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HEADER HYDROLASE/HYDROLASE INHIBITOR 29-JAN-19 6NTN
TITLE CRYSTAL STRUCTURE OF RECOMBINANT HUMAN ACETYLCHOLINESTERASE INHIBITED
TITLE 2 BY A-230 IN COMPLEX WITH THE REACTIVATOR, HI-6
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ACHE;
COMPND 5 EC: 3.1.1.7;
COMPND 6 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: ACHE;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606
KEYWDS HYDROLASE, INHIBITOR, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR S.M.BESTER,M.A.GUELTA,J.J.HEIGHT,S.D.PEGAN
REVDAT 1 01-JUL-20 6NTN 0
JRNL AUTH J.J.HEIGHT,S.M.BESTER,M.A.GUELTA,S.Y.BAE,J.CHEUNG,S.D.PEGAN
JRNL TITL INSIGHTS INTO INHIBITION OF HUMAN ACETYLCHOLINESTERASE BY
JRNL TITL 2 NOVICHOK, A-SERIES NERVE AGENTS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (DEV_3311: ???)
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) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.33
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 57079
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.173
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.215
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.710
REMARK 3 FREE R VALUE TEST SET COUNT : 2687
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 46.3342 - 7.1880 0.98 3073 162 0.2022 0.2532
REMARK 3 2 7.1880 - 5.7087 0.99 2941 139 0.1926 0.2125
REMARK 3 3 5.7087 - 4.9880 1.00 2906 150 0.1581 0.1862
REMARK 3 4 4.9880 - 4.5324 1.00 2877 150 0.1280 0.1765
REMARK 3 5 4.5324 - 4.2078 0.99 2904 131 0.1278 0.1754
REMARK 3 6 4.2078 - 3.9598 0.99 2854 160 0.1372 0.1814
REMARK 3 7 3.9598 - 3.7616 0.99 2876 117 0.1407 0.1738
REMARK 3 8 3.7616 - 3.5979 1.00 2839 145 0.1488 0.1653
REMARK 3 9 3.5979 - 3.4595 1.00 2917 107 0.1540 0.2181
REMARK 3 10 3.4595 - 3.3401 1.00 2871 128 0.1730 0.2283
REMARK 3 11 3.3401 - 3.2357 0.99 2773 186 0.1798 0.2434
REMARK 3 12 3.2357 - 3.1432 1.00 2829 142 0.1908 0.2426
REMARK 3 13 3.1432 - 3.0605 0.99 2828 130 0.1902 0.2214
REMARK 3 14 3.0605 - 2.9859 0.99 2834 134 0.1887 0.2380
REMARK 3 15 2.9859 - 2.9180 0.99 2804 152 0.2009 0.2337
REMARK 3 16 2.9180 - 2.8559 0.99 2857 140 0.2149 0.2800
REMARK 3 17 2.8559 - 2.7988 1.00 2834 132 0.2272 0.3185
REMARK 3 18 2.7988 - 2.7460 1.00 2768 151 0.2394 0.2764
REMARK 3 19 2.7460 - 2.6969 0.98 2807 131 0.2528 0.3286
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) : 0.300
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.830
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) : 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 8711
REMARK 3 ANGLE : 0.703 11915
REMARK 3 CHIRALITY : 0.046 1290
REMARK 3 PLANARITY : 0.005 1558
REMARK 3 DIHEDRAL : 4.599 5048
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 5
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ( CHAIN A AND RESID 4:333 )
REMARK 3 ORIGIN FOR THE GROUP (A): -53.7669 30.6040 -19.8656
REMARK 3 T TENSOR
REMARK 3 T11: 0.5754 T22: 0.4256
REMARK 3 T33: 0.2625 T12: 0.0385
REMARK 3 T13: 0.0109 T23: -0.0234
REMARK 3 L TENSOR
REMARK 3 L11: 2.1796 L22: 2.1341
REMARK 3 L33: 3.1606 L12: -0.5612
REMARK 3 L13: -0.3195 L23: 0.6974
REMARK 3 S TENSOR
REMARK 3 S11: -0.0512 S12: -0.1599 S13: -0.0589
REMARK 3 S21: 0.2572 S22: 0.0303 S23: -0.0339
REMARK 3 S31: 0.2717 S32: -0.1076 S33: 0.0172
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: ( CHAIN A AND RESID 334:542 )
REMARK 3 ORIGIN FOR THE GROUP (A): -53.2732 36.1061 -43.0759
REMARK 3 T TENSOR
REMARK 3 T11: 0.6116 T22: 0.6295
REMARK 3 T33: 0.3253 T12: 0.0666
REMARK 3 T13: -0.0039 T23: 0.0064
REMARK 3 L TENSOR
REMARK 3 L11: 1.9010 L22: 1.3766
REMARK 3 L33: 2.8065 L12: -0.1940
REMARK 3 L13: -1.5600 L23: 0.6896
REMARK 3 S TENSOR
REMARK 3 S11: 0.0318 S12: 0.2196 S13: 0.1351
REMARK 3 S21: -0.1987 S22: 0.0179 S23: 0.0025
REMARK 3 S31: -0.1967 S32: -0.3269 S33: -0.0457
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: ( CHAIN B AND RESID 4:36 )
REMARK 3 ORIGIN FOR THE GROUP (A): -29.1489 -19.0887 2.8711
REMARK 3 T TENSOR
REMARK 3 T11: 0.4999 T22: 0.6976
REMARK 3 T33: 0.3325 T12: 0.0820
REMARK 3 T13: -0.0162 T23: -0.0273
REMARK 3 L TENSOR
REMARK 3 L11: 7.2402 L22: 8.5901
REMARK 3 L33: 3.5191 L12: 6.2997
REMARK 3 L13: 0.9629 L23: -1.3563
REMARK 3 S TENSOR
REMARK 3 S11: 0.6231 S12: -1.2473 S13: -0.1121
REMARK 3 S21: 1.0227 S22: -0.5701 S23: -0.0810
REMARK 3 S31: 0.2337 S32: 0.0432 S33: 0.0195
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: ( CHAIN B AND RESID 37:327 )
REMARK 3 ORIGIN FOR THE GROUP (A): -29.5412 -11.1006 -19.5212
REMARK 3 T TENSOR
REMARK 3 T11: 0.3643 T22: 0.4986
REMARK 3 T33: 0.2854 T12: 0.0956
REMARK 3 T13: -0.0159 T23: -0.0412
REMARK 3 L TENSOR
REMARK 3 L11: 1.2464 L22: 3.4233
REMARK 3 L33: 2.7156 L12: 0.2699
REMARK 3 L13: 0.1585 L23: -0.1648
REMARK 3 S TENSOR
REMARK 3 S11: 0.0056 S12: -0.1331 S13: 0.1628
REMARK 3 S21: -0.1739 S22: -0.0360 S23: -0.0390
REMARK 3 S31: -0.2854 S32: -0.0138 S33: 0.0151
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: ( CHAIN B AND RESID 328:542 )
REMARK 3 ORIGIN FOR THE GROUP (A): -44.7846 -24.6719 -31.0303
REMARK 3 T TENSOR
REMARK 3 T11: 0.5008 T22: 0.5226
REMARK 3 T33: 0.3340 T12: -0.0045
REMARK 3 T13: -0.0334 T23: -0.0611
REMARK 3 L TENSOR
REMARK 3 L11: 1.6384 L22: 1.2451
REMARK 3 L33: 5.2052 L12: -0.4632
REMARK 3 L13: 1.2134 L23: -1.0410
REMARK 3 S TENSOR
REMARK 3 S11: -0.0536 S12: -0.1083 S13: -0.0588
REMARK 3 S21: -0.0787 S22: 0.0458 S23: 0.1799
REMARK 3 S31: 0.0574 S32: -0.6751 S33: 0.0071
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 6NTN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-FEB-19.
REMARK 100 THE DEPOSITION ID IS D_1000239407.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-MAR-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
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 : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 57260
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.697
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 5.500
REMARK 200 R MERGE (I) : 0.13000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.75
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 5.70
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.200
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: 4EY4
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 71.28
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.28
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15-21% POLYETHYLENE GLYCOL 3350 (PEG)
REMARK 280 AND 0.17- 0.21M POTASSIUM NITRATE, PH 7.0, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 107.89433
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 215.78867
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 215.78867
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 107.89433
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: 5750 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 37820 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 29.0 KCAL/MOL
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 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -107.89433
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 2
REMARK 465 ARG A 3
REMARK 465 GLY A 260
REMARK 465 GLY A 261
REMARK 465 ARG A 493
REMARK 465 ASP A 494
REMARK 465 PRO A 495
REMARK 465 LYS A 496
REMARK 465 THR A 543
REMARK 465 GLY B 2
REMARK 465 ARG B 3
REMARK 465 PRO B 259
REMARK 465 GLY B 260
REMARK 465 GLY B 261
REMARK 465 THR B 262
REMARK 465 GLY B 263
REMARK 465 GLY B 264
REMARK 465 ARG B 493
REMARK 465 ASP B 494
REMARK 465 PRO B 495
REMARK 465 LYS B 496
REMARK 465 ALA B 497
REMARK 465 THR B 543
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 ALA A 62 71.75 -101.24
REMARK 500 CYS A 96 9.04 -150.06
REMARK 500 ALA A 167 64.82 -155.95
REMARK 500 SER A 203 -122.76 61.51
REMARK 500 ASP A 306 -87.20 -96.99
REMARK 500 VAL A 407 -65.13 -126.16
REMARK 500 PHE B 47 -3.06 74.03
REMARK 500 ALA B 62 51.31 -118.41
REMARK 500 ASP B 95 91.88 -69.41
REMARK 500 PHE B 158 10.69 -141.31
REMARK 500 ALA B 167 72.72 -153.93
REMARK 500 SER B 203 -129.02 58.03
REMARK 500 ASP B 306 -83.44 -102.18
REMARK 500 VAL B 407 -62.98 -133.70
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 HI6 A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue L2Y A 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HI6 B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues FUC A
REMARK 800 605 through NAG A 607 bound to ASN A 265
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues FUC A
REMARK 800 602 through NAG A 604 bound to ASN A 350
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues FUC B
REMARK 800 602 through NAG B 604 bound to ASN B 350
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 605 bound
REMARK 800 to ASN B 464
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide L2Y B 606 and SER B
REMARK 800 203
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6NTG RELATED DB: PDB
REMARK 900 RELATED ID: 6NTH RELATED DB: PDB
REMARK 900 RELATED ID: 6NTK RELATED DB: PDB
REMARK 900 RELATED ID: 6NTL RELATED DB: PDB
REMARK 900 RELATED ID: 6NTM RELATED DB: PDB
DBREF 6NTN A 2 543 UNP P22303 ACES_HUMAN 33 574
DBREF 6NTN B 2 543 UNP P22303 ACES_HUMAN 33 574
SEQRES 1 A 542 GLY ARG GLU ASP ALA GLU LEU LEU VAL THR VAL ARG GLY
SEQRES 2 A 542 GLY ARG LEU ARG GLY ILE ARG LEU LYS THR PRO GLY GLY
SEQRES 3 A 542 PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO
SEQRES 4 A 542 PRO MET GLY PRO ARG ARG PHE LEU PRO PRO GLU PRO LYS
SEQRES 5 A 542 GLN PRO TRP SER GLY VAL VAL ASP ALA THR THR PHE GLN
SEQRES 6 A 542 SER VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO GLY
SEQRES 7 A 542 PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU LEU
SEQRES 8 A 542 SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO TYR
SEQRES 9 A 542 PRO ARG PRO THR SER PRO THR PRO VAL LEU VAL TRP ILE
SEQRES 10 A 542 TYR GLY GLY GLY PHE TYR SER GLY ALA SER SER LEU ASP
SEQRES 11 A 542 VAL TYR ASP GLY ARG PHE LEU VAL GLN ALA GLU ARG THR
SEQRES 12 A 542 VAL LEU VAL SER MET ASN TYR ARG VAL GLY ALA PHE GLY
SEQRES 13 A 542 PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY ASN
SEQRES 14 A 542 VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP VAL
SEQRES 15 A 542 GLN GLU ASN VAL ALA ALA PHE GLY GLY ASP PRO THR SER
SEQRES 16 A 542 VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER VAL
SEQRES 17 A 542 GLY MET HIS LEU LEU SER PRO PRO SER ARG GLY LEU PHE
SEQRES 18 A 542 HIS ARG ALA VAL LEU GLN SER GLY ALA PRO ASN GLY PRO
SEQRES 19 A 542 TRP ALA THR VAL GLY MET GLY GLU ALA ARG ARG ARG ALA
SEQRES 20 A 542 THR GLN LEU ALA HIS LEU VAL GLY CYS PRO PRO GLY GLY
SEQRES 21 A 542 THR GLY GLY ASN ASP THR GLU LEU VAL ALA CYS LEU ARG
SEQRES 22 A 542 THR ARG PRO ALA GLN VAL LEU VAL ASN HIS GLU TRP HIS
SEQRES 23 A 542 VAL LEU PRO GLN GLU SER VAL PHE ARG PHE SER PHE VAL
SEQRES 24 A 542 PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO GLU
SEQRES 25 A 542 ALA LEU ILE ASN ALA GLY ASP PHE HIS GLY LEU GLN VAL
SEQRES 26 A 542 LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE LEU
SEQRES 27 A 542 VAL TYR GLY ALA PRO GLY PHE SER LYS ASP ASN GLU SER
SEQRES 28 A 542 LEU ILE SER ARG ALA GLU PHE LEU ALA GLY VAL ARG VAL
SEQRES 29 A 542 GLY VAL PRO GLN VAL SER ASP LEU ALA ALA GLU ALA VAL
SEQRES 30 A 542 VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP PRO
SEQRES 31 A 542 ALA ARG LEU ARG GLU ALA LEU SER ASP VAL VAL GLY ASP
SEQRES 32 A 542 HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY ARG
SEQRES 33 A 542 LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR VAL PHE
SEQRES 34 A 542 GLU HIS ARG ALA SER THR LEU SER TRP PRO LEU TRP MET
SEQRES 35 A 542 GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE GLY
SEQRES 36 A 542 ILE PRO LEU ASP PRO SER ARG ASN TYR THR ALA GLU GLU
SEQRES 37 A 542 LYS ILE PHE ALA GLN ARG LEU MET ARG TYR TRP ALA ASN
SEQRES 38 A 542 PHE ALA ARG THR GLY ASP PRO ASN GLU PRO ARG ASP PRO
SEQRES 39 A 542 LYS ALA PRO GLN TRP PRO PRO TYR THR ALA GLY ALA GLN
SEQRES 40 A 542 GLN TYR VAL SER LEU ASP LEU ARG PRO LEU GLU VAL ARG
SEQRES 41 A 542 ARG GLY LEU ARG ALA GLN ALA CYS ALA PHE TRP ASN ARG
SEQRES 42 A 542 PHE LEU PRO LYS LEU LEU SER ALA THR
SEQRES 1 B 542 GLY ARG GLU ASP ALA GLU LEU LEU VAL THR VAL ARG GLY
SEQRES 2 B 542 GLY ARG LEU ARG GLY ILE ARG LEU LYS THR PRO GLY GLY
SEQRES 3 B 542 PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO
SEQRES 4 B 542 PRO MET GLY PRO ARG ARG PHE LEU PRO PRO GLU PRO LYS
SEQRES 5 B 542 GLN PRO TRP SER GLY VAL VAL ASP ALA THR THR PHE GLN
SEQRES 6 B 542 SER VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO GLY
SEQRES 7 B 542 PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU LEU
SEQRES 8 B 542 SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO TYR
SEQRES 9 B 542 PRO ARG PRO THR SER PRO THR PRO VAL LEU VAL TRP ILE
SEQRES 10 B 542 TYR GLY GLY GLY PHE TYR SER GLY ALA SER SER LEU ASP
SEQRES 11 B 542 VAL TYR ASP GLY ARG PHE LEU VAL GLN ALA GLU ARG THR
SEQRES 12 B 542 VAL LEU VAL SER MET ASN TYR ARG VAL GLY ALA PHE GLY
SEQRES 13 B 542 PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY ASN
SEQRES 14 B 542 VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP VAL
SEQRES 15 B 542 GLN GLU ASN VAL ALA ALA PHE GLY GLY ASP PRO THR SER
SEQRES 16 B 542 VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER VAL
SEQRES 17 B 542 GLY MET HIS LEU LEU SER PRO PRO SER ARG GLY LEU PHE
SEQRES 18 B 542 HIS ARG ALA VAL LEU GLN SER GLY ALA PRO ASN GLY PRO
SEQRES 19 B 542 TRP ALA THR VAL GLY MET GLY GLU ALA ARG ARG ARG ALA
SEQRES 20 B 542 THR GLN LEU ALA HIS LEU VAL GLY CYS PRO PRO GLY GLY
SEQRES 21 B 542 THR GLY GLY ASN ASP THR GLU LEU VAL ALA CYS LEU ARG
SEQRES 22 B 542 THR ARG PRO ALA GLN VAL LEU VAL ASN HIS GLU TRP HIS
SEQRES 23 B 542 VAL LEU PRO GLN GLU SER VAL PHE ARG PHE SER PHE VAL
SEQRES 24 B 542 PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO GLU
SEQRES 25 B 542 ALA LEU ILE ASN ALA GLY ASP PHE HIS GLY LEU GLN VAL
SEQRES 26 B 542 LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE LEU
SEQRES 27 B 542 VAL TYR GLY ALA PRO GLY PHE SER LYS ASP ASN GLU SER
SEQRES 28 B 542 LEU ILE SER ARG ALA GLU PHE LEU ALA GLY VAL ARG VAL
SEQRES 29 B 542 GLY VAL PRO GLN VAL SER ASP LEU ALA ALA GLU ALA VAL
SEQRES 30 B 542 VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP PRO
SEQRES 31 B 542 ALA ARG LEU ARG GLU ALA LEU SER ASP VAL VAL GLY ASP
SEQRES 32 B 542 HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY ARG
SEQRES 33 B 542 LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR VAL PHE
SEQRES 34 B 542 GLU HIS ARG ALA SER THR LEU SER TRP PRO LEU TRP MET
SEQRES 35 B 542 GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE GLY
SEQRES 36 B 542 ILE PRO LEU ASP PRO SER ARG ASN TYR THR ALA GLU GLU
SEQRES 37 B 542 LYS ILE PHE ALA GLN ARG LEU MET ARG TYR TRP ALA ASN
SEQRES 38 B 542 PHE ALA ARG THR GLY ASP PRO ASN GLU PRO ARG ASP PRO
SEQRES 39 B 542 LYS ALA PRO GLN TRP PRO PRO TYR THR ALA GLY ALA GLN
SEQRES 40 B 542 GLN TYR VAL SER LEU ASP LEU ARG PRO LEU GLU VAL ARG
SEQRES 41 B 542 ARG GLY LEU ARG ALA GLN ALA CYS ALA PHE TRP ASN ARG
SEQRES 42 B 542 PHE LEU PRO LYS LEU LEU SER ALA THR
HET HI6 A 601 21
HET FUC A 602 10
HET NAG A 603 14
HET NAG A 604 14
HET FUC A 605 10
HET NAG A 606 14
HET NAG A 607 14
HET L2Y A 608 11
HET HI6 B 601 21
HET FUC B 602 10
HET NAG B 603 14
HET NAG B 604 14
HET NAG B 605 14
HET L2Y B 606 11
HETNAM HI6 4-(AMINOCARBONYL)-1-[({2-[(E)-(HYDROXYIMINO)
HETNAM 2 HI6 METHYL]PYRIDINIUM-1-YL}METHOXY)METHYL]PYRIDINIUM
HETNAM FUC ALPHA-L-FUCOSE
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM L2Y (S)-N-[(1E)-1-(DIETHYLAMINO)ETHYLIDENE]-P-
HETNAM 2 L2Y METHYLPHOSPHONAMIDIC FLUORIDE
HETSYN HI6 1-(2-HYDROXY-IMINOMETHYLPYRIDINIUM)-1-(4-CARBOXYAMINO)-
HETSYN 2 HI6 PYRIDINIUM DIMETHYLETHER
HETSYN L2Y A-230 (NERVE AGENT)
FORMUL 3 HI6 2(C14 H16 N4 O3 2+)
FORMUL 4 FUC 3(C6 H12 O5)
FORMUL 4 NAG 7(C8 H15 N O6)
FORMUL 6 L2Y 2(C7 H16 F N2 O P)
FORMUL 11 HOH *458(H2 O)
HELIX 1 AA1 ASP A 5 GLU A 7 5 3
HELIX 2 AA2 MET A 42 ARG A 46 5 5
HELIX 3 AA3 PHE A 80 MET A 85 1 6
HELIX 4 AA4 LEU A 130 ASP A 134 5 5
HELIX 5 AA5 GLY A 135 ARG A 143 1 9
HELIX 6 AA6 GLY A 154 LEU A 159 1 6
HELIX 7 AA7 ASN A 170 VAL A 187 1 18
HELIX 8 AA8 ALA A 188 PHE A 190 5 3
HELIX 9 AA9 SER A 203 SER A 215 1 13
HELIX 10 AB1 SER A 215 GLY A 220 1 6
HELIX 11 AB2 GLY A 240 VAL A 255 1 16
HELIX 12 AB3 ASN A 265 THR A 275 1 11
HELIX 13 AB4 PRO A 277 ASN A 283 1 7
HELIX 14 AB5 HIS A 284 LEU A 289 5 6
HELIX 15 AB6 THR A 311 GLY A 319 1 9
HELIX 16 AB7 GLY A 335 VAL A 340 1 6
HELIX 17 AB8 SER A 355 VAL A 367 1 13
HELIX 18 AB9 SER A 371 THR A 383 1 13
HELIX 19 AC1 ASP A 390 VAL A 407 1 18
HELIX 20 AC2 VAL A 407 GLN A 421 1 15
HELIX 21 AC3 PRO A 440 GLY A 444 5 5
HELIX 22 AC4 GLU A 450 PHE A 455 1 6
HELIX 23 AC5 GLY A 456 ASP A 460 5 5
HELIX 24 AC6 THR A 466 GLY A 487 1 22
HELIX 25 AC7 ARG A 525 ARG A 534 1 10
HELIX 26 AC8 PHE A 535 SER A 541 1 7
HELIX 27 AC9 ASP B 5 GLU B 7 5 3
HELIX 28 AD1 MET B 42 ARG B 46 5 5
HELIX 29 AD2 PHE B 80 MET B 85 1 6
HELIX 30 AD3 LEU B 130 ASP B 134 5 5
HELIX 31 AD4 GLY B 135 ARG B 143 1 9
HELIX 32 AD5 VAL B 153 LEU B 159 1 7
HELIX 33 AD6 ASN B 170 VAL B 187 1 18
HELIX 34 AD7 ALA B 188 PHE B 190 5 3
HELIX 35 AD8 SER B 203 LEU B 214 1 12
HELIX 36 AD9 SER B 215 GLY B 220 1 6
HELIX 37 AE1 MET B 241 VAL B 255 1 15
HELIX 38 AE2 ASP B 266 THR B 275 1 10
HELIX 39 AE3 PRO B 277 TRP B 286 1 10
HELIX 40 AE4 HIS B 287 LEU B 289 5 3
HELIX 41 AE5 THR B 311 ALA B 318 1 8
HELIX 42 AE6 GLY B 335 GLY B 342 5 8
HELIX 43 AE7 SER B 355 VAL B 367 1 13
HELIX 44 AE8 SER B 371 THR B 383 1 13
HELIX 45 AE9 ASP B 390 VAL B 407 1 18
HELIX 46 AF1 VAL B 407 GLN B 421 1 15
HELIX 47 AF2 PRO B 440 GLY B 444 5 5
HELIX 48 AF3 GLU B 450 PHE B 455 1 6
HELIX 49 AF4 GLY B 456 ASP B 460 5 5
HELIX 50 AF5 THR B 466 GLY B 487 1 22
HELIX 51 AF6 ARG B 525 ARG B 534 1 10
HELIX 52 AF7 ARG B 534 SER B 541 1 8
SHEET 1 AA1 3 LEU A 9 VAL A 12 0
SHEET 2 AA1 3 GLY A 15 ARG A 18 -1 O LEU A 17 N VAL A 10
SHEET 3 AA1 3 VAL A 59 ASP A 61 1 O VAL A 60 N ARG A 16
SHEET 1 AA211 ILE A 20 LEU A 22 0
SHEET 2 AA211 VAL A 29 PRO A 36 -1 O VAL A 29 N LEU A 22
SHEET 3 AA211 TYR A 98 PRO A 104 -1 O LEU A 99 N ILE A 35
SHEET 4 AA211 VAL A 145 MET A 149 -1 O SER A 148 N ASN A 100
SHEET 5 AA211 THR A 112 ILE A 118 1 N LEU A 115 O VAL A 147
SHEET 6 AA211 GLY A 192 GLU A 202 1 O THR A 198 N VAL A 114
SHEET 7 AA211 ARG A 224 GLN A 228 1 O ARG A 224 N LEU A 199
SHEET 8 AA211 GLN A 325 VAL A 331 1 O LEU A 327 N LEU A 227
SHEET 9 AA211 ARG A 424 PHE A 430 1 O TYR A 426 N VAL A 328
SHEET 10 AA211 GLN A 509 LEU A 513 1 O LEU A 513 N VAL A 429
SHEET 11 AA211 GLU A 519 ARG A 522 -1 O ARG A 521 N TYR A 510
SHEET 1 AA3 2 VAL A 68 CYS A 69 0
SHEET 2 AA3 2 LEU A 92 SER A 93 1 O SER A 93 N VAL A 68
SHEET 1 AA4 3 LEU B 9 VAL B 12 0
SHEET 2 AA4 3 GLY B 15 ARG B 18 -1 O LEU B 17 N VAL B 10
SHEET 3 AA4 3 VAL B 59 ASP B 61 1 O VAL B 60 N ARG B 16
SHEET 1 AA511 ILE B 20 LEU B 22 0
SHEET 2 AA511 VAL B 29 PRO B 36 -1 O VAL B 29 N LEU B 22
SHEET 3 AA511 TYR B 98 PRO B 104 -1 O THR B 103 N SER B 30
SHEET 4 AA511 VAL B 145 MET B 149 -1 O SER B 148 N ASN B 100
SHEET 5 AA511 THR B 112 ILE B 118 1 N TRP B 117 O VAL B 147
SHEET 6 AA511 GLY B 192 GLU B 202 1 O ASP B 193 N THR B 112
SHEET 7 AA511 ARG B 224 GLN B 228 1 O ARG B 224 N LEU B 199
SHEET 8 AA511 GLN B 325 VAL B 331 1 O LEU B 327 N LEU B 227
SHEET 9 AA511 ARG B 424 PHE B 430 1 O TYR B 426 N VAL B 328
SHEET 10 AA511 GLN B 509 LEU B 513 1 O LEU B 513 N VAL B 429
SHEET 11 AA511 GLU B 519 ARG B 522 -1 O ARG B 521 N TYR B 510
SHEET 1 AA6 2 VAL B 68 CYS B 69 0
SHEET 2 AA6 2 LEU B 92 SER B 93 1 O SER B 93 N VAL B 68
SHEET 1 AA7 2 VAL B 239 GLY B 240 0
SHEET 2 AA7 2 VAL B 302 VAL B 303 1 O VAL B 303 N VAL B 239
SSBOND 1 CYS A 69 CYS A 96 1555 1555 2.04
SSBOND 2 CYS A 257 CYS A 272 1555 1555 2.04
SSBOND 3 CYS A 409 CYS A 529 1555 1555 2.06
SSBOND 4 CYS B 69 CYS B 96 1555 1555 2.05
SSBOND 5 CYS B 257 CYS B 272 1555 1555 2.03
SSBOND 6 CYS B 409 CYS B 529 1555 1555 2.06
LINK OG SER A 203 P09 L2Y A 608 1555 1555 1.56
LINK ND2 ASN A 265 C1 NAG A 606 1555 1555 1.51
LINK ND2 ASN A 350 C1 NAG A 603 1555 1555 1.47
LINK OG SER B 203 P09 L2Y B 606 1555 1555 1.56
LINK ND2 ASN B 350 C1 NAG B 603 1555 1555 1.40
LINK ND2 ASN B 464 C1 NAG B 605 1555 1555 1.38
LINK C1 FUC A 602 O6 NAG A 603 1555 1555 1.44
LINK O4 NAG A 603 C1 NAG A 604 1555 1555 1.44
LINK C1 FUC A 605 O6 NAG A 606 1555 1555 1.44
LINK O4 NAG A 606 C1 NAG A 607 1555 1555 1.44
LINK C1 FUC B 602 O6 NAG B 603 1555 1555 1.44
LINK O4 NAG B 603 C1 NAG B 604 1555 1555 1.44
CISPEP 1 TYR A 105 PRO A 106 0 4.06
CISPEP 2 CYS A 257 PRO A 258 0 -2.49
CISPEP 3 TYR B 105 PRO B 106 0 -2.64
CISPEP 4 CYS B 257 PRO B 258 0 6.28
SITE 1 AC1 9 TYR A 72 ASP A 74 TYR A 124 VAL A 282
SITE 2 AC1 9 GLU A 285 TRP A 286 TYR A 337 TYR A 341
SITE 3 AC1 9 HOH A 706
SITE 1 AC2 10 TRP A 86 GLY A 121 GLY A 122 GLU A 202
SITE 2 AC2 10 SER A 203 ALA A 204 PHE A 295 PHE A 297
SITE 3 AC2 10 TYR A 337 HIS A 447
SITE 1 AC3 9 TYR B 72 TYR B 124 GLU B 285 TRP B 286
SITE 2 AC3 9 PHE B 297 SER B 298 TYR B 337 TYR B 341
SITE 3 AC3 9 L2Y B 606
SITE 1 AC4 4 ASN A 265 THR A 267 GLU A 268 HOH A 779
SITE 1 AC5 4 PRO A 344 GLY A 345 SER A 347 ASN A 350
SITE 1 AC6 2 GLY B 345 ASN B 350
SITE 1 AC7 2 SER B 462 ASN B 464
SITE 1 AC8 15 GLY B 121 GLY B 122 TYR B 133 GLU B 202
SITE 2 AC8 15 ALA B 204 GLY B 205 ALA B 206 ALA B 207
SITE 3 AC8 15 GLN B 228 SER B 229 PHE B 295 PHE B 297
SITE 4 AC8 15 TYR B 337 HIS B 447 HI6 B 601
CRYST1 104.402 104.402 323.683 90.00 90.00 120.00 P 31 2 1 12
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 0.009578 0.005530 0.000000 0.00000
SCALE2 0.000000 0.011060 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003089 0.00000
TER 4139 ALA A 542
TER 8251 ALA B 542
MASTER 404 0 14 52 34 0 17 6 8899 2 210 84
END |