1555 1555 2.37
LINK CU CU D 152 NE2 HIS D 61 1555 1555 2.16
LINK CU CU D 152 ND1 HIS D 44 1555 1555 1.82
LINK ZN ZN D 153 ND1 HIS D 78 1555 1555 1.91
LINK ZN ZN D 153 OD1 ASP D 81 1555 1555 1.79
LINK ZN ZN D 153 ND1 HIS D 61 1555 1555 1.96
LINK ZN ZN D 153 ND1 HIS D 69 1555 1555 2.13
SITE 1 A 9 HIS A 44 HIS A 46 HIS A 61 HIS A 118
SITE 2 A 9 HIS A 69 HIS A 78 ASP A 81 CU A 152
SITE 3 A 9 ZN A 153
SITE 1 B 9 HIS B 44 HIS B 46 HIS B 61 HIS B 118
SITE 2 B 9 HIS B 69 HIS B 78 ASP B 81 CU B 152
SITE 3 B 9 ZN B 153
SITE 1 C 9 HIS C 44 HIS C 46 HIS C 61 HIS C 118
SITE 2 C 9 HIS C 69 HIS C 78 ASP C 81 CU C 152
SITE 3 C 9 ZN C 153
SITE 1 D 9 HIS D 44 HIS D 46 HIS D 61 HIS D 118
SITE 2 D 9 HIS D 69 HIS D 78 ASP D 81 CU D 152
SITE 3 D 9 ZN D 153
SITE 1 AC1 5 HIS A 44 HIS A 46 HIS A 61 HIS A 118
SITE 2 AC1 5 HOH A 154
SITE 1 AC2 4 HIS A 61 HIS A 69 HIS A 78 ASP A 81
SITE 1 AC3 5 HIS B 44 HIS B 46 HIS B 61 HIS B 118
SITE 2 AC3 5 HOH B 154
SITE 1 AC4 4 HIS B 61 HIS B 69 HIS B 78 ASP B 81
SITE 1 AC5 5 HIS C 44 HIS C 46 HIS C 61 HIS C 118
SITE 2 AC5 5 HOH C 154
SITE 1 AC6 4 HIS C 61 HIS C 69 HIS C 78 ASP C 81
SITE 1 AC7 5 HIS D 44 HIS D 46 HIS D 61 HIS D 118
SITE 2 AC7 5 HOH D 154
SITE 1 AC8 4 HIS D 61 HIS D 69 HIS D 78 ASP D 81
CRYST1 105.300 143.000 62.100 90.00 90.00 90.00 P 21 21 2 16
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 0.009497 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006993 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016103 0.00000
MTRIX1 1 -0.608980 -0.793150 0.008050 66.12000 1
MTRIX2 1 -0.791750 0.608450 0.054010 32.64200 1
MTRIX3 1 -0.047740 0.026520 -0.998510 1.61800 1
MTRIX1 2 -0.982760 0.172050 -0.067710 12.74300 1
MTRIX2 2 0.147180 0.506310 -0.849700 31.96600 1
MTRIX3 2 -0.111910 -0.845020 -0.522900 59.01400 1
(ATOM LINES ARE NOT SHOWN.)
END
