| content |
HEADER HYDROLASE 31-MAY-11 3S8Y
TITLE BROMIDE SOAKED STRUCTURE OF AN ESTERASE FROM THE OIL-DEGRADING
TITLE 2 BACTERIUM OLEISPIRA ANTARCTICA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE APC40077;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.2;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: OLEISPIRA ANTARCTICA;
SOURCE 3 ORGANISM_TAXID: 188908;
SOURCE 4 GENE: OLEI01171;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: P15TV LIC
KEYWDS ROSSMANN FOLD, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.PETIT,A.DONG,O.KAGAN,A.SAVCHENKO,A.F.YAKUNIN
REVDAT 1 15-JUN-11 3S8Y 0
JRNL AUTH S.LEMAK,A.TCHIGVINTSEV,P.PETIT,A.U.SINGER,G.BROWN,
JRNL AUTH 2 E.EVDOKIMOVA,O.EGOROVA,R.FLICK,C.F.GONZALEZ,M.M.YAKIMOV,
JRNL AUTH 3 P.N.GOLYSHIN,A.SAVCHENKO,A.F.YAKUNIN
JRNL TITL STRUCTURE AND ACTIVITY OF THE COLD-ACTIVE AND
JRNL TITL 2 ANION-ACTIVATED CARBOXYL ESTERASE OLEI01171 FROM THE
JRNL TITL 3 OIL-DEGRADING MARINE BACTERIUM OLEISPIRA ANTARCTICA
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7_650)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.69
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.5
REMARK 3 NUMBER OF REFLECTIONS : 19117
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.156
REMARK 3 R VALUE (WORKING SET) : 0.154
REMARK 3 FREE R VALUE : 0.185
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020
REMARK 3 FREE R VALUE TEST SET COUNT : 959
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 19.6964 - 4.0075 0.98 2796 141 0.1775 0.1800
REMARK 3 2 4.0075 - 3.1852 0.99 2715 135 0.1369 0.1620
REMARK 3 3 3.1852 - 2.7838 0.97 2631 147 0.1405 0.1617
REMARK 3 4 2.7838 - 2.5299 0.96 2583 151 0.1407 0.2094
REMARK 3 5 2.5299 - 2.3489 0.95 2537 132 0.1512 0.2008
REMARK 3 6 2.3489 - 2.2106 0.91 2445 126 0.1623 0.2041
REMARK 3 7 2.2106 - 2.1000 0.92 2451 127 0.1681 0.2302
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.20
REMARK 3 SHRINKAGE RADIUS : 0.95
REMARK 3 K_SOL : 0.41
REMARK 3 B_SOL : 45.68
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.200
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 15.750
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.42640
REMARK 3 B22 (A**2) : 2.59640
REMARK 3 B33 (A**2) : -7.02280
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.008 2222
REMARK 3 ANGLE : 1.043 3026
REMARK 3 CHIRALITY : 0.073 314
REMARK 3 PLANARITY : 0.004 402
REMARK 3 DIHEDRAL : 12.684 787
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: all
REMARK 3 ORIGIN FOR THE GROUP (A): -4.8407 15.6966 -7.7503
REMARK 3 T TENSOR
REMARK 3 T11: 0.0532 T22: 0.0550
REMARK 3 T33: 0.0594 T12: 0.0008
REMARK 3 T13: 0.0020 T23: -0.0063
REMARK 3 L TENSOR
REMARK 3 L11: 0.2087 L22: 0.2956
REMARK 3 L33: 0.4278 L12: -0.0883
REMARK 3 L13: 0.0117 L23: -0.1561
REMARK 3 S TENSOR
REMARK 3 S11: -0.0023 S12: 0.0109 S13: 0.0095
REMARK 3 S21: -0.0010 S22: -0.0015 S23: 0.0218
REMARK 3 S31: 0.0073 S32: -0.0326 S33: 0.0012
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3S8Y COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-JUN-11.
REMARK 100 THE RCSB ID CODE IS RCSB065910.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-APR-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR-E SUPERBRIGHT
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS HTC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19720
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 19.730
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 6.200
REMARK 200 R MERGE (I) : 0.09000
REMARK 200 R SYM (I) : 0.08300
REMARK 200 FOR THE DATA SET : 17.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.21
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.30
REMARK 200 R MERGE FOR SHELL (I) : 0.30000
REMARK 200 R SYM FOR SHELL (I) : 0.27000
REMARK 200 FOR SHELL : 6.300
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: PDB ENTRY 3I6Y
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.84
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.66
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.4M DI-AMMONIUM CITRATE, 22%
REMARK 280 PEG3350, SOAKING STEP: KBR 0.8M, 30S. , PH 4.8, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 21 21
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,Y+1/2,-Z+1/2
REMARK 290 4555 -X,-Y+1/2,Z+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 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 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 42.22550
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 44.02550
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 42.22550
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 44.02550
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 GLY A 0
REMARK 465 MET A 1
REMARK 465 ALA A 279
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ASN A 24 CG OD1
REMARK 470 GLU A 163 CD OE1 OE2
REMARK 470 LYS A 193 CE NZ
REMARK 470 LYS A 211 CG CD CE NZ
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 THR A 56 -4.07 76.02
REMARK 500 SER A 58 -162.94 -100.52
REMARK 500 ALA A 103 47.51 -152.05
REMARK 500 PHE A 105 14.91 56.56
REMARK 500 ASN A 126 -60.60 -107.63
REMARK 500 SER A 148 -124.14 58.55
REMARK 500 ASP A 256 -153.79 -108.07
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 387 DISTANCE = 5.05 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR A 280
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3I6Y RELATED DB: PDB
REMARK 900 APO-STATE ENZYME
DBREF 3S8Y A 0 279 UNP D0VWZ4 D0VWZ4_OLEAN 1 280
SEQRES 1 A 280 GLY MET SER ILE GLU ASN LEU SER SER ASN LYS SER PHE
SEQRES 2 A 280 GLY GLY TRP HIS LYS GLN TYR SER HIS VAL SER ASN THR
SEQRES 3 A 280 LEU ASN CYS ALA MET ARG PHE ALA ILE TYR LEU PRO PRO
SEQRES 4 A 280 GLN ALA SER THR GLY ALA LYS VAL PRO VAL LEU TYR TRP
SEQRES 5 A 280 LEU SER GLY LEU THR CYS SER ASP GLU ASN PHE MET GLN
SEQRES 6 A 280 LYS ALA GLY ALA GLN ARG LEU ALA ALA GLU LEU GLY ILE
SEQRES 7 A 280 ALA ILE VAL ALA PRO ASP THR SER PRO ARG GLY GLU GLY
SEQRES 8 A 280 VAL ALA ASP ASP GLU GLY TYR ASP LEU GLY GLN GLY ALA
SEQRES 9 A 280 GLY PHE TYR VAL ASN ALA THR GLN ALA PRO TRP ASN ARG
SEQRES 10 A 280 HIS TYR GLN MET TYR ASP TYR VAL VAL ASN GLU LEU PRO
SEQRES 11 A 280 GLU LEU ILE GLU SER MET PHE PRO VAL SER ASP LYS ARG
SEQRES 12 A 280 ALA ILE ALA GLY HIS SER MET GLY GLY HIS GLY ALA LEU
SEQRES 13 A 280 THR ILE ALA LEU ARG ASN PRO GLU ARG TYR GLN SER VAL
SEQRES 14 A 280 SER ALA PHE SER PRO ILE ASN ASN PRO VAL ASN CYS PRO
SEQRES 15 A 280 TRP GLY GLN LYS ALA PHE THR ALA TYR LEU GLY LYS ASP
SEQRES 16 A 280 THR ASP THR TRP ARG GLU TYR ASP ALA SER LEU LEU MET
SEQRES 17 A 280 ARG ALA ALA LYS GLN TYR VAL PRO ALA LEU VAL ASP GLN
SEQRES 18 A 280 GLY GLU ALA ASP ASN PHE LEU ALA GLU GLN LEU LYS PRO
SEQRES 19 A 280 GLU VAL LEU GLU ALA ALA ALA SER SER ASN ASN TYR PRO
SEQRES 20 A 280 LEU GLU LEU ARG SER HIS GLU GLY TYR ASP HIS SER TYR
SEQRES 21 A 280 TYR PHE ILE ALA SER PHE ILE GLU ASP HIS LEU ARG PHE
SEQRES 22 A 280 HIS SER ASN TYR LEU ASN ALA
HET BR A 280 1
HETNAM BR BROMIDE ION
FORMUL 2 BR BR 1-
FORMUL 3 HOH *181(H2 O)
HELIX 1 1 PRO A 37 THR A 42 5 6
HELIX 2 2 GLU A 60 ALA A 66 1 7
HELIX 3 3 ALA A 68 GLY A 76 1 9
HELIX 4 4 PRO A 113 HIS A 117 5 5
HELIX 5 5 GLN A 119 ASN A 126 1 8
HELIX 6 6 ASN A 126 PHE A 136 1 11
HELIX 7 7 SER A 148 ASN A 161 1 14
HELIX 8 8 ASN A 176 ASN A 179 5 4
HELIX 9 9 CYS A 180 GLY A 192 1 13
HELIX 10 10 ASP A 194 TYR A 201 5 8
HELIX 11 11 ASP A 202 ALA A 210 1 9
HELIX 12 12 LYS A 232 SER A 242 1 11
HELIX 13 13 SER A 258 ASN A 278 1 21
SHEET 1 A 9 ILE A 3 SER A 11 0
SHEET 2 A 9 GLY A 14 SER A 23 -1 O SER A 20 N GLU A 4
SHEET 3 A 9 CYS A 28 LEU A 36 -1 O PHE A 32 N TYR A 19
SHEET 4 A 9 ALA A 78 PRO A 82 -1 O ALA A 81 N ALA A 33
SHEET 5 A 9 VAL A 46 LEU A 52 1 N TRP A 51 O VAL A 80
SHEET 6 A 9 VAL A 138 HIS A 147 1 O ALA A 145 N LEU A 52
SHEET 7 A 9 VAL A 168 PHE A 171 1 O PHE A 171 N GLY A 146
SHEET 8 A 9 ALA A 216 GLY A 221 1 O ASP A 219 N ALA A 170
SHEET 9 A 9 LEU A 247 HIS A 252 1 O ARG A 250 N VAL A 218
CISPEP 1 ALA A 112 PRO A 113 0 -3.71
SITE 1 AC1 5 GLY A 54 LEU A 55 SER A 148 MET A 149
SITE 2 AC1 5 HOH A 434
CRYST1 44.532 84.451 88.051 90.00 90.00 90.00 P 2 21 21 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 0.022456 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011841 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011357 0.00000
TER 2162 ASN A 278
MASTER 278 0 1 13 9 0 2 6 2343 1 0 22
END |