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HEADER HYDROLASE 20-OCT-17 6ESJ
TITLE HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX WITH PROPIDIUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHOLINESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ACYLCHOLINE ACYLHYDROLASE,BUTYRYLCHOLINE ESTERASE,CHOLINE
COMPND 5 ESTERASE II,PSEUDOCHOLINESTERASE;
COMPND 6 EC: 3.1.1.8;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: BCHE, CHE1;
SOURCE 6 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FRUIT FLY;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7227;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: S2
KEYWDS BUTYRYLCHOLINESTERASE, INHIBITOR, COMPLEX, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR F.NACHON,X.BRAZZOLOTTO,M.WANDHAMMER,M.TROVASLET-LEROY,I.R.MACDONALD,
AUTHOR 2 S.DARVESH,T.L.ROSENBERRY
REVDAT 1 13-DEC-17 6ESJ 0
JRNL AUTH T.L.ROSENBERRY,X.BRAZZOLOTTO,I.R.MACDONALD,M.WANDHAMMER,
JRNL AUTH 2 M.TROVASLET-LEROY,S.DARVESH,F.NACHON
JRNL TITL COMPARISON OF THE BINDING OF REVERSIBLE INHIBITORS TO HUMAN
JRNL TITL 2 BUTYRYLCHOLINESTERASE AND ACETYLCHOLINESTERASE: A
JRNL TITL 3 CRYSTALLOGRAPHIC, KINETIC AND CALORIMETRIC STUDY.
JRNL REF MOLECULES V. 22 2017
JRNL REFN ESSN 1420-3049
JRNL PMID 29186056
JRNL DOI 10.3390/MOLECULES22122098
REMARK 2
REMARK 2 RESOLUTION. 2.98 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.12_2829
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.98
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.06
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.369
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.8
REMARK 3 NUMBER OF REFLECTIONS : 27720
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.224
REMARK 3 R VALUE (WORKING SET) : 0.221
REMARK 3 FREE R VALUE : 0.299
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.499
REMARK 3 FREE R VALUE TEST SET COUNT : 970
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 38.0614 - 5.6948 0.95 3946 141 0.2030 0.2728
REMARK 3 2 5.6948 - 4.5225 0.96 3833 140 0.1941 0.2204
REMARK 3 3 4.5225 - 3.9515 0.97 3786 137 0.1917 0.3045
REMARK 3 4 3.9515 - 3.5905 0.97 3804 138 0.2277 0.3335
REMARK 3 5 3.5905 - 3.3333 0.98 3834 140 0.2552 0.3349
REMARK 3 6 3.3333 - 3.1369 0.99 3842 139 0.2902 0.4006
REMARK 3 7 3.1369 - 2.9798 0.95 3705 135 0.3264 0.4286
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.491
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.909
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 72.68
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 81.25
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 : 0.004 8932
REMARK 3 ANGLE : 0.890 12171
REMARK 3 CHIRALITY : 0.064 1324
REMARK 3 PLANARITY : 0.005 1548
REMARK 3 DIHEDRAL : 5.243 6144
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A'
REMARK 3 ORIGIN FOR THE GROUP (A): -5.4935 -5.1996 -16.0937
REMARK 3 T TENSOR
REMARK 3 T11: 0.6054 T22: 0.7090
REMARK 3 T33: 0.4612 T12: -0.0652
REMARK 3 T13: 0.0064 T23: -0.0044
REMARK 3 L TENSOR
REMARK 3 L11: 2.9754 L22: 1.8253
REMARK 3 L33: 2.3306 L12: 0.6010
REMARK 3 L13: -0.6932 L23: -0.3387
REMARK 3 S TENSOR
REMARK 3 S11: 0.0571 S12: -0.8482 S13: -0.1704
REMARK 3 S21: 0.3373 S22: -0.0668 S23: 0.0268
REMARK 3 S31: 0.0487 S32: 0.1964 S33: -0.0012
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'B'
REMARK 3 ORIGIN FOR THE GROUP (A): -25.8136 30.8845 -43.6955
REMARK 3 T TENSOR
REMARK 3 T11: 0.4155 T22: 0.4505
REMARK 3 T33: 0.5289 T12: -0.0106
REMARK 3 T13: -0.0289 T23: -0.0139
REMARK 3 L TENSOR
REMARK 3 L11: 2.0407 L22: 2.4683
REMARK 3 L33: 2.6937 L12: 0.4087
REMARK 3 L13: -0.4470 L23: -0.1137
REMARK 3 S TENSOR
REMARK 3 S11: 0.1882 S12: -0.0546 S13: 0.2077
REMARK 3 S21: 0.0856 S22: -0.1814 S23: 0.0512
REMARK 3 S31: -0.1893 S32: -0.3161 S33: 0.0005
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 6ESJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-OCT-17.
REMARK 100 THE DEPOSITION ID IS D_1200007182.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-FEB-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00442
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27721
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.979
REMARK 200 RESOLUTION RANGE LOW (A) : 38.060
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.7
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.09197
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.8300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.98
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.09
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : 0.56700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.010
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: 5DYW
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.98
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.86
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM SULFATE, 12%
REMARK 280 POLYETHYLENE GLYCOL 4000, PH 7.4, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
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
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 37.52000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 114.17500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.61000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 114.17500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 37.52000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.61000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 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 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 -39.61000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -114.17500
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
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 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 39.61000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -114.17500
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 1
REMARK 465 ASP A 2
REMARK 465 GLU B 1
REMARK 465 ASP B 2
REMARK 465 ASP B 3
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 ARG A 40 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 54 CG OD1 OD2
REMARK 470 SER A 253 OG
REMARK 470 ARG A 254 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 506 CG CD OE1 OE2
REMARK 470 ASP B 54 CG OD1 OD2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O ARG A 240 OG1 THR A 243 1.98
REMARK 500 OE1 GLU B 441 O HOH B 701 2.10
REMARK 500 ND2 ASN B 341 C2 NAG B 606 2.14
REMARK 500 O THR B 250 NZ LYS B 267 2.15
REMARK 500 O VAL A 148 O HOH A 701 2.16
REMARK 500 ND2 ASN B 17 O5 NAG B 601 2.18
REMARK 500 OE1 GLN B 270 O6 NAG A 606 2.19
REMARK 500 O ASN B 455 O HOH B 702 2.19
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 PHE A 21 20.80 48.65
REMARK 500 THR A 50 -71.83 -79.36
REMARK 500 LYS A 60 149.75 -171.88
REMARK 500 ASP A 91 93.54 -67.41
REMARK 500 LEU A 93 70.43 -100.72
REMARK 500 LYS A 105 -64.07 -94.17
REMARK 500 PHE A 118 19.24 56.15
REMARK 500 ALA A 162 72.33 -162.57
REMARK 500 ASN A 181 28.90 -141.83
REMARK 500 SER A 198 -23.14 73.22
REMARK 500 ALA A 199 -26.55 -145.15
REMARK 500 ASN A 256 -163.57 -125.41
REMARK 500 GLU A 276 0.84 -69.22
REMARK 500 TYR A 282 58.37 -93.88
REMARK 500 PRO A 285 -15.92 -48.87
REMARK 500 GLN A 311 66.99 -100.13
REMARK 500 ASP A 375 85.44 -67.70
REMARK 500 GLU A 482 -72.73 -78.35
REMARK 500 ASN A 485 0.24 85.06
REMARK 500 ASN A 486 -1.04 -144.36
REMARK 500 PHE B 43 -6.70 74.14
REMARK 500 ASP B 54 -177.90 -69.09
REMARK 500 PHE B 118 18.77 59.28
REMARK 500 PHE B 153 25.34 -141.51
REMARK 500 ALA B 162 76.40 -152.13
REMARK 500 ASN B 181 -32.43 -133.02
REMARK 500 SER B 198 -17.56 70.78
REMARK 500 ALA B 199 -25.00 -140.11
REMARK 500 CYS B 252 23.34 -143.65
REMARK 500 ARG B 381 108.14 -55.90
REMARK 500 PHE B 398 -50.95 -122.49
REMARK 500 PRO B 527 -8.96 -59.54
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 PRM A 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 611
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 612
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GLY B 614
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PRM B 615
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 601 bound
REMARK 800 to ASN A 17
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 602 through NAG A 603 bound to ASN A 106
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 604 bound
REMARK 800 to ASN A 241
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 605 bound
REMARK 800 to ASN A 341
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 606 through NAG A 607 bound to ASN A 481
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 601 bound
REMARK 800 to ASN B 17
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 602 bound
REMARK 800 to ASN B 57
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B
REMARK 800 603 through NAG B 604 bound to ASN B 241
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 605 bound
REMARK 800 to ASN B 256
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 606 bound
REMARK 800 to ASN B 341
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B
REMARK 800 607 through NAG B 608 bound to ASN B 455
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 609 bound
REMARK 800 to ASN B 481
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6EP4 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN IN COMPLEX WITH DIFFERENT LIGAND
REMARK 900 RELATED ID: 6EQP RELATED DB: PDB
REMARK 900 THE SAME PROTEIN IN COMPLEX WITH DIFFERENT LIGAND
REMARK 900 RELATED ID: 6EQQ RELATED DB: PDB
REMARK 900 THE SAME PROTEIN IN COMPLEX WITH DIFFERENT LIGAND
DBREF 6ESJ A 1 529 UNP P06276 CHLE_HUMAN 29 557
DBREF 6ESJ B 1 529 UNP P06276 CHLE_HUMAN 29 557
SEQRES 1 A 529 GLU ASP ASP ILE ILE ILE ALA THR LYS ASN GLY LYS VAL
SEQRES 2 A 529 ARG GLY MET ASN LEU THR VAL PHE GLY GLY THR VAL THR
SEQRES 3 A 529 ALA PHE LEU GLY ILE PRO TYR ALA GLN PRO PRO LEU GLY
SEQRES 4 A 529 ARG LEU ARG PHE LYS LYS PRO GLN SER LEU THR LYS TRP
SEQRES 5 A 529 SER ASP ILE TRP ASN ALA THR LYS TYR ALA ASN SER CYS
SEQRES 6 A 529 CYS GLN ASN ILE ASP GLN SER PHE PRO GLY PHE HIS GLY
SEQRES 7 A 529 SER GLU MET TRP ASN PRO ASN THR ASP LEU SER GLU ASP
SEQRES 8 A 529 CYS LEU TYR LEU ASN VAL TRP ILE PRO ALA PRO LYS PRO
SEQRES 9 A 529 LYS ASN ALA THR VAL LEU ILE TRP ILE TYR GLY GLY GLY
SEQRES 10 A 529 PHE GLN THR GLY THR SER SER LEU HIS VAL TYR ASP GLY
SEQRES 11 A 529 LYS PHE LEU ALA ARG VAL GLU ARG VAL ILE VAL VAL SER
SEQRES 12 A 529 MET ASN TYR ARG VAL GLY ALA LEU GLY PHE LEU ALA LEU
SEQRES 13 A 529 PRO GLY ASN PRO GLU ALA PRO GLY ASN MET GLY LEU PHE
SEQRES 14 A 529 ASP GLN GLN LEU ALA LEU GLN TRP VAL GLN LYS ASN ILE
SEQRES 15 A 529 ALA ALA PHE GLY GLY ASN PRO LYS SER VAL THR LEU PHE
SEQRES 16 A 529 GLY GLU SER ALA GLY ALA ALA SER VAL SER LEU HIS LEU
SEQRES 17 A 529 LEU SER PRO GLY SER HIS SER LEU PHE THR ARG ALA ILE
SEQRES 18 A 529 LEU GLN SER GLY SER PHE ASN ALA PRO TRP ALA VAL THR
SEQRES 19 A 529 SER LEU TYR GLU ALA ARG ASN ARG THR LEU ASN LEU ALA
SEQRES 20 A 529 LYS LEU THR GLY CYS SER ARG GLU ASN GLU THR GLU ILE
SEQRES 21 A 529 ILE LYS CYS LEU ARG ASN LYS ASP PRO GLN GLU ILE LEU
SEQRES 22 A 529 LEU ASN GLU ALA PHE VAL VAL PRO TYR GLY THR PRO LEU
SEQRES 23 A 529 SER VAL ASN PHE GLY PRO THR VAL ASP GLY ASP PHE LEU
SEQRES 24 A 529 THR ASP MET PRO ASP ILE LEU LEU GLU LEU GLY GLN PHE
SEQRES 25 A 529 LYS LYS THR GLN ILE LEU VAL GLY VAL ASN LYS ASP GLU
SEQRES 26 A 529 GLY THR ALA PHE LEU VAL TYR GLY ALA PRO GLY PHE SER
SEQRES 27 A 529 LYS ASP ASN ASN SER ILE ILE THR ARG LYS GLU PHE GLN
SEQRES 28 A 529 GLU GLY LEU LYS ILE PHE PHE PRO GLY VAL SER GLU PHE
SEQRES 29 A 529 GLY LYS GLU SER ILE LEU PHE HIS TYR THR ASP TRP VAL
SEQRES 30 A 529 ASP ASP GLN ARG PRO GLU ASN TYR ARG GLU ALA LEU GLY
SEQRES 31 A 529 ASP VAL VAL GLY ASP TYR ASN PHE ILE CYS PRO ALA LEU
SEQRES 32 A 529 GLU PHE THR LYS LYS PHE SER GLU TRP GLY ASN ASN ALA
SEQRES 33 A 529 PHE PHE TYR TYR PHE GLU HIS ARG SER SER LYS LEU PRO
SEQRES 34 A 529 TRP PRO GLU TRP MET GLY VAL MET HIS GLY TYR GLU ILE
SEQRES 35 A 529 GLU PHE VAL PHE GLY LEU PRO LEU GLU ARG ARG ASP ASN
SEQRES 36 A 529 TYR THR LYS ALA GLU GLU ILE LEU SER ARG SER ILE VAL
SEQRES 37 A 529 LYS ARG TRP ALA ASN PHE ALA LYS TYR GLY ASN PRO ASN
SEQRES 38 A 529 GLU THR GLN ASN ASN SER THR SER TRP PRO VAL PHE LYS
SEQRES 39 A 529 SER THR GLU GLN LYS TYR LEU THR LEU ASN THR GLU SER
SEQRES 40 A 529 THR ARG ILE MET THR LYS LEU ARG ALA GLN GLN CYS ARG
SEQRES 41 A 529 PHE TRP THR SER PHE PHE PRO LYS VAL
SEQRES 1 B 529 GLU ASP ASP ILE ILE ILE ALA THR LYS ASN GLY LYS VAL
SEQRES 2 B 529 ARG GLY MET ASN LEU THR VAL PHE GLY GLY THR VAL THR
SEQRES 3 B 529 ALA PHE LEU GLY ILE PRO TYR ALA GLN PRO PRO LEU GLY
SEQRES 4 B 529 ARG LEU ARG PHE LYS LYS PRO GLN SER LEU THR LYS TRP
SEQRES 5 B 529 SER ASP ILE TRP ASN ALA THR LYS TYR ALA ASN SER CYS
SEQRES 6 B 529 CYS GLN ASN ILE ASP GLN SER PHE PRO GLY PHE HIS GLY
SEQRES 7 B 529 SER GLU MET TRP ASN PRO ASN THR ASP LEU SER GLU ASP
SEQRES 8 B 529 CYS LEU TYR LEU ASN VAL TRP ILE PRO ALA PRO LYS PRO
SEQRES 9 B 529 LYS ASN ALA THR VAL LEU ILE TRP ILE TYR GLY GLY GLY
SEQRES 10 B 529 PHE GLN THR GLY THR SER SER LEU HIS VAL TYR ASP GLY
SEQRES 11 B 529 LYS PHE LEU ALA ARG VAL GLU ARG VAL ILE VAL VAL SER
SEQRES 12 B 529 MET ASN TYR ARG VAL GLY ALA LEU GLY PHE LEU ALA LEU
SEQRES 13 B 529 PRO GLY ASN PRO GLU ALA PRO GLY ASN MET GLY LEU PHE
SEQRES 14 B 529 ASP GLN GLN LEU ALA LEU GLN TRP VAL GLN LYS ASN ILE
SEQRES 15 B 529 ALA ALA PHE GLY GLY ASN PRO LYS SER VAL THR LEU PHE
SEQRES 16 B 529 GLY GLU SER ALA GLY ALA ALA SER VAL SER LEU HIS LEU
SEQRES 17 B 529 LEU SER PRO GLY SER HIS SER LEU PHE THR ARG ALA ILE
SEQRES 18 B 529 LEU GLN SER GLY SER PHE ASN ALA PRO TRP ALA VAL THR
SEQRES 19 B 529 SER LEU TYR GLU ALA ARG ASN ARG THR LEU ASN LEU ALA
SEQRES 20 B 529 LYS LEU THR GLY CYS SER ARG GLU ASN GLU THR GLU ILE
SEQRES 21 B 529 ILE LYS CYS LEU ARG ASN LYS ASP PRO GLN GLU ILE LEU
SEQRES 22 B 529 LEU ASN GLU ALA PHE VAL VAL PRO TYR GLY THR PRO LEU
SEQRES 23 B 529 SER VAL ASN PHE GLY PRO THR VAL ASP GLY ASP PHE LEU
SEQRES 24 B 529 THR ASP MET PRO ASP ILE LEU LEU GLU LEU GLY GLN PHE
SEQRES 25 B 529 LYS LYS THR GLN ILE LEU VAL GLY VAL ASN LYS ASP GLU
SEQRES 26 B 529 GLY THR ALA PHE LEU VAL TYR GLY ALA PRO GLY PHE SER
SEQRES 27 B 529 LYS ASP ASN ASN SER ILE ILE THR ARG LYS GLU PHE GLN
SEQRES 28 B 529 GLU GLY LEU LYS ILE PHE PHE PRO GLY VAL SER GLU PHE
SEQRES 29 B 529 GLY LYS GLU SER ILE LEU PHE HIS TYR THR ASP TRP VAL
SEQRES 30 B 529 ASP ASP GLN ARG PRO GLU ASN TYR ARG GLU ALA LEU GLY
SEQRES 31 B 529 ASP VAL VAL GLY ASP TYR ASN PHE ILE CYS PRO ALA LEU
SEQRES 32 B 529 GLU PHE THR LYS LYS PHE SER GLU TRP GLY ASN ASN ALA
SEQRES 33 B 529 PHE PHE TYR TYR PHE GLU HIS ARG SER SER LYS LEU PRO
SEQRES 34 B 529 TRP PRO GLU TRP MET GLY VAL MET HIS GLY TYR GLU ILE
SEQRES 35 B 529 GLU PHE VAL PHE GLY LEU PRO LEU GLU ARG ARG ASP ASN
SEQRES 36 B 529 TYR THR LYS ALA GLU GLU ILE LEU SER ARG SER ILE VAL
SEQRES 37 B 529 LYS ARG TRP ALA ASN PHE ALA LYS TYR GLY ASN PRO ASN
SEQRES 38 B 529 GLU THR GLN ASN ASN SER THR SER TRP PRO VAL PHE LYS
SEQRES 39 B 529 SER THR GLU GLN LYS TYR LEU THR LEU ASN THR GLU SER
SEQRES 40 B 529 THR ARG ILE MET THR LYS LEU ARG ALA GLN GLN CYS ARG
SEQRES 41 B 529 PHE TRP THR SER PHE PHE PRO LYS VAL
HET NAG A 601 14
HET NAG A 602 14
HET NAG A 603 14
HET NAG A 604 14
HET NAG A 605 14
HET NAG A 606 14
HET NAG A 607 14
HET PRM A 608 31
HET NAG B 601 14
HET NAG B 602 14
HET NAG B 603 14
HET NAG B 604 14
HET NAG B 605 14
HET NAG B 606 14
HET NAG B 607 14
HET NAG B 608 14
HET NAG B 609 14
HET CL B 610 1
HET CL B 611 1
HET CL B 612 1
HET CL B 613 1
HET GLY B 614 5
HET PRM B 615 31
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM PRM 3,8-DIAMINO-5[3-(DIETHYLMETHYLAMMONIO)PROPYL]-6-
HETNAM 2 PRM PHENYLPHENANTHRIDINIUM
HETNAM CL CHLORIDE ION
HETNAM GLY GLYCINE
HETSYN PRM PROPIDIUM
FORMUL 3 NAG 16(C8 H15 N O6)
FORMUL 8 PRM 2(C27 H34 N4 2+)
FORMUL 16 CL 4(CL 1-)
FORMUL 20 GLY C2 H5 N O2
FORMUL 22 HOH *141(H2 O)
HELIX 1 AA1 PHE A 76 TRP A 82 1 7
HELIX 2 AA2 GLY A 130 GLU A 137 1 8
HELIX 3 AA3 GLY A 149 LEU A 154 1 6
HELIX 4 AA4 ASN A 165 ILE A 182 1 18
HELIX 5 AA5 ALA A 199 LEU A 208 1 10
HELIX 6 AA6 LEU A 209 HIS A 214 5 6
HELIX 7 AA7 SER A 235 ARG A 240 1 6
HELIX 8 AA8 ARG A 240 THR A 250 1 11
HELIX 9 AA9 ILE A 260 LYS A 267 1 8
HELIX 10 AB1 ASP A 268 LEU A 274 1 7
HELIX 11 AB2 MET A 302 LEU A 309 1 8
HELIX 12 AB3 ASP A 324 LEU A 330 5 7
HELIX 13 AB4 THR A 346 ILE A 356 1 11
HELIX 14 AB5 SER A 362 TYR A 373 1 12
HELIX 15 AB6 GLU A 383 PHE A 398 1 16
HELIX 16 AB7 PHE A 398 GLU A 411 1 14
HELIX 17 AB8 PRO A 431 GLY A 435 5 5
HELIX 18 AB9 GLU A 441 PHE A 446 1 6
HELIX 19 AC1 THR A 457 GLY A 478 1 22
HELIX 20 AC2 ARG A 515 PHE A 525 1 11
HELIX 21 AC3 PHE A 526 VAL A 529 5 4
HELIX 22 AC4 LEU B 38 ARG B 42 5 5
HELIX 23 AC5 PHE B 76 MET B 81 1 6
HELIX 24 AC6 LEU B 125 ASP B 129 5 5
HELIX 25 AC7 PHE B 132 ARG B 138 1 7
HELIX 26 AC8 GLY B 149 LEU B 154 1 6
HELIX 27 AC9 ASN B 165 LYS B 180 1 16
HELIX 28 AD1 ASN B 181 GLY B 186 1 6
HELIX 29 AD2 ALA B 199 LEU B 208 1 10
HELIX 30 AD3 SER B 210 HIS B 214 5 5
HELIX 31 AD4 SER B 235 THR B 250 1 16
HELIX 32 AD5 ASN B 256 LYS B 267 1 12
HELIX 33 AD6 ASP B 268 LEU B 274 1 7
HELIX 34 AD7 MET B 302 GLY B 310 1 9
HELIX 35 AD8 ASP B 324 LEU B 330 5 7
HELIX 36 AD9 THR B 346 PHE B 358 1 13
HELIX 37 AE1 SER B 362 TYR B 373 1 12
HELIX 38 AE2 GLU B 383 TYR B 396 1 14
HELIX 39 AE3 PHE B 398 GLU B 411 1 14
HELIX 40 AE4 PRO B 431 GLY B 435 5 5
HELIX 41 AE5 GLU B 441 PHE B 446 1 6
HELIX 42 AE6 GLY B 447 GLU B 451 5 5
HELIX 43 AE7 THR B 457 GLY B 478 1 22
HELIX 44 AE8 ARG B 515 PHE B 525 1 11
SHEET 1 AA1 3 ILE A 6 ALA A 7 0
SHEET 2 AA1 3 LYS A 12 ARG A 14 -1 O VAL A 13 N ILE A 6
SHEET 3 AA1 3 TRP A 56 ASN A 57 1 O TRP A 56 N LYS A 12
SHEET 1 AA211 MET A 16 LEU A 18 0
SHEET 2 AA211 VAL A 25 PRO A 32 -1 O VAL A 25 N LEU A 18
SHEET 3 AA211 TYR A 94 PRO A 100 -1 O ILE A 99 N THR A 26
SHEET 4 AA211 ILE A 140 MET A 144 -1 O SER A 143 N ASN A 96
SHEET 5 AA211 ALA A 107 ILE A 113 1 N LEU A 110 O VAL A 142
SHEET 6 AA211 GLY A 187 GLU A 197 1 O THR A 193 N VAL A 109
SHEET 7 AA211 ARG A 219 GLN A 223 1 O ARG A 219 N LEU A 194
SHEET 8 AA211 ILE A 317 ASN A 322 1 O GLY A 320 N LEU A 222
SHEET 9 AA211 ALA A 416 PHE A 421 1 O PHE A 421 N VAL A 321
SHEET 10 AA211 LYS A 499 LEU A 503 1 O LEU A 501 N PHE A 418
SHEET 11 AA211 ILE A 510 THR A 512 -1 O MET A 511 N TYR A 500
SHEET 1 AA3 2 SER A 64 CYS A 65 0
SHEET 2 AA3 2 LEU A 88 SER A 89 1 O SER A 89 N SER A 64
SHEET 1 AA412 TRP B 56 ALA B 58 0
SHEET 2 AA412 VAL B 13 THR B 19 1 N ARG B 14 O ALA B 58
SHEET 3 AA412 THR B 24 PRO B 32 -1 O VAL B 25 N LEU B 18
SHEET 4 AA412 TYR B 94 PRO B 100 -1 O ILE B 99 N THR B 26
SHEET 5 AA412 ILE B 140 MET B 144 -1 O SER B 143 N ASN B 96
SHEET 6 AA412 ALA B 107 ILE B 113 1 N LEU B 110 O ILE B 140
SHEET 7 AA412 GLY B 187 GLY B 196 1 O THR B 193 N ILE B 111
SHEET 8 AA412 ARG B 219 GLN B 223 1 O ARG B 219 N LEU B 194
SHEET 9 AA412 ILE B 317 ASN B 322 1 O LEU B 318 N LEU B 222
SHEET 10 AA412 ALA B 416 PHE B 421 1 O PHE B 421 N VAL B 321
SHEET 11 AA412 LYS B 499 LEU B 503 1 O LEU B 503 N TYR B 420
SHEET 12 AA412 ILE B 510 THR B 512 -1 O MET B 511 N TYR B 500
SSBOND 1 CYS A 65 CYS A 92 1555 1555 2.03
SSBOND 2 CYS A 252 CYS A 263 1555 1555 2.03
SSBOND 3 CYS A 400 CYS A 519 1555 1555 2.03
SSBOND 4 CYS B 65 CYS B 92 1555 1555 2.02
SSBOND 5 CYS B 252 CYS B 263 1555 1555 2.03
SSBOND 6 CYS B 400 CYS B 519 1555 1555 2.03
LINK ND2 ASN A 17 C1 NAG A 601 1555 1555 1.44
LINK ND2 ASN A 106 C1 NAG A 602 1555 1555 1.45
LINK ND2 ASN A 241 C1 NAG A 604 1555 1555 1.44
LINK ND2 ASN A 341 C1 NAG A 605 1555 1555 1.45
LINK ND2 ASN A 481 C1 NAG A 606 1555 1555 1.45
LINK ND2 ASN B 17 C1 NAG B 601 1555 1555 1.44
LINK ND2 ASN B 57 C1 NAG B 602 1555 1555 1.46
LINK ND2 ASN B 241 C1 NAG B 603 1555 1555 1.45
LINK ND2 ASN B 256 C1 NAG B 605 1555 1555 1.44
LINK ND2 ASN B 341 C1 NAG B 606 1555 1555 1.45
LINK ND2 ASN B 455 C1 NAG B 607 1555 1555 1.44
LINK ND2 ASN B 481 C1 NAG B 609 1555 1555 1.48
LINK O4 NAG A 602 C1 NAG A 603 1555 1555 1.45
LINK O4 NAG A 606 C1 NAG A 607 1555 1555 1.44
LINK O4 NAG B 603 C1 NAG B 604 1555 1555 1.46
LINK O4 NAG B 607 C1 NAG B 608 1555 1555 1.45
CISPEP 1 ALA A 101 PRO A 102 0 3.03
CISPEP 2 ALA B 101 PRO B 102 0 0.62
SITE 1 AC1 15 TRP A 82 GLY A 116 GLY A 117 THR A 120
SITE 2 AC1 15 TYR A 128 GLU A 197 SER A 198 TRP A 231
SITE 3 AC1 15 PRO A 285 LEU A 286 SER A 287 TYR A 332
SITE 4 AC1 15 PHE A 398 HIS A 438 HOH A 738
SITE 1 AC2 1 GLU B 461
SITE 1 AC3 1 ASP B 295
SITE 1 AC4 1 ASP B 129
SITE 1 AC5 14 ASP B 70 TRP B 82 GLY B 116 GLU B 197
SITE 2 AC5 14 SER B 198 TRP B 231 PRO B 285 LEU B 286
SITE 3 AC5 14 SER B 287 PHE B 329 TYR B 332 PHE B 398
SITE 4 AC5 14 HIS B 438 ILE B 442
SITE 1 AC6 3 ILE A 4 ASN A 17 THR A 24
SITE 1 AC7 4 LYS A 105 ASN A 106 ASN A 188 LYS A 190
SITE 1 AC8 3 ASN A 241 NAG B 607 NAG B 608
SITE 1 AC9 1 ASN A 341
SITE 1 AD1 8 ASN A 473 TYR A 477 ASN A 481 GLU A 482
SITE 2 AD1 8 HOH A 726 HOH A 739 LEU B 88 GLN B 270
SITE 1 AD2 3 ILE B 4 ASN B 17 THR B 24
SITE 1 AD3 3 ARG B 14 ASN B 57 THR B 59
SITE 1 AD4 3 ASN B 241 LEU B 244 TYR B 282
SITE 1 AD5 2 ASN B 256 GLU B 411
SITE 1 AD6 4 GLY B 336 SER B 338 ASN B 341 HOH B 706
SITE 1 AD7 9 TYR A 237 ARG A 240 ASN A 241 NAG A 604
SITE 2 AD7 9 LYS B 427 ARG B 453 ASP B 454 ASN B 455
SITE 3 AD7 9 HOH B 728
SITE 1 AD8 3 TYR B 477 ASN B 481 GLU B 482
CRYST1 75.040 79.220 228.350 90.00 90.00 90.00 P 21 21 21 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 0.013326 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012623 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004379 0.00000
TER 4187 VAL A 529
TER 8376 VAL B 529
MASTER 418 0 23 44 28 0 26 6 8803 2 310 82
END |