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HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 06-JUL-06 2DST
TITLE CRYSTAL STRUCTURE ANALYSIS OF TT1977
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYPOTHETICAL PROTEIN TTHA1544;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 3 ORGANISM_TAXID: 274;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET11A
KEYWDS CONSERVED HYPOTHETICAL PROTEIN, STRUCTURAL GENOMICS, NPPSFA,
KEYWDS 2 NATIONAL PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL
KEYWDS 3 ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE,
KEYWDS 4 RSGI, UNKNOWN FUNCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.XIE,S.KISHISHITA,K.MURAYAMA,M.SHIROUZU,L.CHEN,Z.J.LIU,
AUTHOR 2 B.C.WANG,RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE
AUTHOR 3 (RSGI)
REVDAT 4 09-JUN-09 2DST 1 REVDAT
REVDAT 3 24-FEB-09 2DST 1 VERSN
REVDAT 2 27-JAN-09 2DST 1 JRNL
REVDAT 1 06-JAN-07 2DST 0
JRNL AUTH Y.XIE,C.TAKEMOTO,S.KISHISHITA,T.UCHIKUBO-KAMO,
JRNL AUTH 2 K.MURAYAMA,L.CHEN,Z.J.LIU,B.C.WANG,M.MANZOKU,
JRNL AUTH 3 A.EBIHARA,S.KURAMITSU,M.SHIROUZU,S.YOKOYAMA
JRNL TITL STRUCTURE OF THE MINIMIZED ALPHA/BETA-HYDROLASE
JRNL TITL 2 FOLD PROTEIN FROM THERMUS THERMOPHILUS HB8.
JRNL REF ACTA CRYSTALLOGR.,SECT.F V. 63 993 2007
JRNL REFN ESSN 1744-3091
JRNL PMID 18084077
JRNL DOI 10.1107/S1744309107061106
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.68
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 741938.110
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 82.5
REMARK 3 NUMBER OF REFLECTIONS : 13671
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 SET) : 0.201
REMARK 3 FREE R VALUE : 0.245
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.700
REMARK 3 FREE R VALUE TEST SET COUNT : 1325
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.007
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.13
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 58.80
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1467
REMARK 3 BIN R VALUE (WORKING SET) : 0.2480
REMARK 3 BIN FREE R VALUE : 0.3200
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.60
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 156
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.026
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1858
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 146
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 7.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -7.81000
REMARK 3 B22 (A**2) : 24.44000
REMARK 3 B33 (A**2) : -16.63000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -4.95000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.24
REMARK 3 ESD FROM SIGMAA (A) : 0.27
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.31
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.35
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.011
REMARK 3 BOND ANGLES (DEGREES) : 1.60
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.70
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.02
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.420 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.190 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.280 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.010 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.35
REMARK 3 BSOL : 63.80
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2DST COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 10-JUL-06.
REMARK 100 THE RCSB ID CODE IS RCSB025802.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-APR-06; 16-FEB-06
REMARK 200 TEMPERATURE (KELVIN) : 100; 100
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : SPRING-8; APS
REMARK 200 BEAMLINE : BL26B1; 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000; 0.9724
REMARK 200 MONOCHROMATOR : SILICON; SILICON
REMARK 200 OPTICS : MIRRORS; MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU JUPITER 210; MARMOSAIC
REMARK 200 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15276
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.5
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06400
REMARK 200 FOR THE DATA SET : 20.4360
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 80.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : 0.15100
REMARK 200 R SYM FOR SHELL (I) : 0.15100
REMARK 200 FOR SHELL : 6.640
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.95
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1M 1,6-HEXANEDIOL, 0.1M NA ACETATE
REMARK 280 (PH 4.6), 0.005M COCL2, 10% GLYCEROL, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 32.91100
REMARK 290 SMTRY3 2 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: IN THIS CRYSTAL PACKING, IT LOOKS LIKE DIMER. BUT, THERE
REMARK 300 IS NO EXPERIMENTAL EVIDENCE.
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: DIMERIC
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 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 MET A 1
REMARK 465 ASN A 124
REMARK 465 ILE A 125
REMARK 465 ASP A 126
REMARK 465 LEU A 127
REMARK 465 GLY A 128
REMARK 465 GLY A 129
REMARK 465 ASN A 130
REMARK 465 LEU A 131
REMARK 465 MET B 1
REMARK 465 ASN B 124
REMARK 465 ILE B 125
REMARK 465 ASP B 126
REMARK 465 LEU B 127
REMARK 465 GLY B 128
REMARK 465 GLY B 129
REMARK 465 ASN B 130
REMARK 465 LEU B 131
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 VAL B 19 144.49 -177.67
REMARK 500 LEU B 120 -62.88 171.21
REMARK 500 TYR B 122 70.00 9.83
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 139 DISTANCE = 5.30 ANGSTROMS
REMARK 525 HOH A 178 DISTANCE = 6.41 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2CYD RELATED DB: PDB
REMARK 900 31% AMINO ACID IDENTITY WITH THAT OF TT1977
REMARK 900 RELATED ID: TTK003001977.1 RELATED DB: TARGETDB
DBREF 2DST A 1 131 UNP Q5SI36 Q5SI36_THET8 1 131
DBREF 2DST B 1 131 UNP Q5SI36 Q5SI36_THET8 1 131
SEQRES 1 A 131 MET ARG ARG ALA GLY TYR LEU HIS LEU TYR GLY LEU ASN
SEQRES 2 A 131 LEU VAL PHE ASP ARG VAL GLY LYS GLY PRO PRO VAL LEU
SEQRES 3 A 131 LEU VAL ALA GLU GLU ALA SER ARG TRP PRO GLU ALA LEU
SEQRES 4 A 131 PRO GLU GLY TYR ALA PHE TYR LEU LEU ASP LEU PRO GLY
SEQRES 5 A 131 TYR GLY ARG THR GLU GLY PRO ARG MET ALA PRO GLU GLU
SEQRES 6 A 131 LEU ALA HIS PHE VAL ALA GLY PHE ALA VAL MET MET ASN
SEQRES 7 A 131 LEU GLY ALA PRO TRP VAL LEU LEU ARG GLY LEU GLY LEU
SEQRES 8 A 131 ALA LEU GLY PRO HIS LEU GLU ALA LEU GLY LEU ARG ALA
SEQRES 9 A 131 LEU PRO ALA GLU GLY VAL GLU VAL ALA GLU VAL LEU SER
SEQRES 10 A 131 SER LYS LEU SER TYR GLY ASN ILE ASP LEU GLY GLY ASN
SEQRES 11 A 131 LEU
SEQRES 1 B 131 MET ARG ARG ALA GLY TYR LEU HIS LEU TYR GLY LEU ASN
SEQRES 2 B 131 LEU VAL PHE ASP ARG VAL GLY LYS GLY PRO PRO VAL LEU
SEQRES 3 B 131 LEU VAL ALA GLU GLU ALA SER ARG TRP PRO GLU ALA LEU
SEQRES 4 B 131 PRO GLU GLY TYR ALA PHE TYR LEU LEU ASP LEU PRO GLY
SEQRES 5 B 131 TYR GLY ARG THR GLU GLY PRO ARG MET ALA PRO GLU GLU
SEQRES 6 B 131 LEU ALA HIS PHE VAL ALA GLY PHE ALA VAL MET MET ASN
SEQRES 7 B 131 LEU GLY ALA PRO TRP VAL LEU LEU ARG GLY LEU GLY LEU
SEQRES 8 B 131 ALA LEU GLY PRO HIS LEU GLU ALA LEU GLY LEU ARG ALA
SEQRES 9 B 131 LEU PRO ALA GLU GLY VAL GLU VAL ALA GLU VAL LEU SER
SEQRES 10 B 131 SER LYS LEU SER TYR GLY ASN ILE ASP LEU GLY GLY ASN
SEQRES 11 B 131 LEU
FORMUL 3 HOH *146(H2 O)
HELIX 1 1 GLU A 31 TRP A 35 5 5
HELIX 2 2 ALA A 62 MET A 77 1 16
HELIX 3 3 GLY A 88 ALA A 92 5 5
HELIX 4 4 LEU A 93 LEU A 100 1 8
HELIX 5 5 GLU A 111 TYR A 122 1 12
HELIX 6 6 GLU B 31 TRP B 35 5 5
HELIX 7 7 ALA B 62 MET B 77 1 16
HELIX 8 8 GLY B 88 ALA B 92 5 5
HELIX 9 9 LEU B 93 LEU B 100 1 8
HELIX 10 10 GLU B 111 LYS B 119 1 9
SHEET 1 A 6 ARG A 3 LEU A 9 0
SHEET 2 A 6 LEU A 12 VAL A 19 -1 O LEU A 12 N LEU A 9
SHEET 3 A 6 ALA A 44 ASP A 49 -1 O LEU A 47 N ASP A 17
SHEET 4 A 6 PRO A 24 ALA A 29 1 N VAL A 25 O ALA A 44
SHEET 5 A 6 TRP A 83 LEU A 86 1 O LEU A 85 N VAL A 28
SHEET 6 A 6 ALA A 104 PRO A 106 1 O LEU A 105 N VAL A 84
SHEET 1 B 6 ARG B 3 LEU B 9 0
SHEET 2 B 6 LEU B 12 VAL B 19 -1 O LEU B 12 N LEU B 9
SHEET 3 B 6 ALA B 44 LEU B 48 -1 O LEU B 47 N ASP B 17
SHEET 4 B 6 PRO B 24 VAL B 28 1 N LEU B 27 O TYR B 46
SHEET 5 B 6 TRP B 83 LEU B 86 1 O LEU B 85 N VAL B 28
SHEET 6 B 6 ALA B 104 PRO B 106 1 O LEU B 105 N VAL B 84
CRYST1 31.714 65.822 59.320 90.00 92.61 90.00 P 1 21 1 4
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 0.031532 0.000000 0.001437 0.00000
SCALE2 0.000000 0.015192 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016875 0.00000
TER 930 GLY A 123
TER 1860 GLY B 123
MASTER 273 0 0 10 12 0 0 6 2004 2 0 22
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