HEADER HYDROLASE 18-JUN-10 2XHL
TITLE STRUCTURE OF A FUNCTIONAL DERIVATIVE OF CLOSTRIDIUM BOTULINUM
TITLE 2 NEUROTOXIN TYPE B
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BOTULINUM NEUROTOXIN B LIGHT CHAIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 1-437;
COMPND 5 SYNONYM: BONT/B, BONTOXILYSIN-B;
COMPND 6 EC: 3.4.24.69;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: BOTULINUM NEUROTOXIN B HEAVY CHAIN;
COMPND 10 CHAIN: B;
COMPND 11 FRAGMENT: RESIDUES 446-858;
COMPND 12 SYNONYM: BONT/B, BONTOXILYSIN-B;
COMPND 13 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CLOSTRIDIUM BOTULINUM;
SOURCE 3 ORGANISM_TAXID: 1491;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: MODIFIED PET;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: CLOSTRIDIUM BOTULINUM;
SOURCE 11 ORGANISM_TAXID: 1491;
SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 14 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 15 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 16 EXPRESSION_SYSTEM_PLASMID: MODIFIED PET
KEYWDS HYDROLASE, METALLOPROTEASE, MEMBRANE DOMAIN, ENDOPEPTIDASE, ZINC
KEYWDS 2 PROTEASE, BOTULISM, TOXIN
EXPDTA X-RAY DIFFRACTION
AUTHOR G.MASUYER,M.BEARD,V.A.CADD,J.A.CHADDOCK,K.R.ACHARYA
REVDAT 4 31-JAN-24 2XHL 1 ATOM
REVDAT 3 20-DEC-23 2XHL 1 REMARK LINK
REVDAT 2 06-JUL-11 2XHL 1 JRNL REMARK
REVDAT 1 01-DEC-10 2XHL 0
JRNL AUTH G.MASUYER,M.BEARD,V.A.CADD,J.A.CHADDOCK,K.R.ACHARYA
JRNL TITL STRUCTURE AND ACTIVITY OF A FUNCTIONAL DERIVATIVE OF
JRNL TITL 2 CLOSTRIDIUM BOTULINUM NEUROTOXIN B.
JRNL REF J.STRUCT.BIOL. V. 174 52 2011
JRNL REFN ISSN 1047-8477
JRNL PMID 21078393
JRNL DOI 10.1016/J.JSB.2010.11.010
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0072
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) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 113.49
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 27162
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) : 0.242
REMARK 3 R VALUE (WORKING SET) : 0.240
REMARK 3 FREE R VALUE : 0.282
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1448
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) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1966
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2760
REMARK 3 BIN FREE R VALUE SET COUNT : 102
REMARK 3 BIN FREE R VALUE : 0.3300
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6828
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 31
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.56
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.06000
REMARK 3 B22 (A**2) : 0.48000
REMARK 3 B33 (A**2) : 2.59000
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 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.405
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.314
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 33.922
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.900
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.853
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6968 ; 0.006 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9422 ; 0.855 ; 1.964
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 836 ; 4.371 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 349 ;35.817 ;25.903
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1271 ;13.921 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 18 ;13.914 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1042 ; 0.058 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5261 ; 0.003 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 4190 ; 0.304 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6828 ; 0.570 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2778 ; 0.558 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2594 ; 1.017 ; 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 : 2
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 1 A 441
REMARK 3 ORIGIN FOR THE GROUP (A): 33.6447 30.8321 18.6171
REMARK 3 T TENSOR
REMARK 3 T11: 0.0392 T22: 0.0366
REMARK 3 T33: 0.0902 T12: 0.0079
REMARK 3 T13: -0.0324 T23: -0.0137
REMARK 3 L TENSOR
REMARK 3 L11: 0.6457 L22: 0.6916
REMARK 3 L33: 0.9288 L12: 0.2305
REMARK 3 L13: -0.1800 L23: 0.2453
REMARK 3 S TENSOR
REMARK 3 S11: 0.0493 S12: -0.0613 S13: 0.1295
REMARK 3 S21: -0.0182 S22: -0.1130 S23: 0.0530
REMARK 3 S31: -0.0376 S32: 0.0134 S33: 0.0638
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 458 B 872
REMARK 3 ORIGIN FOR THE GROUP (A): 16.1970 13.2033 34.7492
REMARK 3 T TENSOR
REMARK 3 T11: 0.0381 T22: 0.0985
REMARK 3 T33: 0.0893 T12: -0.0037
REMARK 3 T13: 0.0171 T23: -0.0820
REMARK 3 L TENSOR
REMARK 3 L11: 0.3387 L22: 0.3440
REMARK 3 L33: 0.4907 L12: 0.1184
REMARK 3 L13: 0.0790 L23: 0.1888
REMARK 3 S TENSOR
REMARK 3 S11: 0.0159 S12: -0.1251 S13: 0.0658
REMARK 3 S21: 0.0622 S22: -0.1094 S23: 0.0960
REMARK 3 S31: 0.0894 S32: -0.0695 S33: 0.0936
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. RESIDUES 208-218,626-630 ARE DISORDERED.
REMARK 4
REMARK 4 2XHL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-JUN-10.
REMARK 100 THE DEPOSITION ID IS D_1290044286.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-JAN-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.978
REMARK 200 MONOCHROMATOR : SI(III)
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28644
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 37.640
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 5.800
REMARK 200 R MERGE (I) : 0.12000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.80
REMARK 200 R MERGE FOR SHELL (I) : 0.51000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.500
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: PDB ENTRY 1EPW
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG3350, 0.1M BIS-TRIS-PROPANE PH
REMARK 280 6.5, 0.2M SODIUM SULPHATE, PH 7.2
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 33.44500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 74.55000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 33.44500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 74.55000
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 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10480 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 37670 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -82.2 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 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 GLU A 208
REMARK 465 ASN A 209
REMARK 465 LYS A 210
REMARK 465 GLY A 211
REMARK 465 ALA A 212
REMARK 465 SER A 213
REMARK 465 ILE A 214
REMARK 465 PHE A 215
REMARK 465 ASN A 216
REMARK 465 ARG A 217
REMARK 465 ARG A 218
REMARK 465 ILE A 442
REMARK 465 THR A 443
REMARK 465 SER A 444
REMARK 465 LYS A 445
REMARK 465 THR A 446
REMARK 465 LYS A 447
REMARK 465 SER A 448
REMARK 465 LEU A 449
REMARK 465 ILE A 450
REMARK 465 GLU A 451
REMARK 465 GLY A 452
REMARK 465 ARG A 453
REMARK 465 ASN B 454
REMARK 465 LYS B 455
REMARK 465 ALA B 456
REMARK 465 LEU B 457
REMARK 465 MET B 626
REMARK 465 ASP B 627
REMARK 465 LYS B 628
REMARK 465 ILE B 629
REMARK 465 ALA B 630
REMARK 465 SER B 873
REMARK 465 LEU B 874
REMARK 465 GLU B 875
REMARK 465 ALA B 876
REMARK 465 LEU B 877
REMARK 465 ALA B 878
REMARK 465 SER B 879
REMARK 465 GLY B 880
REMARK 465 HIS B 881
REMARK 465 HIS B 882
REMARK 465 HIS B 883
REMARK 465 HIS B 884
REMARK 465 HIS B 885
REMARK 465 HIS B 886
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 17 -72.41 -140.58
REMARK 500 SER A 63 7.29 -64.81
REMARK 500 ASP A 75 97.39 -162.36
REMARK 500 ASP A 439 4.02 85.35
REMARK 500 ASP B 500 146.64 -171.07
REMARK 500 ASP B 511 4.41 -68.90
REMARK 500 LEU B 579 -70.84 -70.02
REMARK 500 ASN B 624 -159.44 -128.18
REMARK 500 SER B 633 -151.24 60.10
REMARK 500 LEU B 643 -30.24 -130.56
REMARK 500 GLU B 648 49.22 39.27
REMARK 500 ASP B 688 19.78 57.62
REMARK 500 THR B 722 -40.58 -139.69
REMARK 500 MET B 802 -56.63 -124.00
REMARK 500 ILE B 833 -131.37 49.17
REMARK 500 ASP B 861 72.01 32.00
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 ZN A1442 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 230 NE2
REMARK 620 2 HIS A 234 NE2 99.2
REMARK 620 3 GLU A 268 OE2 92.8 106.1
REMARK 620 4 GLU A 268 OE1 147.4 93.0 54.7
REMARK 620 5 HOH A2022 O 91.3 123.6 128.7 106.8
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1442
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1S0D RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF BOTULINUM NEUROTOXIN TYPE B AT PH 5.5
REMARK 900 RELATED ID: 1EPW RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CLOSTRIDIUM NEUROTOXIN TYPE B
REMARK 900 RELATED ID: 1G9B RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CLOSTRIDIUM BOTULINUM NEUROTOXIN BCOMPLEXED
REMARK 900 WITH AN INHIBITOR (EXPERIMENT 1)
REMARK 900 RELATED ID: 1F82 RELATED DB: PDB
REMARK 900 BOTULINUM NEUROTOXIN TYPE B CATALYTIC DOMAIN
REMARK 900 RELATED ID: 2ETF RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF FULL LENGTH BOTULINUM NEUROTOXIN (TYPEB) LIGHT
REMARK 900 CHAIN
REMARK 900 RELATED ID: 1I1E RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CLOSTRIDIUM BOTULINUM NEUROTOXIN BCOMPLEXED
REMARK 900 WITH DOXORUBICIN
REMARK 900 RELATED ID: 1S0F RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF BOTULINUM NEUROTOXIN TYPE B AT PH 7.0
REMARK 900 RELATED ID: 1G9A RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CLOSTRIDIUM BOTULINUM NEUROTOXIN BCOMPLEXED
REMARK 900 WITH AN INHIBITOR (EXPERIMENT 3)
REMARK 900 RELATED ID: 1G9C RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CLOSTRIDIUM BOTULINUM NEUROTOXIN BCOMPLEXED
REMARK 900 WITH AN INHIBITOR (EXPERIMENT 4)
REMARK 900 RELATED ID: 1S0B RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF BOTULINUM NEUROTOXIN TYPE B AT PH 4.0
REMARK 900 RELATED ID: 1S0G RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF BOTULINUM NEUROTOXIN TYPE B APO FORM
REMARK 900 RELATED ID: 1S0C RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF BOTULINUM NEUROTOXIN TYPE B AT PH 5.0
REMARK 900 RELATED ID: 1G9D RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CLOSTRIDIUM BOTULINUM NEUROTOXIN BCOMPLEXED
REMARK 900 WITH AN INHIBITOR (EXPERIMENT 2)
REMARK 900 RELATED ID: 1Z0H RELATED DB: PDB
REMARK 900 N-TERMINAL HELIX REORIENTS IN RECOMBINANT C -FRAGMENT OFCLOSTRIDIUM
REMARK 900 BOTULINUM TYPE B
REMARK 900 RELATED ID: 1F31 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CLOSTRIDIUM BOTULINUM NEUROTOXIN B COMPLEXED
REMARK 900 WITH A TRISACCHARIDE
REMARK 900 RELATED ID: 1S0E RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF BOTULINUM NEUROTOXIN TYPE B AT PH 6.0
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 OWING TO THE PRESENCE OF AN INTERNAL EXPRESSION TAG FOR
REMARK 999 CLEAVAGE BETWEEN THE TWO CHAINS THE NUMBERING OF THE B-CHAIN
REMARK 999 IS ADVANCED BY FIFTEEN POSITIONS COMPARED WITH THE
REMARK 999 UNENGINEERED CASE.
DBREF 2XHL A 1 437 UNP P10844 BXB_CLOBO 1 437
DBREF 2XHL B 461 873 UNP P10844 BXB_CLOBO 446 858
SEQADV 2XHL VAL A 438 UNP P10844 EXPRESSION TAG
SEQADV 2XHL ASP A 439 UNP P10844 EXPRESSION TAG
SEQADV 2XHL GLY A 440 UNP P10844 EXPRESSION TAG
SEQADV 2XHL ILE A 441 UNP P10844 EXPRESSION TAG
SEQADV 2XHL ILE A 442 UNP P10844 EXPRESSION TAG
SEQADV 2XHL THR A 443 UNP P10844 EXPRESSION TAG
SEQADV 2XHL SER A 444 UNP P10844 EXPRESSION TAG
SEQADV 2XHL LYS A 445 UNP P10844 EXPRESSION TAG
SEQADV 2XHL THR A 446 UNP P10844 EXPRESSION TAG
SEQADV 2XHL LYS A 447 UNP P10844 EXPRESSION TAG
SEQADV 2XHL SER A 448 UNP P10844 EXPRESSION TAG
SEQADV 2XHL LEU A 449 UNP P10844 EXPRESSION TAG
SEQADV 2XHL ILE A 450 UNP P10844 EXPRESSION TAG
SEQADV 2XHL GLU A 451 UNP P10844 EXPRESSION TAG
SEQADV 2XHL GLY A 452 UNP P10844 EXPRESSION TAG
SEQADV 2XHL ARG A 453 UNP P10844 EXPRESSION TAG
SEQADV 2XHL ASN B 454 UNP P10844 EXPRESSION TAG
SEQADV 2XHL LYS B 455 UNP P10844 EXPRESSION TAG
SEQADV 2XHL ALA B 456 UNP P10844 EXPRESSION TAG
SEQADV 2XHL LEU B 457 UNP P10844 EXPRESSION TAG
SEQADV 2XHL ASN B 458 UNP P10844 EXPRESSION TAG
SEQADV 2XHL LEU B 459 UNP P10844 EXPRESSION TAG
SEQADV 2XHL GLN B 460 UNP P10844 EXPRESSION TAG
SEQADV 2XHL LEU B 874 UNP P10844 EXPRESSION TAG
SEQADV 2XHL GLU B 875 UNP P10844 EXPRESSION TAG
SEQADV 2XHL ALA B 876 UNP P10844 EXPRESSION TAG
SEQADV 2XHL LEU B 877 UNP P10844 EXPRESSION TAG
SEQADV 2XHL ALA B 878 UNP P10844 EXPRESSION TAG
SEQADV 2XHL SER B 879 UNP P10844 EXPRESSION TAG
SEQADV 2XHL GLY B 880 UNP P10844 EXPRESSION TAG
SEQADV 2XHL HIS B 881 UNP P10844 EXPRESSION TAG
SEQADV 2XHL HIS B 882 UNP P10844 EXPRESSION TAG
SEQADV 2XHL HIS B 883 UNP P10844 EXPRESSION TAG
SEQADV 2XHL HIS B 884 UNP P10844 EXPRESSION TAG
SEQADV 2XHL HIS B 885 UNP P10844 EXPRESSION TAG
SEQADV 2XHL HIS B 886 UNP P10844 EXPRESSION TAG
SEQRES 1 A 453 MET PRO VAL THR ILE ASN ASN PHE ASN TYR ASN ASP PRO
SEQRES 2 A 453 ILE ASP ASN ASN ASN ILE ILE MET MET GLU PRO PRO PHE
SEQRES 3 A 453 ALA ARG GLY THR GLY ARG TYR TYR LYS ALA PHE LYS ILE
SEQRES 4 A 453 THR ASP ARG ILE TRP ILE ILE PRO GLU ARG TYR THR PHE
SEQRES 5 A 453 GLY TYR LYS PRO GLU ASP PHE ASN LYS SER SER GLY ILE
SEQRES 6 A 453 PHE ASN ARG ASP VAL CYS GLU TYR TYR ASP PRO ASP TYR
SEQRES 7 A 453 LEU ASN THR ASN ASP LYS LYS ASN ILE PHE LEU GLN THR
SEQRES 8 A 453 MET ILE LYS LEU PHE ASN ARG ILE LYS SER LYS PRO LEU
SEQRES 9 A 453 GLY GLU LYS LEU LEU GLU MET ILE ILE ASN GLY ILE PRO
SEQRES 10 A 453 TYR LEU GLY ASP ARG ARG VAL PRO LEU GLU GLU PHE ASN
SEQRES 11 A 453 THR ASN ILE ALA SER VAL THR VAL ASN LYS LEU ILE SER
SEQRES 12 A 453 ASN PRO GLY GLU VAL GLU ARG LYS LYS GLY ILE PHE ALA
SEQRES 13 A 453 ASN LEU ILE ILE PHE GLY PRO GLY PRO VAL LEU ASN GLU
SEQRES 14 A 453 ASN GLU THR ILE ASP ILE GLY ILE GLN ASN HIS PHE ALA
SEQRES 15 A 453 SER ARG GLU GLY PHE GLY GLY ILE MET GLN MET LYS PHE
SEQRES 16 A 453 CYS PRO GLU TYR VAL SER VAL PHE ASN ASN VAL GLN GLU
SEQRES 17 A 453 ASN LYS GLY ALA SER ILE PHE ASN ARG ARG GLY TYR PHE
SEQRES 18 A 453 SER ASP PRO ALA LEU ILE LEU MET HIS GLU LEU ILE HIS
SEQRES 19 A 453 VAL LEU HIS GLY LEU TYR GLY ILE LYS VAL ASP ASP LEU
SEQRES 20 A 453 PRO ILE VAL PRO ASN GLU LYS LYS PHE PHE MET GLN SER
SEQRES 21 A 453 THR ASP ALA ILE GLN ALA GLU GLU LEU TYR THR PHE GLY
SEQRES 22 A 453 GLY GLN ASP PRO SER ILE ILE THR PRO SER THR ASP LYS
SEQRES 23 A 453 SER ILE TYR ASP LYS VAL LEU GLN ASN PHE ARG GLY ILE
SEQRES 24 A 453 VAL ASP ARG LEU ASN LYS VAL LEU VAL CYS ILE SER ASP
SEQRES 25 A 453 PRO ASN ILE ASN ILE ASN ILE TYR LYS ASN LYS PHE LYS
SEQRES 26 A 453 ASP LYS TYR LYS PHE VAL GLU ASP SER GLU GLY LYS TYR
SEQRES 27 A 453 SER ILE ASP VAL GLU SER PHE ASP LYS LEU TYR LYS SER
SEQRES 28 A 453 LEU MET PHE GLY PHE THR GLU THR ASN ILE ALA GLU ASN
SEQRES 29 A 453 TYR LYS ILE LYS THR ARG ALA SER TYR PHE SER ASP SER
SEQRES 30 A 453 LEU PRO PRO VAL LYS ILE LYS ASN LEU LEU ASP ASN GLU
SEQRES 31 A 453 ILE TYR THR ILE GLU GLU GLY PHE ASN ILE SER ASP LYS
SEQRES 32 A 453 ASP MET GLU LYS GLU TYR ARG GLY GLN ASN LYS ALA ILE
SEQRES 33 A 453 ASN LYS GLN ALA TYR GLU GLU ILE SER LYS GLU HIS LEU
SEQRES 34 A 453 ALA VAL TYR LYS ILE GLN MET CYS VAL ASP GLY ILE ILE
SEQRES 35 A 453 THR SER LYS THR LYS SER LEU ILE GLU GLY ARG
SEQRES 1 B 433 ASN LYS ALA LEU ASN LEU GLN CYS ILE ASP VAL ASP ASN
SEQRES 2 B 433 GLU ASP LEU PHE PHE ILE ALA ASP LYS ASN SER PHE SER
SEQRES 3 B 433 ASP ASP LEU SER LYS ASN GLU ARG ILE GLU TYR ASN THR
SEQRES 4 B 433 GLN SER ASN TYR ILE GLU ASN ASP PHE PRO ILE ASN GLU
SEQRES 5 B 433 LEU ILE LEU ASP THR ASP LEU ILE SER LYS ILE GLU LEU
SEQRES 6 B 433 PRO SER GLU ASN THR GLU SER LEU THR ASP PHE ASN VAL
SEQRES 7 B 433 ASP VAL PRO VAL TYR GLU LYS GLN PRO ALA ILE LYS LYS
SEQRES 8 B 433 ILE PHE THR ASP GLU ASN THR ILE PHE GLN TYR LEU TYR
SEQRES 9 B 433 SER GLN THR PHE PRO LEU ASP ILE ARG ASP ILE SER LEU
SEQRES 10 B 433 THR SER SER PHE ASP ASP ALA LEU LEU PHE SER ASN LYS
SEQRES 11 B 433 VAL TYR SER PHE PHE SER MET ASP TYR ILE LYS THR ALA
SEQRES 12 B 433 ASN LYS VAL VAL GLU ALA GLY LEU PHE ALA GLY TRP VAL
SEQRES 13 B 433 LYS GLN ILE VAL ASN ASP PHE VAL ILE GLU ALA ASN LYS
SEQRES 14 B 433 SER ASN THR MET ASP LYS ILE ALA ASP ILE SER LEU ILE
SEQRES 15 B 433 VAL PRO TYR ILE GLY LEU ALA LEU ASN VAL GLY ASN GLU
SEQRES 16 B 433 THR ALA LYS GLY ASN PHE GLU ASN ALA PHE GLU ILE ALA
SEQRES 17 B 433 GLY ALA SER ILE LEU LEU GLU PHE ILE PRO GLU LEU LEU
SEQRES 18 B 433 ILE PRO VAL VAL GLY ALA PHE LEU LEU GLU SER TYR ILE
SEQRES 19 B 433 ASP ASN LYS ASN LYS ILE ILE LYS THR ILE ASP ASN ALA
SEQRES 20 B 433 LEU THR LYS ARG ASN GLU LYS TRP SER ASP MET TYR GLY
SEQRES 21 B 433 LEU ILE VAL ALA GLN TRP LEU SER THR VAL ASN THR GLN
SEQRES 22 B 433 PHE TYR THR ILE LYS GLU GLY MET TYR LYS ALA LEU ASN
SEQRES 23 B 433 TYR GLN ALA GLN ALA LEU GLU GLU ILE ILE LYS TYR ARG
SEQRES 24 B 433 TYR ASN ILE TYR SER GLU LYS GLU LYS SER ASN ILE ASN
SEQRES 25 B 433 ILE ASP PHE ASN ASP ILE ASN SER LYS LEU ASN GLU GLY
SEQRES 26 B 433 ILE ASN GLN ALA ILE ASP ASN ILE ASN ASN PHE ILE ASN
SEQRES 27 B 433 GLY CYS SER VAL SER TYR LEU MET LYS LYS MET ILE PRO
SEQRES 28 B 433 LEU ALA VAL GLU LYS LEU LEU ASP PHE ASP ASN THR LEU
SEQRES 29 B 433 LYS LYS ASN LEU LEU ASN TYR ILE ASP GLU ASN LYS LEU
SEQRES 30 B 433 TYR LEU ILE GLY SER ALA GLU TYR GLU LYS SER LYS VAL
SEQRES 31 B 433 ASN LYS TYR LEU LYS THR ILE MET PRO PHE ASP LEU SER
SEQRES 32 B 433 ILE TYR THR ASN ASP THR ILE LEU ILE GLU MET PHE ASN
SEQRES 33 B 433 LYS TYR ASN SER LEU GLU ALA LEU ALA SER GLY HIS HIS
SEQRES 34 B 433 HIS HIS HIS HIS
HET ZN A1442 1
HETNAM ZN ZINC ION
FORMUL 3 ZN ZN 2+
FORMUL 4 HOH *31(H2 O)
HELIX 1 1 PRO A 24 ARG A 28 5 5
HELIX 2 2 LYS A 55 ASN A 60 5 6
HELIX 3 3 THR A 81 LYS A 100 1 20
HELIX 4 4 LYS A 102 GLY A 115 1 14
HELIX 5 5 ALA A 182 GLU A 185 5 4
HELIX 6 6 ASP A 223 TYR A 240 1 18
HELIX 7 7 GLN A 265 GLY A 273 1 9
HELIX 8 8 GLN A 275 ILE A 280 5 6
HELIX 9 9 THR A 281 ASN A 304 1 24
HELIX 10 10 ASN A 316 TYR A 328 1 13
HELIX 11 11 ASP A 341 GLY A 355 1 15
HELIX 12 12 THR A 357 TYR A 365 1 9
HELIX 13 13 ILE A 400 ASP A 404 5 5
HELIX 14 14 GLU A 406 GLN A 412 5 7
HELIX 15 15 SER A 425 GLU A 427 5 3
HELIX 16 16 GLU B 467 LEU B 469 5 3
HELIX 17 17 ASP B 474 PHE B 478 5 5
HELIX 18 18 ASP B 480 LYS B 484 5 5
HELIX 19 19 PRO B 502 ASP B 509 1 8
HELIX 20 20 THR B 510 ILE B 513 5 4
HELIX 21 21 THR B 551 SER B 558 1 8
HELIX 22 22 SER B 573 PHE B 580 1 8
HELIX 23 23 SER B 589 ALA B 596 1 8
HELIX 24 24 LEU B 604 ASN B 621 1 18
HELIX 25 25 TYR B 638 ASN B 644 1 7
HELIX 26 26 ASN B 653 GLY B 662 1 10
HELIX 27 27 ALA B 663 LEU B 666 5 4
HELIX 28 28 ASN B 689 SER B 721 1 33
HELIX 29 29 VAL B 723 TYR B 756 1 34
HELIX 30 30 SER B 757 ILE B 764 1 8
HELIX 31 31 ASP B 767 MET B 802 1 36
HELIX 32 32 MET B 802 ASN B 828 1 27
HELIX 33 33 SER B 835 LEU B 847 1 13
HELIX 34 34 ASP B 854 TYR B 858 5 5
HELIX 35 35 ILE B 863 ASN B 869 1 7
SHEET 1 AA 9 GLU A 171 ILE A 173 0
SHEET 2 AA 9 MET A 191 LYS A 194 -1 O GLN A 192 N ILE A 173
SHEET 3 AA 9 LEU A 158 PHE A 161 1 O ILE A 159 N MET A 193
SHEET 4 AA 9 ILE A 43 ILE A 46 1 O TRP A 44 N ILE A 160
SHEET 5 AA 9 TYR A 34 THR A 40 -1 O PHE A 37 N ILE A 45
SHEET 6 AA 9 ILE A 19 GLU A 23 -1 O ILE A 20 N ALA A 36
SHEET 7 AA 9 THR A 137 LEU A 141 -1 O ASN A 139 N GLU A 23
SHEET 8 AA 9 LYS A 151 PHE A 155 -1 O LYS A 152 N LYS A 140
SHEET 9 AA 9 ASN B 522 THR B 523 -1 O THR B 523 N GLY A 153
SHEET 1 AB 2 GLY A 64 ILE A 65 0
SHEET 2 AB 2 GLN B 539 PRO B 540 -1 O GLN B 539 N ILE A 65
SHEET 1 AC 2 GLU A 72 TYR A 73 0
SHEET 2 AC 2 LEU A 429 ALA A 430 -1 O ALA A 430 N GLU A 72
SHEET 1 AD 2 GLU A 128 PHE A 129 0
SHEET 2 AD 2 VAL A 308 CYS A 309 1 O VAL A 308 N PHE A 129
SHEET 1 AE 4 TYR A 220 PHE A 221 0
SHEET 2 AE 4 TYR A 199 PHE A 203 -1 O PHE A 203 N TYR A 220
SHEET 3 AE 4 LEU A 378 ILE A 383 -1 O LEU A 378 N VAL A 202
SHEET 4 AE 4 TYR A 421 GLU A 422 -1 O GLU A 422 N LYS A 382
SHEET 1 AF 2 VAL A 331 GLU A 332 0
SHEET 2 AF 2 TYR A 338 SER A 339 -1 O SER A 339 N VAL A 331
SHEET 1 BA 3 CYS B 461 ASP B 465 0
SHEET 2 BA 3 LYS A 433 CYS A 437 -1 O ILE A 434 N VAL B 464
SHEET 3 BA 3 ILE B 542 PHE B 546 1 O LYS B 543 N GLN A 435
SHEET 1 BB 2 GLU B 486 ILE B 488 0
SHEET 2 BB 2 PHE B 681 LEU B 683 1 O LEU B 682 N ILE B 488
SHEET 1 BC 2 SER B 569 THR B 571 0
SHEET 2 BC 2 LYS B 583 TYR B 585 1 O VAL B 584 N THR B 571
SSBOND 1 CYS A 437 CYS B 461 1555 1555 2.04
LINK NE2 HIS A 230 ZN ZN A1442 1555 1555 2.29
LINK NE2 HIS A 234 ZN ZN A1442 1555 1555 2.20
LINK OE2 GLU A 268 ZN ZN A1442 1555 1555 2.31
LINK OE1 GLU A 268 ZN ZN A1442 1555 1555 2.48
LINK ZN ZN A1442 O HOH A2022 1555 1555 2.14
SITE 1 AC1 4 HIS A 230 HIS A 234 GLU A 268 HOH A2022
CRYST1 66.890 149.100 113.490 90.00 90.00 90.00 P 21 21 2 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 0.014950 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006707 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008811 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
