HEADER HYDROLASE 02-OCT-06 2IL2
TITLE CRYSTAL STRUCTURE OF HUMAN RENIN COMPLEXED WITH INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RENIN;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ANGIOTENSINOGENASE;
COMPND 5 EC: 3.4.23.15;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 8 EXPRESSION_SYSTEM_CELL: OVARY
KEYWDS RENIN, INHIBITORS, DRUG DESIGN, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR I.MOCHALKIN
REVDAT 6 30-AUG-23 2IL2 1 REMARK
REVDAT 5 18-OCT-17 2IL2 1 REMARK
REVDAT 4 13-JUL-11 2IL2 1 VERSN
REVDAT 3 24-FEB-09 2IL2 1 VERSN
REVDAT 2 02-JAN-07 2IL2 1 JRNL
REVDAT 1 05-DEC-06 2IL2 0
JRNL AUTH R.W.SARVER,J.PEEVERS,W.L.CODY,F.L.CISKE,J.DYER,S.D.EMERSON,
JRNL AUTH 2 J.C.HAGADORN,D.D.HOLSWORTH,M.JALAIE,M.KAUFMAN,M.MASTRONARDI,
JRNL AUTH 3 P.MCCONNELL,N.A.POWELL,J.QUIN,C.A.VAN HUIS,E.ZHANG,
JRNL AUTH 4 I.MOCHALKIN
JRNL TITL BINDING THERMODYNAMICS OF SUBSTITUTED DIAMINOPYRIMIDINE
JRNL TITL 2 RENIN INHIBITORS.
JRNL REF ANAL.BIOCHEM. V. 360 30 2007
JRNL REFN ISSN 0003-2697
JRNL PMID 17113558
JRNL DOI 10.1016/J.AB.2006.10.017
REMARK 2
REMARK 2 RESOLUTION. 2.24 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.24
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 45166
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.208
REMARK 3 R VALUE (WORKING SET) : 0.206
REMARK 3 FREE R VALUE : 0.242
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2281
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.24
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.30
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3055
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.02
REMARK 3 BIN R VALUE (WORKING SET) : 0.3230
REMARK 3 BIN FREE R VALUE SET COUNT : 166
REMARK 3 BIN FREE R VALUE : 0.3820
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5212
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 101
REMARK 3 SOLVENT ATOMS : 242
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.97
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.244
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.199
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.146
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.297
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.953
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.940
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5446 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 3600 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7403 ; 1.411 ; 1.977
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8764 ; 0.884 ; 3.003
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 674 ; 7.584 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 224 ;34.472 ;24.196
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 866 ;16.160 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 20 ;20.333 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 814 ; 0.085 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6082 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1142 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 833 ; 0.191 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 3644 ; 0.188 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2598 ; 0.180 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 2902 ; 0.086 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 242 ; 0.129 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 24 ; 0.274 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 52 ; 0.295 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 16 ; 0.177 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 4266 ; 0.846 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1392 ; 0.119 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5396 ; 1.003 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2561 ; 1.585 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2007 ; 2.325 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A -2 A 335
REMARK 3 ORIGIN FOR THE GROUP (A): -29.6190 3.5720 -11.8910
REMARK 3 T TENSOR
REMARK 3 T11: -0.1035 T22: -0.1322
REMARK 3 T33: -0.2244 T12: 0.0330
REMARK 3 T13: 0.0344 T23: -0.0087
REMARK 3 L TENSOR
REMARK 3 L11: 2.0904 L22: 1.3826
REMARK 3 L33: 0.8378 L12: 1.0732
REMARK 3 L13: 0.4399 L23: 0.2925
REMARK 3 S TENSOR
REMARK 3 S11: 0.1464 S12: -0.2421 S13: 0.0532
REMARK 3 S21: 0.0852 S22: -0.1672 S23: 0.0467
REMARK 3 S31: -0.0889 S32: -0.1629 S33: 0.0207
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B -2 B 335
REMARK 3 ORIGIN FOR THE GROUP (A): -52.8230 -12.8220 -35.1220
REMARK 3 T TENSOR
REMARK 3 T11: -0.1890 T22: -0.0762
REMARK 3 T33: -0.1894 T12: -0.0446
REMARK 3 T13: 0.0114 T23: 0.0719
REMARK 3 L TENSOR
REMARK 3 L11: 1.2909 L22: 2.2840
REMARK 3 L33: 1.8717 L12: -0.6795
REMARK 3 L13: -0.0766 L23: 0.6876
REMARK 3 S TENSOR
REMARK 3 S11: 0.0710 S12: -0.0238 S13: -0.1185
REMARK 3 S21: 0.1526 S22: -0.0093 S23: 0.1720
REMARK 3 S31: 0.2626 S32: -0.3023 S33: -0.0618
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 401 A 401
REMARK 3 ORIGIN FOR THE GROUP (A): -24.8090 -2.2850 -10.2660
REMARK 3 T TENSOR
REMARK 3 T11: -0.0119 T22: -0.0208
REMARK 3 T33: -0.0188 T12: -0.0282
REMARK 3 T13: 0.0337 T23: 0.0279
REMARK 3 L TENSOR
REMARK 3 L11: 18.1908 L22: 6.2848
REMARK 3 L33: 25.6952 L12: -9.2382
REMARK 3 L13: 5.5401 L23: 0.7370
REMARK 3 S TENSOR
REMARK 3 S11: 0.0549 S12: -0.5931 S13: -1.2898
REMARK 3 S21: -0.0097 S22: 0.2503 S23: 0.9134
REMARK 3 S31: 1.0692 S32: -0.3536 S33: -0.3053
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 402 B 402
REMARK 3 RESIDUE RANGE : A 501 A 501
REMARK 3 ORIGIN FOR THE GROUP (A): -47.3100 -18.8210 -29.6350
REMARK 3 T TENSOR
REMARK 3 T11: 0.0218 T22: 0.0075
REMARK 3 T33: 0.0027 T12: 0.0255
REMARK 3 T13: 0.0084 T23: 0.0015
REMARK 3 L TENSOR
REMARK 3 L11: 11.1241 L22: 2.5538
REMARK 3 L33: 2.8292 L12: 2.5072
REMARK 3 L13: 4.6714 L23: -0.2486
REMARK 3 S TENSOR
REMARK 3 S11: 0.4582 S12: -0.9633 S13: -0.4694
REMARK 3 S21: -0.2344 S22: -0.2054 S23: 0.3581
REMARK 3 S31: 0.7524 S32: -0.6346 S33: -0.2528
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2IL2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-OCT-06.
REMARK 100 THE DEPOSITION ID IS D_1000039704.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JAN-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45325
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.240
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 7.300
REMARK 200 R MERGE (I) : 0.07300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.24
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.32
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.1
REMARK 200 DATA REDUNDANCY IN SHELL : 6.80
REMARK 200 R MERGE FOR SHELL (I) : 0.62700
REMARK 200 R SYM FOR SHELL (I) : 0.62700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.280
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 2IKO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.18
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10-20 % PEG 3350, 50 MM SODIUM CITRATE
REMARK 280 PH 4.5, 0.6 M NACL., VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290 5555 Z,X,Y
REMARK 290 6555 Z+1/2,-X+1/2,-Y
REMARK 290 7555 -Z+1/2,-X,Y+1/2
REMARK 290 8555 -Z,X+1/2,-Y+1/2
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z+1/2,-X+1/2
REMARK 290 11555 Y+1/2,-Z+1/2,-X
REMARK 290 12555 -Y+1/2,-Z,X+1/2
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 70.76650
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 70.76650
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 70.76650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 70.76650
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 70.76650
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 70.76650
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 70.76650
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 70.76650
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 70.76650
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 70.76650
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 70.76650
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 70.76650
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 70.76650
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 70.76650
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 70.76650
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 70.76650
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 70.76650
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 70.76650
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 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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 24710 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 71340 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 350 BIOMT1 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT1 3 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT3 3 1.000000 0.000000 0.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 LEU A -4
REMARK 465 THR A -3
REMARK 465 LEU B -4
REMARK 465 THR B -3
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 GLU B 18 CA CB CG CD OE1 OE2
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 ASN A 70 -66.47 -131.16
REMARK 500 SER A 207 56.72 -102.43
REMARK 500 SER A 208 126.99 -170.00
REMARK 500 CYS A 216 -166.97 -161.62
REMARK 500 ARG A 246 -166.70 -114.41
REMARK 500 ALA A 294 46.74 -89.46
REMARK 500 ASP B 12 12.37 56.52
REMARK 500 ASN B 70 -56.97 -129.42
REMARK 500 ARG B 134 44.88 37.53
REMARK 500 GLN B 165 50.03 -100.23
REMARK 500 SER B 207 79.58 -102.67
REMARK 500 SER B 208 117.56 158.31
REMARK 500 ARG B 246 -92.24 -60.70
REMARK 500 LEU B 247 -61.99 -120.98
REMARK 500 ALA B 294 40.61 -90.14
REMARK 500 ALA B 334 -128.84 96.23
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 GLY B 96 ILE B 97 149.72
REMARK 500 LEU B 333 ALA B 334 136.92
REMARK 500 ALA B 334 ARG B 335 -35.09
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LIX A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LIX B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT A 501
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2IKU RELATED DB: PDB
REMARK 900 RELATED ID: 2IKO RELATED DB: PDB
DBREF 2IL2 A -4 335 UNP P00797 RENI_HUMAN 67 406
DBREF 2IL2 B -4 335 UNP P00797 RENI_HUMAN 67 406
SEQRES 1 A 340 LEU THR LEU GLY ASN THR THR SER SER VAL ILE LEU THR
SEQRES 2 A 340 ASN TYR MET ASP THR GLN TYR TYR GLY GLU ILE GLY ILE
SEQRES 3 A 340 GLY THR PRO PRO GLN THR PHE LYS VAL VAL PHE ASP THR
SEQRES 4 A 340 GLY SER SER ASN VAL TRP VAL PRO SER SER LYS CYS SER
SEQRES 5 A 340 ARG LEU TYR THR ALA CYS VAL TYR HIS LYS LEU PHE ASP
SEQRES 6 A 340 ALA SER ASP SER SER SER TYR LYS HIS ASN GLY THR GLU
SEQRES 7 A 340 LEU THR LEU ARG TYR SER THR GLY THR VAL SER GLY PHE
SEQRES 8 A 340 LEU SER GLN ASP ILE ILE THR VAL GLY GLY ILE THR VAL
SEQRES 9 A 340 THR GLN MET PHE GLY GLU VAL THR GLU MET PRO ALA LEU
SEQRES 10 A 340 PRO PHE MET LEU ALA GLU PHE ASP GLY VAL VAL GLY MET
SEQRES 11 A 340 GLY PHE ILE GLU GLN ALA ILE GLY ARG VAL THR PRO ILE
SEQRES 12 A 340 PHE ASP ASN ILE ILE SER GLN GLY VAL LEU LYS GLU ASP
SEQRES 13 A 340 VAL PHE SER PHE TYR TYR ASN ARG ASP SER GLU ASN SER
SEQRES 14 A 340 GLN SER LEU GLY GLY GLN ILE VAL LEU GLY GLY SER ASP
SEQRES 15 A 340 PRO GLN HIS TYR GLU GLY ASN PHE HIS TYR ILE ASN LEU
SEQRES 16 A 340 ILE LYS THR GLY VAL TRP GLN ILE GLN MET LYS GLY VAL
SEQRES 17 A 340 SER VAL GLY SER SER THR LEU LEU CYS GLU ASP GLY CYS
SEQRES 18 A 340 LEU ALA LEU VAL ASP THR GLY ALA SER TYR ILE SER GLY
SEQRES 19 A 340 SER THR SER SER ILE GLU LYS LEU MET GLU ALA LEU GLY
SEQRES 20 A 340 ALA LYS LYS ARG LEU PHE ASP TYR VAL VAL LYS CYS ASN
SEQRES 21 A 340 GLU GLY PRO THR LEU PRO ASP ILE SER PHE HIS LEU GLY
SEQRES 22 A 340 GLY LYS GLU TYR THR LEU THR SER ALA ASP TYR VAL PHE
SEQRES 23 A 340 GLN GLU SER TYR SER SER LYS LYS LEU CYS THR LEU ALA
SEQRES 24 A 340 ILE HIS ALA MET ASP ILE PRO PRO PRO THR GLY PRO THR
SEQRES 25 A 340 TRP ALA LEU GLY ALA THR PHE ILE ARG LYS PHE TYR THR
SEQRES 26 A 340 GLU PHE ASP ARG ARG ASN ASN ARG ILE GLY PHE ALA LEU
SEQRES 27 A 340 ALA ARG
SEQRES 1 B 340 LEU THR LEU GLY ASN THR THR SER SER VAL ILE LEU THR
SEQRES 2 B 340 ASN TYR MET ASP THR GLN TYR TYR GLY GLU ILE GLY ILE
SEQRES 3 B 340 GLY THR PRO PRO GLN THR PHE LYS VAL VAL PHE ASP THR
SEQRES 4 B 340 GLY SER SER ASN VAL TRP VAL PRO SER SER LYS CYS SER
SEQRES 5 B 340 ARG LEU TYR THR ALA CYS VAL TYR HIS LYS LEU PHE ASP
SEQRES 6 B 340 ALA SER ASP SER SER SER TYR LYS HIS ASN GLY THR GLU
SEQRES 7 B 340 LEU THR LEU ARG TYR SER THR GLY THR VAL SER GLY PHE
SEQRES 8 B 340 LEU SER GLN ASP ILE ILE THR VAL GLY GLY ILE THR VAL
SEQRES 9 B 340 THR GLN MET PHE GLY GLU VAL THR GLU MET PRO ALA LEU
SEQRES 10 B 340 PRO PHE MET LEU ALA GLU PHE ASP GLY VAL VAL GLY MET
SEQRES 11 B 340 GLY PHE ILE GLU GLN ALA ILE GLY ARG VAL THR PRO ILE
SEQRES 12 B 340 PHE ASP ASN ILE ILE SER GLN GLY VAL LEU LYS GLU ASP
SEQRES 13 B 340 VAL PHE SER PHE TYR TYR ASN ARG ASP SER GLU ASN SER
SEQRES 14 B 340 GLN SER LEU GLY GLY GLN ILE VAL LEU GLY GLY SER ASP
SEQRES 15 B 340 PRO GLN HIS TYR GLU GLY ASN PHE HIS TYR ILE ASN LEU
SEQRES 16 B 340 ILE LYS THR GLY VAL TRP GLN ILE GLN MET LYS GLY VAL
SEQRES 17 B 340 SER VAL GLY SER SER THR LEU LEU CYS GLU ASP GLY CYS
SEQRES 18 B 340 LEU ALA LEU VAL ASP THR GLY ALA SER TYR ILE SER GLY
SEQRES 19 B 340 SER THR SER SER ILE GLU LYS LEU MET GLU ALA LEU GLY
SEQRES 20 B 340 ALA LYS LYS ARG LEU PHE ASP TYR VAL VAL LYS CYS ASN
SEQRES 21 B 340 GLU GLY PRO THR LEU PRO ASP ILE SER PHE HIS LEU GLY
SEQRES 22 B 340 GLY LYS GLU TYR THR LEU THR SER ALA ASP TYR VAL PHE
SEQRES 23 B 340 GLN GLU SER TYR SER SER LYS LYS LEU CYS THR LEU ALA
SEQRES 24 B 340 ILE HIS ALA MET ASP ILE PRO PRO PRO THR GLY PRO THR
SEQRES 25 B 340 TRP ALA LEU GLY ALA THR PHE ILE ARG LYS PHE TYR THR
SEQRES 26 B 340 GLU PHE ASP ARG ARG ASN ASN ARG ILE GLY PHE ALA LEU
SEQRES 27 B 340 ALA ARG
HET LIX A 401 44
HET CIT A 501 13
HET LIX B 402 44
HETNAM LIX N-[2-({2-AMINO-6-ETHYL-5-[4-(3-METHOXYPROPYL)-2,2-
HETNAM 2 LIX DIMETHYL-3-OXO-3,4-DIHYDRO-2H-1,4-BENZOXAZIN-6-
HETNAM 3 LIX YL]PYRIMIDIN-4-YL}AMINO)ETHYL]NAPHTHALENE-2-
HETNAM 4 LIX SULFONAMIDE
HETNAM CIT CITRIC ACID
FORMUL 3 LIX 2(C32 H38 N6 O5 S)
FORMUL 4 CIT C6 H8 O7
FORMUL 6 HOH *242(H2 O)
HELIX 1 1 TYR A 50 TYR A 55 1 6
HELIX 2 2 ASP A 60 SER A 64 5 5
HELIX 3 3 PRO A 110 MET A 115 1 6
HELIX 4 4 PHE A 127 VAL A 135 5 9
HELIX 5 5 PRO A 137 SER A 144 1 8
HELIX 6 6 ASP A 177 GLN A 179 5 3
HELIX 7 7 SER A 230 GLY A 242 1 13
HELIX 8 8 GLU A 256 LEU A 260 5 5
HELIX 9 9 THR A 275 VAL A 280 1 6
HELIX 10 10 GLY A 311 ARG A 316 1 6
HELIX 11 11 TYR B 50 TYR B 55 1 6
HELIX 12 12 ASP B 60 SER B 64 5 5
HELIX 13 13 PRO B 110 MET B 115 1 6
HELIX 14 14 PHE B 127 VAL B 135 5 9
HELIX 15 15 PRO B 137 GLN B 145 1 9
HELIX 16 16 ASP B 177 TYR B 181 5 5
HELIX 17 17 SER B 230 GLY B 242 1 13
HELIX 18 18 ASN B 255 LEU B 260 5 6
HELIX 19 19 THR B 275 VAL B 280 1 6
HELIX 20 20 GLY B 311 LYS B 317 1 7
SHEET 1 A 9 LYS A 68 TYR A 78 0
SHEET 2 A 9 GLY A 81 VAL A 94 -1 O VAL A 83 N LEU A 76
SHEET 3 A 9 GLN A 14 ILE A 21 -1 N GLY A 20 O THR A 93
SHEET 4 A 9 SER A 3 TYR A 10 -1 N THR A 8 O TYR A 16
SHEET 5 A 9 GLY A 169 LEU A 173 -1 O LEU A 173 N SER A 3
SHEET 6 A 9 VAL A 152 TYR A 157 -1 N TYR A 156 O GLN A 170
SHEET 7 A 9 PHE A 318 ASP A 323 -1 O PHE A 322 N PHE A 153
SHEET 8 A 9 ARG A 328 ALA A 334 -1 O GLY A 330 N GLU A 321
SHEET 9 A 9 TYR A 181 ASN A 189 -1 N ILE A 188 O ILE A 329
SHEET 1 B13 LYS A 68 TYR A 78 0
SHEET 2 B13 GLY A 81 VAL A 94 -1 O VAL A 83 N LEU A 76
SHEET 3 B13 ILE A 97 GLU A 108 -1 O GLU A 105 N PHE A 86
SHEET 4 B13 VAL A 39 PRO A 42 1 N VAL A 39 O GLY A 104
SHEET 5 B13 GLY A 121 GLY A 124 -1 O VAL A 122 N TRP A 40
SHEET 6 B13 GLN A 26 ASP A 33 1 N VAL A 31 O VAL A 123
SHEET 7 B13 GLN A 14 ILE A 21 -1 N ILE A 21 O GLN A 26
SHEET 8 B13 SER A 3 TYR A 10 -1 N THR A 8 O TYR A 16
SHEET 9 B13 GLY A 169 LEU A 173 -1 O LEU A 173 N SER A 3
SHEET 10 B13 VAL A 152 TYR A 157 -1 N TYR A 156 O GLN A 170
SHEET 11 B13 PHE A 318 ASP A 323 -1 O PHE A 322 N PHE A 153
SHEET 12 B13 ARG A 328 ALA A 334 -1 O GLY A 330 N GLU A 321
SHEET 13 B13 TYR A 181 ASN A 189 -1 N ILE A 188 O ILE A 329
SHEET 1 C 5 GLN A 197 MET A 200 0
SHEET 2 C 5 CYS A 216 VAL A 220 -1 O CYS A 216 N MET A 200
SHEET 3 C 5 TRP A 308 LEU A 310 1 O LEU A 310 N LEU A 219
SHEET 4 C 5 ILE A 227 GLY A 229 -1 N SER A 228 O ALA A 309
SHEET 5 C 5 ILE A 295 ALA A 297 1 O HIS A 296 N ILE A 227
SHEET 1 D 3 GLY A 202 VAL A 205 0
SHEET 2 D 3 ILE A 263 LEU A 267 -1 O HIS A 266 N GLY A 202
SHEET 3 D 3 LYS A 270 LEU A 274 -1 O LEU A 274 N ILE A 263
SHEET 1 E 3 LYS A 244 LYS A 245 0
SHEET 2 E 3 TYR A 250 LYS A 253 -1 O VAL A 251 N LYS A 244
SHEET 3 E 3 LEU A 290 THR A 292 -1 O CYS A 291 N VAL A 252
SHEET 1 F 9 LYS B 68 ARG B 77 0
SHEET 2 F 9 THR B 82 VAL B 94 -1 O VAL B 83 N LEU B 76
SHEET 3 F 9 GLN B 14 ILE B 21 -1 N GLY B 20 O THR B 93
SHEET 4 F 9 SER B 3 TYR B 10 -1 N THR B 8 O TYR B 16
SHEET 5 F 9 GLY B 169 LEU B 173 -1 O LEU B 173 N SER B 3
SHEET 6 F 9 VAL B 152 TYR B 157 -1 N TYR B 156 O GLN B 170
SHEET 7 F 9 PHE B 318 ASP B 323 -1 O PHE B 322 N PHE B 153
SHEET 8 F 9 ARG B 328 LEU B 333 -1 O GLY B 330 N GLU B 321
SHEET 9 F 9 GLU B 182 ASN B 189 -1 N ILE B 188 O ILE B 329
SHEET 1 G13 LYS B 68 ARG B 77 0
SHEET 2 G13 THR B 82 VAL B 94 -1 O VAL B 83 N LEU B 76
SHEET 3 G13 ILE B 97 GLU B 108 -1 O GLU B 105 N PHE B 86
SHEET 4 G13 VAL B 39 PRO B 42 1 N VAL B 39 O GLY B 104
SHEET 5 G13 GLY B 121 GLY B 124 -1 O VAL B 122 N TRP B 40
SHEET 6 G13 GLN B 26 ASP B 33 1 N VAL B 31 O VAL B 123
SHEET 7 G13 GLN B 14 ILE B 21 -1 N ILE B 21 O GLN B 26
SHEET 8 G13 SER B 3 TYR B 10 -1 N THR B 8 O TYR B 16
SHEET 9 G13 GLY B 169 LEU B 173 -1 O LEU B 173 N SER B 3
SHEET 10 G13 VAL B 152 TYR B 157 -1 N TYR B 156 O GLN B 170
SHEET 11 G13 PHE B 318 ASP B 323 -1 O PHE B 322 N PHE B 153
SHEET 12 G13 ARG B 328 LEU B 333 -1 O GLY B 330 N GLU B 321
SHEET 13 G13 GLU B 182 ASN B 189 -1 N ILE B 188 O ILE B 329
SHEET 1 H 5 GLN B 197 MET B 200 0
SHEET 2 H 5 CYS B 216 VAL B 220 -1 O CYS B 216 N MET B 200
SHEET 3 H 5 TRP B 308 LEU B 310 1 O LEU B 310 N LEU B 219
SHEET 4 H 5 ILE B 227 GLY B 229 -1 N SER B 228 O ALA B 309
SHEET 5 H 5 ILE B 295 ALA B 297 1 O HIS B 296 N ILE B 227
SHEET 1 I 3 VAL B 203 VAL B 205 0
SHEET 2 I 3 ILE B 263 LEU B 267 -1 O SER B 264 N SER B 204
SHEET 3 I 3 LYS B 270 LEU B 274 -1 O LEU B 274 N ILE B 263
SHEET 1 J 3 LYS B 244 LYS B 245 0
SHEET 2 J 3 TYR B 250 LYS B 253 -1 O VAL B 251 N LYS B 244
SHEET 3 J 3 LEU B 290 THR B 292 -1 O CYS B 291 N VAL B 252
SSBOND 1 CYS A 46 CYS A 53 1555 1555 2.02
SSBOND 2 CYS A 212 CYS A 216 1555 1555 2.04
SSBOND 3 CYS A 254 CYS A 291 1555 1555 2.03
SSBOND 4 CYS B 46 CYS B 53 1555 1555 2.03
SSBOND 5 CYS B 212 CYS B 216 1555 1555 2.04
SSBOND 6 CYS B 254 CYS B 291 1555 1555 2.05
CISPEP 1 THR A 23 PRO A 24 0 -5.90
CISPEP 2 LEU A 112 PRO A 113 0 3.90
CISPEP 3 PRO A 302 PRO A 303 0 6.70
CISPEP 4 GLY A 305 PRO A 306 0 -4.83
CISPEP 5 THR B 23 PRO B 24 0 0.39
CISPEP 6 LEU B 112 PRO B 113 0 -0.30
CISPEP 7 PRO B 302 PRO B 303 0 10.42
CISPEP 8 GLY B 305 PRO B 306 0 -4.67
SITE 1 AC1 19 THR A 13 GLN A 14 TYR A 15 VAL A 31
SITE 2 AC1 19 ASP A 33 GLY A 35 TYR A 78 SER A 79
SITE 3 AC1 19 THR A 80 PRO A 113 LEU A 116 VAL A 122
SITE 4 AC1 19 ASP A 221 THR A 222 GLY A 223 SER A 225
SITE 5 AC1 19 PHE A 248 HOH A 504 HOH A 608
SITE 1 AC2 19 THR B 13 GLN B 14 TYR B 15 VAL B 31
SITE 2 AC2 19 ASP B 33 GLY B 35 TYR B 78 SER B 79
SITE 3 AC2 19 THR B 80 ASP B 221 THR B 222 GLY B 223
SITE 4 AC2 19 ALA B 224 SER B 225 TYR B 226 HIS B 296
SITE 5 AC2 19 ALA B 297 MET B 298 HOH B 475
SITE 1 AC3 1 LEU A 116
CRYST1 141.533 141.533 141.533 90.00 90.00 90.00 P 21 3 24
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 0.007065 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007065 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007065 0.00000
(ATOM LINES ARE NOT SHOWN.)
END