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HEADER HYDROLASE 23-SEP-22 8B5O
TITLE STRUCTURE OF HALOALKANE DEHALOGENASE DMMARA FROM MYCOBACTERIUM MARINUM
TITLE 2 AT PH 5.5
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HALOALKANE DEHALOGENASE DHAA;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM MARINUM;
SOURCE 3 ORGANISM_TAXID: 1781;
SOURCE 4 GENE: DHAA, MMAR_4113;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HALOALKANE DEHALOGENASE, ENZYME, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.SNAJDAROVA,M.MAREK
REVDAT 1 30-AUG-23 8B5O 0
JRNL AUTH K.SNAJDAROVA,M.MAREK
JRNL TITL STRUCTURE OF HALOALKANE DEHALOGENASE DMMARA FROM
JRNL TITL 2 MYCOBACTERIUM MARINUM AT PH 5.5
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.14-3260
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.70
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 144116
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.200
REMARK 3 R VALUE (WORKING SET) : 0.198
REMARK 3 FREE R VALUE : 0.238
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.910
REMARK 3 FREE R VALUE TEST SET COUNT : 7081
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 43.7020 - 4.9610 1.00 4785 250 0.1878 0.2089
REMARK 3 2 4.9610 - 3.9385 1.00 4708 231 0.1676 0.1952
REMARK 3 3 3.9385 - 3.4409 1.00 4652 241 0.1807 0.2365
REMARK 3 4 3.4409 - 3.1264 1.00 4644 233 0.1778 0.2007
REMARK 3 5 3.1264 - 2.9024 1.00 4606 243 0.1892 0.2401
REMARK 3 6 2.9024 - 2.7313 1.00 4648 216 0.1858 0.2388
REMARK 3 7 2.7313 - 2.5945 1.00 4608 248 0.1904 0.2281
REMARK 3 8 2.5945 - 2.4816 1.00 4593 254 0.1865 0.2241
REMARK 3 9 2.4816 - 2.3860 1.00 4553 271 0.1892 0.2262
REMARK 3 10 2.3860 - 2.3037 0.99 4644 226 0.1902 0.2290
REMARK 3 11 2.3037 - 2.2317 0.99 4516 249 0.2079 0.2625
REMARK 3 12 2.2317 - 2.1679 1.00 4590 237 0.1938 0.2233
REMARK 3 13 2.1679 - 2.1108 0.99 4586 268 0.1896 0.2401
REMARK 3 14 2.1108 - 2.0593 0.98 4518 216 0.2104 0.2706
REMARK 3 15 2.0593 - 2.0125 0.99 4536 268 0.2084 0.2766
REMARK 3 16 2.0125 - 1.9697 1.00 4602 235 0.2071 0.2323
REMARK 3 17 1.9697 - 1.9303 0.98 4553 217 0.2067 0.2516
REMARK 3 18 1.9303 - 1.8939 0.99 4536 218 0.2542 0.3071
REMARK 3 19 1.8939 - 1.8600 0.99 4558 213 0.2293 0.2771
REMARK 3 20 1.8600 - 1.8285 0.99 4542 231 0.2297 0.2880
REMARK 3 21 1.8285 - 1.7990 0.99 4620 213 0.2220 0.2703
REMARK 3 22 1.7990 - 1.7713 0.98 4509 234 0.2274 0.2731
REMARK 3 23 1.7713 - 1.7453 0.99 4527 230 0.2245 0.2711
REMARK 3 24 1.7453 - 1.7207 0.98 4561 226 0.2309 0.2629
REMARK 3 25 1.7207 - 1.6974 0.99 4523 237 0.2488 0.2940
REMARK 3 26 1.6974 - 1.6754 0.98 4483 252 0.2597 0.3149
REMARK 3 27 1.6754 - 1.6544 0.98 4437 247 0.2606 0.2983
REMARK 3 28 1.6544 - 1.6345 0.98 4519 249 0.2623 0.2925
REMARK 3 29 1.6345 - 1.6155 0.98 4503 220 0.2857 0.2900
REMARK 3 30 1.6155 - 1.5974 0.95 4375 208 0.3126 0.3468
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.210
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.240
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.32
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 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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
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): 36.9065 -7.0357 26.7306
REMARK 3 T TENSOR
REMARK 3 T11: 0.1874 T22: 0.0931
REMARK 3 T33: 0.0981 T12: -0.0154
REMARK 3 T13: -0.0172 T23: 0.0058
REMARK 3 L TENSOR
REMARK 3 L11: 0.2123 L22: 0.3652
REMARK 3 L33: 0.3599 L12: -0.0212
REMARK 3 L13: -0.0351 L23: -0.0222
REMARK 3 S TENSOR
REMARK 3 S11: 0.0204 S12: 0.0251 S13: -0.0198
REMARK 3 S21: -0.1464 S22: 0.0167 S23: 0.0519
REMARK 3 S31: 0.0523 S32: -0.0168 S33: -0.0240
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 8B5O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-SEP-22.
REMARK 100 THE DEPOSITION ID IS D_1292125808.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-OCT-19
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06DA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.7.4
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 144169
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.597
REMARK 200 RESOLUTION RANGE LOW (A) : 47.710
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : 0.10700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.62
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.90
REMARK 200 R MERGE FOR SHELL (I) : 1.29100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 8B5K
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.25
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM ACETATE, BIS-TRIS, PEG 3350,
REMARK 280 PH 5.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293.15K
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 30.38300
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 GLN A 284
REMARK 465 ASP A 285
REMARK 465 GLY A 286
REMARK 465 ALA A 287
REMARK 465 ASP A 288
REMARK 465 ARG A 289
REMARK 465 ALA A 290
REMARK 465 HIS A 291
REMARK 465 HIS A 292
REMARK 465 HIS A 293
REMARK 465 HIS A 294
REMARK 465 HIS A 295
REMARK 465 HIS A 296
REMARK 465 ARG B 283
REMARK 465 GLN B 284
REMARK 465 ASP B 285
REMARK 465 GLY B 286
REMARK 465 ALA B 287
REMARK 465 ASP B 288
REMARK 465 ARG B 289
REMARK 465 ALA B 290
REMARK 465 HIS B 291
REMARK 465 HIS B 292
REMARK 465 HIS B 293
REMARK 465 HIS B 294
REMARK 465 HIS B 295
REMARK 465 HIS B 296
REMARK 465 ASP C 285
REMARK 465 GLY C 286
REMARK 465 ALA C 287
REMARK 465 ASP C 288
REMARK 465 ARG C 289
REMARK 465 ALA C 290
REMARK 465 HIS C 291
REMARK 465 HIS C 292
REMARK 465 HIS C 293
REMARK 465 HIS C 294
REMARK 465 HIS C 295
REMARK 465 HIS C 296
REMARK 465 ALA D 113
REMARK 465 GLY D 114
REMARK 465 LEU D 234
REMARK 465 HIS D 235
REMARK 465 GLU D 282
REMARK 465 ARG D 283
REMARK 465 GLN D 284
REMARK 465 ASP D 285
REMARK 465 GLY D 286
REMARK 465 ALA D 287
REMARK 465 ASP D 288
REMARK 465 ARG D 289
REMARK 465 ALA D 290
REMARK 465 HIS D 291
REMARK 465 HIS D 292
REMARK 465 HIS D 293
REMARK 465 HIS D 294
REMARK 465 HIS D 295
REMARK 465 HIS D 296
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 ASP A 204 CB - CG - OD1 ANGL. DEV. = 5.9 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 LEU A 7 -124.46 49.16
REMARK 500 PRO A 29 47.30 -106.32
REMARK 500 THR A 30 -152.84 -101.80
REMARK 500 ASP A 95 -134.13 55.17
REMARK 500 ASP A 119 69.22 24.56
REMARK 500 THR A 131 -121.38 36.22
REMARK 500 ALA A 232 -82.58 -145.04
REMARK 500 ARG A 258 -145.59 -103.16
REMARK 500 LEU B 7 -126.56 47.68
REMARK 500 SER B 9 -152.31 -138.50
REMARK 500 PRO B 29 49.98 -105.58
REMARK 500 THR B 30 -155.85 -106.48
REMARK 500 ASP B 95 -135.39 54.15
REMARK 500 ASP B 119 68.63 28.56
REMARK 500 THR B 131 -126.31 42.52
REMARK 500 ALA B 232 -81.48 -151.68
REMARK 500 ARG B 258 -138.46 -102.76
REMARK 500 LEU C 7 -120.20 52.22
REMARK 500 SER C 9 -159.17 -137.23
REMARK 500 PRO C 29 48.01 -103.59
REMARK 500 THR C 30 -152.25 -101.82
REMARK 500 ASP C 95 -135.15 52.39
REMARK 500 ASP C 119 67.84 29.71
REMARK 500 THR C 131 -116.65 35.37
REMARK 500 ALA C 232 -75.00 -145.16
REMARK 500 ARG C 258 -141.01 -95.35
REMARK 500 PHE C 260 57.97 -93.51
REMARK 500 LEU D 7 -125.59 53.43
REMARK 500 SER D 9 -156.25 -134.42
REMARK 500 PRO D 29 51.47 -107.19
REMARK 500 THR D 30 -157.10 -102.95
REMARK 500 SER D 31 -165.22 -160.90
REMARK 500 LEU D 42 10.16 -165.61
REMARK 500 SER D 43 21.28 -76.78
REMARK 500 THR D 86 -140.39 -123.07
REMARK 500 GLU D 87 -88.26 73.85
REMARK 500 ASP D 95 -136.25 56.67
REMARK 500 GLU D 110 35.67 -67.75
REMARK 500 ASP D 119 75.80 34.37
REMARK 500 THR D 131 -116.13 41.10
REMARK 500 LYS D 158 -39.26 -131.10
REMARK 500 ALA D 232 -75.33 -152.27
REMARK 500 SER D 246 23.00 -75.45
REMARK 500 ASN D 249 85.17 44.45
REMARK 500 ARG D 251 -137.39 -69.66
REMARK 500 GLU D 252 141.89 160.40
REMARK 500 ARG D 258 -121.96 -102.74
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 C 646 DISTANCE = 6.94 ANGSTROMS
DBREF 8B5O A 1 290 UNP B2HR89 B2HR89_MYCMM 1 290
DBREF 8B5O B 1 290 UNP B2HR89 B2HR89_MYCMM 1 290
DBREF 8B5O C 1 290 UNP B2HR89 B2HR89_MYCMM 1 290
DBREF 8B5O D 1 290 UNP B2HR89 B2HR89_MYCMM 1 290
SEQADV 8B5O HIS A 291 UNP B2HR89 EXPRESSION TAG
SEQADV 8B5O HIS A 292 UNP B2HR89 EXPRESSION TAG
SEQADV 8B5O HIS A 293 UNP B2HR89 EXPRESSION TAG
SEQADV 8B5O HIS A 294 UNP B2HR89 EXPRESSION TAG
SEQADV 8B5O HIS A 295 UNP B2HR89 EXPRESSION TAG
SEQADV 8B5O HIS A 296 UNP B2HR89 EXPRESSION TAG
SEQADV 8B5O HIS B 291 UNP B2HR89 EXPRESSION TAG
SEQADV 8B5O HIS B 292 UNP B2HR89 EXPRESSION TAG
SEQADV 8B5O HIS B 293 UNP B2HR89 EXPRESSION TAG
SEQADV 8B5O HIS B 294 UNP B2HR89 EXPRESSION TAG
SEQADV 8B5O HIS B 295 UNP B2HR89 EXPRESSION TAG
SEQADV 8B5O HIS B 296 UNP B2HR89 EXPRESSION TAG
SEQADV 8B5O HIS C 291 UNP B2HR89 EXPRESSION TAG
SEQADV 8B5O HIS C 292 UNP B2HR89 EXPRESSION TAG
SEQADV 8B5O HIS C 293 UNP B2HR89 EXPRESSION TAG
SEQADV 8B5O HIS C 294 UNP B2HR89 EXPRESSION TAG
SEQADV 8B5O HIS C 295 UNP B2HR89 EXPRESSION TAG
SEQADV 8B5O HIS C 296 UNP B2HR89 EXPRESSION TAG
SEQADV 8B5O HIS D 291 UNP B2HR89 EXPRESSION TAG
SEQADV 8B5O HIS D 292 UNP B2HR89 EXPRESSION TAG
SEQADV 8B5O HIS D 293 UNP B2HR89 EXPRESSION TAG
SEQADV 8B5O HIS D 294 UNP B2HR89 EXPRESSION TAG
SEQADV 8B5O HIS D 295 UNP B2HR89 EXPRESSION TAG
SEQADV 8B5O HIS D 296 UNP B2HR89 EXPRESSION TAG
SEQRES 1 A 296 MET LYS ARG VAL ASP VAL LEU ASP SER ALA MET SER TYR
SEQRES 2 A 296 ILE ASP VAL GLY GLN GLY ASP PRO ILE VAL PHE LEU HIS
SEQRES 3 A 296 GLY ASN PRO THR SER SER TYR LEU TRP ARG ASN VAL ILE
SEQRES 4 A 296 PRO HIS LEU SER ASP VAL GLY ARG CYS LEU ALA PRO ASP
SEQRES 5 A 296 LEU ILE GLY MET GLY ALA SER GLY THR SER PRO THR PHE
SEQRES 6 A 296 SER TYR ARG PHE ALA ASP HIS VAL ARG TYR LEU ASP ALA
SEQRES 7 A 296 TRP PHE GLU ALA VAL GLY ILE THR GLU ASN VAL VAL LEU
SEQRES 8 A 296 VAL VAL HIS ASP TRP GLY SER ALA LEU GLY PHE TYR ARG
SEQRES 9 A 296 ALA LEU ARG TYR PRO GLU GLN ILE ALA GLY ILE ALA TYR
SEQRES 10 A 296 MET ASP ALA LEU VAL GLN PRO ARG THR TRP ALA GLY PHE
SEQRES 11 A 296 THR ASP TYR GLU PRO LEU MET ARG ALA LEU ARG THR GLU
SEQRES 12 A 296 GLN GLY GLU ARG MET ALA LEU ALA GLU ASN VAL PHE VAL
SEQRES 13 A 296 GLU LYS VAL VAL PRO GLY GLY VAL GLN ARG GLN LEU THR
SEQRES 14 A 296 GLU GLU GLU MET ALA VAL TYR ARG THR PRO TYR PRO THR
SEQRES 15 A 296 PRO GLN SER ARG ILE PRO THR LEU LEU TRP ALA ARG GLU
SEQRES 16 A 296 ILE PRO VAL GLU GLY GLU PRO ALA ASP VAL GLN ALA MET
SEQRES 17 A 296 VAL GLN GLU TYR ALA ASP PHE LEU SER ARG SER ASP ILE
SEQRES 18 A 296 PRO LYS LEU LEU ILE VAL ALA GLU PRO GLY ALA ILE LEU
SEQRES 19 A 296 HIS GLU GLY GLY SER GLU LEU ASP PHE ALA ARG SER TRP
SEQRES 20 A 296 PRO ASN GLN ARG GLU VAL LYS VAL ALA GLY ARG HIS PHE
SEQRES 21 A 296 LEU GLN GLU ASP SER PRO ASP ALA ILE GLY ALA ALA VAL
SEQRES 22 A 296 ARG ALA PHE VAL LEU ASP VAL ARG GLU ARG GLN ASP GLY
SEQRES 23 A 296 ALA ASP ARG ALA HIS HIS HIS HIS HIS HIS
SEQRES 1 B 296 MET LYS ARG VAL ASP VAL LEU ASP SER ALA MET SER TYR
SEQRES 2 B 296 ILE ASP VAL GLY GLN GLY ASP PRO ILE VAL PHE LEU HIS
SEQRES 3 B 296 GLY ASN PRO THR SER SER TYR LEU TRP ARG ASN VAL ILE
SEQRES 4 B 296 PRO HIS LEU SER ASP VAL GLY ARG CYS LEU ALA PRO ASP
SEQRES 5 B 296 LEU ILE GLY MET GLY ALA SER GLY THR SER PRO THR PHE
SEQRES 6 B 296 SER TYR ARG PHE ALA ASP HIS VAL ARG TYR LEU ASP ALA
SEQRES 7 B 296 TRP PHE GLU ALA VAL GLY ILE THR GLU ASN VAL VAL LEU
SEQRES 8 B 296 VAL VAL HIS ASP TRP GLY SER ALA LEU GLY PHE TYR ARG
SEQRES 9 B 296 ALA LEU ARG TYR PRO GLU GLN ILE ALA GLY ILE ALA TYR
SEQRES 10 B 296 MET ASP ALA LEU VAL GLN PRO ARG THR TRP ALA GLY PHE
SEQRES 11 B 296 THR ASP TYR GLU PRO LEU MET ARG ALA LEU ARG THR GLU
SEQRES 12 B 296 GLN GLY GLU ARG MET ALA LEU ALA GLU ASN VAL PHE VAL
SEQRES 13 B 296 GLU LYS VAL VAL PRO GLY GLY VAL GLN ARG GLN LEU THR
SEQRES 14 B 296 GLU GLU GLU MET ALA VAL TYR ARG THR PRO TYR PRO THR
SEQRES 15 B 296 PRO GLN SER ARG ILE PRO THR LEU LEU TRP ALA ARG GLU
SEQRES 16 B 296 ILE PRO VAL GLU GLY GLU PRO ALA ASP VAL GLN ALA MET
SEQRES 17 B 296 VAL GLN GLU TYR ALA ASP PHE LEU SER ARG SER ASP ILE
SEQRES 18 B 296 PRO LYS LEU LEU ILE VAL ALA GLU PRO GLY ALA ILE LEU
SEQRES 19 B 296 HIS GLU GLY GLY SER GLU LEU ASP PHE ALA ARG SER TRP
SEQRES 20 B 296 PRO ASN GLN ARG GLU VAL LYS VAL ALA GLY ARG HIS PHE
SEQRES 21 B 296 LEU GLN GLU ASP SER PRO ASP ALA ILE GLY ALA ALA VAL
SEQRES 22 B 296 ARG ALA PHE VAL LEU ASP VAL ARG GLU ARG GLN ASP GLY
SEQRES 23 B 296 ALA ASP ARG ALA HIS HIS HIS HIS HIS HIS
SEQRES 1 C 296 MET LYS ARG VAL ASP VAL LEU ASP SER ALA MET SER TYR
SEQRES 2 C 296 ILE ASP VAL GLY GLN GLY ASP PRO ILE VAL PHE LEU HIS
SEQRES 3 C 296 GLY ASN PRO THR SER SER TYR LEU TRP ARG ASN VAL ILE
SEQRES 4 C 296 PRO HIS LEU SER ASP VAL GLY ARG CYS LEU ALA PRO ASP
SEQRES 5 C 296 LEU ILE GLY MET GLY ALA SER GLY THR SER PRO THR PHE
SEQRES 6 C 296 SER TYR ARG PHE ALA ASP HIS VAL ARG TYR LEU ASP ALA
SEQRES 7 C 296 TRP PHE GLU ALA VAL GLY ILE THR GLU ASN VAL VAL LEU
SEQRES 8 C 296 VAL VAL HIS ASP TRP GLY SER ALA LEU GLY PHE TYR ARG
SEQRES 9 C 296 ALA LEU ARG TYR PRO GLU GLN ILE ALA GLY ILE ALA TYR
SEQRES 10 C 296 MET ASP ALA LEU VAL GLN PRO ARG THR TRP ALA GLY PHE
SEQRES 11 C 296 THR ASP TYR GLU PRO LEU MET ARG ALA LEU ARG THR GLU
SEQRES 12 C 296 GLN GLY GLU ARG MET ALA LEU ALA GLU ASN VAL PHE VAL
SEQRES 13 C 296 GLU LYS VAL VAL PRO GLY GLY VAL GLN ARG GLN LEU THR
SEQRES 14 C 296 GLU GLU GLU MET ALA VAL TYR ARG THR PRO TYR PRO THR
SEQRES 15 C 296 PRO GLN SER ARG ILE PRO THR LEU LEU TRP ALA ARG GLU
SEQRES 16 C 296 ILE PRO VAL GLU GLY GLU PRO ALA ASP VAL GLN ALA MET
SEQRES 17 C 296 VAL GLN GLU TYR ALA ASP PHE LEU SER ARG SER ASP ILE
SEQRES 18 C 296 PRO LYS LEU LEU ILE VAL ALA GLU PRO GLY ALA ILE LEU
SEQRES 19 C 296 HIS GLU GLY GLY SER GLU LEU ASP PHE ALA ARG SER TRP
SEQRES 20 C 296 PRO ASN GLN ARG GLU VAL LYS VAL ALA GLY ARG HIS PHE
SEQRES 21 C 296 LEU GLN GLU ASP SER PRO ASP ALA ILE GLY ALA ALA VAL
SEQRES 22 C 296 ARG ALA PHE VAL LEU ASP VAL ARG GLU ARG GLN ASP GLY
SEQRES 23 C 296 ALA ASP ARG ALA HIS HIS HIS HIS HIS HIS
SEQRES 1 D 296 MET LYS ARG VAL ASP VAL LEU ASP SER ALA MET SER TYR
SEQRES 2 D 296 ILE ASP VAL GLY GLN GLY ASP PRO ILE VAL PHE LEU HIS
SEQRES 3 D 296 GLY ASN PRO THR SER SER TYR LEU TRP ARG ASN VAL ILE
SEQRES 4 D 296 PRO HIS LEU SER ASP VAL GLY ARG CYS LEU ALA PRO ASP
SEQRES 5 D 296 LEU ILE GLY MET GLY ALA SER GLY THR SER PRO THR PHE
SEQRES 6 D 296 SER TYR ARG PHE ALA ASP HIS VAL ARG TYR LEU ASP ALA
SEQRES 7 D 296 TRP PHE GLU ALA VAL GLY ILE THR GLU ASN VAL VAL LEU
SEQRES 8 D 296 VAL VAL HIS ASP TRP GLY SER ALA LEU GLY PHE TYR ARG
SEQRES 9 D 296 ALA LEU ARG TYR PRO GLU GLN ILE ALA GLY ILE ALA TYR
SEQRES 10 D 296 MET ASP ALA LEU VAL GLN PRO ARG THR TRP ALA GLY PHE
SEQRES 11 D 296 THR ASP TYR GLU PRO LEU MET ARG ALA LEU ARG THR GLU
SEQRES 12 D 296 GLN GLY GLU ARG MET ALA LEU ALA GLU ASN VAL PHE VAL
SEQRES 13 D 296 GLU LYS VAL VAL PRO GLY GLY VAL GLN ARG GLN LEU THR
SEQRES 14 D 296 GLU GLU GLU MET ALA VAL TYR ARG THR PRO TYR PRO THR
SEQRES 15 D 296 PRO GLN SER ARG ILE PRO THR LEU LEU TRP ALA ARG GLU
SEQRES 16 D 296 ILE PRO VAL GLU GLY GLU PRO ALA ASP VAL GLN ALA MET
SEQRES 17 D 296 VAL GLN GLU TYR ALA ASP PHE LEU SER ARG SER ASP ILE
SEQRES 18 D 296 PRO LYS LEU LEU ILE VAL ALA GLU PRO GLY ALA ILE LEU
SEQRES 19 D 296 HIS GLU GLY GLY SER GLU LEU ASP PHE ALA ARG SER TRP
SEQRES 20 D 296 PRO ASN GLN ARG GLU VAL LYS VAL ALA GLY ARG HIS PHE
SEQRES 21 D 296 LEU GLN GLU ASP SER PRO ASP ALA ILE GLY ALA ALA VAL
SEQRES 22 D 296 ARG ALA PHE VAL LEU ASP VAL ARG GLU ARG GLN ASP GLY
SEQRES 23 D 296 ALA ASP ARG ALA HIS HIS HIS HIS HIS HIS
HET GOL A 401 6
HET FMT A 402 3
HET FMT A 403 3
HET GOL A 404 6
HET FMT A 405 3
HET FMT A 406 3
HET GOL B 301 6
HET GOL B 302 6
HET ACT B 303 4
HET FMT B 304 3
HET FMT B 305 3
HET FMT B 306 3
HET GOL C 301 6
HET FMT C 302 3
HET GOL C 303 6
HET FMT C 304 3
HET FMT C 305 3
HET GOL C 306 6
HET FMT C 307 3
HET FMT C 308 3
HET FMT D 301 3
HETNAM GOL GLYCEROL
HETNAM FMT FORMIC ACID
HETNAM ACT ACETATE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 GOL 7(C3 H8 O3)
FORMUL 6 FMT 13(C H2 O2)
FORMUL 13 ACT C2 H3 O2 1-
FORMUL 26 HOH *708(H2 O)
HELIX 1 AA1 SER A 31 ARG A 36 5 6
HELIX 2 AA2 VAL A 38 LEU A 42 5 5
HELIX 3 AA3 ARG A 68 GLY A 84 1 17
HELIX 4 AA4 ASP A 95 TYR A 108 1 14
HELIX 5 AA5 THR A 126 ASP A 132 5 7
HELIX 6 AA6 TYR A 133 ARG A 141 1 9
HELIX 7 AA7 GLN A 144 LEU A 150 1 7
HELIX 8 AA8 ASN A 153 LYS A 158 1 6
HELIX 9 AA9 LYS A 158 GLY A 163 1 6
HELIX 10 AB1 THR A 169 THR A 178 1 10
HELIX 11 AB2 THR A 182 SER A 185 5 4
HELIX 12 AB3 ARG A 186 ILE A 196 1 11
HELIX 13 AB4 PRO A 202 SER A 217 1 16
HELIX 14 AB5 GLY A 238 SER A 246 1 9
HELIX 15 AB6 PHE A 260 SER A 265 1 6
HELIX 16 AB7 SER A 265 ARG A 283 1 19
HELIX 17 AB8 SER B 31 ARG B 36 5 6
HELIX 18 AB9 VAL B 38 LEU B 42 5 5
HELIX 19 AC1 ARG B 68 GLY B 84 1 17
HELIX 20 AC2 ASP B 95 TYR B 108 1 14
HELIX 21 AC3 THR B 126 ASP B 132 5 7
HELIX 22 AC4 TYR B 133 ARG B 141 1 9
HELIX 23 AC5 GLN B 144 LEU B 150 1 7
HELIX 24 AC6 ASN B 153 LYS B 158 1 6
HELIX 25 AC7 LYS B 158 GLY B 163 1 6
HELIX 26 AC8 THR B 169 THR B 178 1 10
HELIX 27 AC9 THR B 182 SER B 185 5 4
HELIX 28 AD1 ARG B 186 ILE B 196 1 11
HELIX 29 AD2 PRO B 202 SER B 217 1 16
HELIX 30 AD3 GLY B 238 SER B 246 1 9
HELIX 31 AD4 PHE B 260 ASP B 264 5 5
HELIX 32 AD5 SER B 265 GLU B 282 1 18
HELIX 33 AD6 SER C 31 ARG C 36 5 6
HELIX 34 AD7 VAL C 38 LEU C 42 5 5
HELIX 35 AD8 ARG C 68 GLY C 84 1 17
HELIX 36 AD9 ASP C 95 TYR C 108 1 14
HELIX 37 AE1 THR C 126 ASP C 132 5 7
HELIX 38 AE2 TYR C 133 ARG C 141 1 9
HELIX 39 AE3 GLN C 144 LEU C 150 1 7
HELIX 40 AE4 ASN C 153 LYS C 158 1 6
HELIX 41 AE5 LYS C 158 GLY C 163 1 6
HELIX 42 AE6 THR C 169 THR C 178 1 10
HELIX 43 AE7 THR C 182 SER C 185 5 4
HELIX 44 AE8 ARG C 186 ILE C 196 1 11
HELIX 45 AE9 PRO C 202 SER C 217 1 16
HELIX 46 AF1 GLY C 238 SER C 246 1 9
HELIX 47 AF2 PHE C 260 ASP C 264 5 5
HELIX 48 AF3 SER C 265 GLN C 284 1 20
HELIX 49 AF4 SER D 31 ARG D 36 5 6
HELIX 50 AF5 VAL D 38 LEU D 42 5 5
HELIX 51 AF6 ARG D 68 VAL D 83 1 16
HELIX 52 AF7 ASP D 95 TYR D 108 1 14
HELIX 53 AF8 PRO D 109 ILE D 112 5 4
HELIX 54 AF9 TRP D 127 ASP D 132 5 6
HELIX 55 AG1 TYR D 133 ARG D 141 1 9
HELIX 56 AG2 GLU D 143 LEU D 150 1 8
HELIX 57 AG3 ASN D 153 LYS D 158 1 6
HELIX 58 AG4 VAL D 160 VAL D 164 5 5
HELIX 59 AG5 THR D 169 ARG D 177 1 9
HELIX 60 AG6 THR D 182 SER D 185 5 4
HELIX 61 AG7 ARG D 186 ILE D 196 1 11
HELIX 62 AG8 PRO D 202 ASP D 214 1 13
HELIX 63 AG9 PHE D 215 SER D 219 5 5
HELIX 64 AH1 GLY D 238 SER D 246 1 9
HELIX 65 AH2 PHE D 260 ASP D 264 5 5
HELIX 66 AH3 SER D 265 ARG D 281 1 17
SHEET 1 AA1 8 LYS A 2 VAL A 6 0
SHEET 2 AA1 8 SER A 9 VAL A 16 -1 O TYR A 13 N LYS A 2
SHEET 3 AA1 8 ARG A 47 PRO A 51 -1 O CYS A 48 N VAL A 16
SHEET 4 AA1 8 PRO A 21 LEU A 25 1 N ILE A 22 O ARG A 47
SHEET 5 AA1 8 VAL A 89 HIS A 94 1 O VAL A 92 N VAL A 23
SHEET 6 AA1 8 ILE A 112 MET A 118 1 O ALA A 116 N LEU A 91
SHEET 7 AA1 8 LYS A 223 PRO A 230 1 O LEU A 224 N TYR A 117
SHEET 8 AA1 8 GLN A 250 GLY A 257 1 O ARG A 251 N LEU A 225
SHEET 1 AA2 8 LYS B 2 VAL B 6 0
SHEET 2 AA2 8 SER B 9 VAL B 16 -1 O TYR B 13 N LYS B 2
SHEET 3 AA2 8 ARG B 47 PRO B 51 -1 O CYS B 48 N VAL B 16
SHEET 4 AA2 8 PRO B 21 LEU B 25 1 N ILE B 22 O ARG B 47
SHEET 5 AA2 8 VAL B 89 HIS B 94 1 O VAL B 92 N VAL B 23
SHEET 6 AA2 8 ILE B 112 MET B 118 1 O ALA B 116 N LEU B 91
SHEET 7 AA2 8 LYS B 223 PRO B 230 1 O LEU B 224 N TYR B 117
SHEET 8 AA2 8 GLN B 250 GLY B 257 1 O ARG B 251 N LEU B 225
SHEET 1 AA3 8 LYS C 2 VAL C 6 0
SHEET 2 AA3 8 SER C 9 VAL C 16 -1 O MET C 11 N VAL C 4
SHEET 3 AA3 8 ARG C 47 PRO C 51 -1 O CYS C 48 N VAL C 16
SHEET 4 AA3 8 PRO C 21 LEU C 25 1 N PHE C 24 O LEU C 49
SHEET 5 AA3 8 VAL C 89 HIS C 94 1 O VAL C 92 N VAL C 23
SHEET 6 AA3 8 ILE C 112 MET C 118 1 O ALA C 116 N LEU C 91
SHEET 7 AA3 8 LYS C 223 PRO C 230 1 O ILE C 226 N TYR C 117
SHEET 8 AA3 8 GLN C 250 GLY C 257 1 O ARG C 251 N LEU C 225
SHEET 1 AA4 8 LYS D 2 VAL D 6 0
SHEET 2 AA4 8 SER D 9 VAL D 16 -1 O MET D 11 N VAL D 4
SHEET 3 AA4 8 ARG D 47 PRO D 51 -1 O CYS D 48 N VAL D 16
SHEET 4 AA4 8 PRO D 21 LEU D 25 1 N ILE D 22 O ARG D 47
SHEET 5 AA4 8 VAL D 90 HIS D 94 1 O VAL D 92 N LEU D 25
SHEET 6 AA4 8 ALA D 116 MET D 118 1 O ALA D 116 N LEU D 91
SHEET 7 AA4 8 LEU D 224 PRO D 230 1 O LEU D 224 N TYR D 117
SHEET 8 AA4 8 VAL D 253 GLY D 257 1 O VAL D 253 N VAL D 227
CISPEP 1 ASN A 28 PRO A 29 0 -1.82
CISPEP 2 GLU A 201 PRO A 202 0 -3.96
CISPEP 3 GLU A 229 PRO A 230 0 5.05
CISPEP 4 ASN B 28 PRO B 29 0 -4.51
CISPEP 5 GLU B 201 PRO B 202 0 -3.15
CISPEP 6 GLU B 229 PRO B 230 0 7.79
CISPEP 7 ASN C 28 PRO C 29 0 -4.83
CISPEP 8 GLU C 201 PRO C 202 0 -7.14
CISPEP 9 GLU C 229 PRO C 230 0 11.28
CISPEP 10 ASN D 28 PRO D 29 0 -1.83
CISPEP 11 GLU D 201 PRO D 202 0 -2.10
CISPEP 12 GLU D 229 PRO D 230 0 3.00
CRYST1 90.699 60.766 104.777 90.00 105.49 90.00 P 1 21 1 8
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 0.011025 0.000000 0.003055 0.00000
SCALE2 0.000000 0.016457 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009904 0.00000
TER 2258 ARG A 283
TER 4489 GLU B 282
TER 6758 GLN C 284
TER 8953 ARG D 281
MASTER 405 0 21 66 32 0 0 6 9676 4 85 92
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