HEADER HYDROLASE 10-OCT-17 6EP4
TITLE HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX WITH DECAMETHONIUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHOLINESTERASE;
COMPND 3 CHAIN: A;
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: CRICETULUS GRISEUS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: CHO-K1;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGS
KEYWDS COMPLEX, HYDROLASE, INHIBITOR, QUATERNARY AMMONIUM
EXPDTA X-RAY DIFFRACTION
AUTHOR F.NACHON,X.BRAZZOLOTTO,M.WANDHAMMER,M.TROVASLET-LEROY,T.L.ROSENBERRY,
AUTHOR 2 I.R.MACDONALD,S.DARVESH
REVDAT 3 17-JAN-24 6EP4 1 HETSYN LINK
REVDAT 2 29-JUL-20 6EP4 1 COMPND REMARK HETNAM LINK
REVDAT 2 2 1 SITE ATOM
REVDAT 1 13-DEC-17 6EP4 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. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.11.1_2575
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 : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.39
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.356
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 35643
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.181
REMARK 3 R VALUE (WORKING SET) : 0.179
REMARK 3 FREE R VALUE : 0.217
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.608
REMARK 3 FREE R VALUE TEST SET COUNT : 1999
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 42.4002 - 5.5396 0.99 2563 152 0.1840 0.2088
REMARK 3 2 5.5396 - 4.3984 1.00 2471 147 0.1420 0.1670
REMARK 3 3 4.3984 - 3.8429 1.00 2436 145 0.1417 0.1819
REMARK 3 4 3.8429 - 3.4917 1.00 2432 144 0.1618 0.1974
REMARK 3 5 3.4917 - 3.2415 1.00 2411 143 0.1834 0.2527
REMARK 3 6 3.2415 - 3.0505 1.00 2397 143 0.1908 0.2068
REMARK 3 7 3.0505 - 2.8977 1.00 2404 142 0.2050 0.2432
REMARK 3 8 2.8977 - 2.7716 1.00 2386 143 0.2082 0.2560
REMARK 3 9 2.7716 - 2.6649 1.00 2371 140 0.2111 0.2571
REMARK 3 10 2.6649 - 2.5730 1.00 2395 143 0.2116 0.2936
REMARK 3 11 2.5730 - 2.4925 1.00 2383 142 0.2137 0.2526
REMARK 3 12 2.4925 - 2.4213 1.00 2375 141 0.2171 0.2950
REMARK 3 13 2.4213 - 2.3576 0.99 2371 140 0.2245 0.2493
REMARK 3 14 2.3576 - 2.3001 0.95 2249 134 0.2505 0.3043
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) : 0.268
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.010
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 41.24
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 49.96
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 : 0.003 4502
REMARK 3 ANGLE : 0.626 6139
REMARK 3 CHIRALITY : 0.048 676
REMARK 3 PLANARITY : 0.004 778
REMARK 3 DIHEDRAL : 9.477 3600
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A
REMARK 3 ORIGIN FOR THE GROUP (A): -16.1381 -32.6232 -26.7350
REMARK 3 T TENSOR
REMARK 3 T11: 0.3116 T22: 0.2902
REMARK 3 T33: 0.3302 T12: -0.0320
REMARK 3 T13: -0.0581 T23: -0.0590
REMARK 3 L TENSOR
REMARK 3 L11: 1.2761 L22: 1.3032
REMARK 3 L33: 1.8797 L12: 0.2249
REMARK 3 L13: 0.3104 L23: -0.0664
REMARK 3 S TENSOR
REMARK 3 S11: 0.0196 S12: 0.1078 S13: -0.0780
REMARK 3 S21: -0.1463 S22: 0.0679 S23: -0.0065
REMARK 3 S31: 0.1285 S32: -0.0410 S33: -0.0793
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 6EP4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-OCT-17.
REMARK 100 THE DEPOSITION ID IS D_1200007000.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-JUN-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
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) : 0.934
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 : 35717
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 42.400
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 9.100
REMARK 200 R MERGE (I) : 0.05305
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 29.6300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.9
REMARK 200 DATA REDUNDANCY IN SHELL : 5.50
REMARK 200 R MERGE FOR SHELL (I) : 0.37820
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.820
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1P0I
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.39
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.36
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 MES BUFFER, 2.1 M AMMONIUM
REMARK 280 SULFATE, PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 2 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 -Y,X,Z
REMARK 290 4555 Y,-X,Z
REMARK 290 5555 -X,Y,-Z
REMARK 290 6555 X,-Y,-Z
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z
REMARK 290 9555 X+1/2,Y+1/2,Z+1/2
REMARK 290 10555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 11555 -Y+1/2,X+1/2,Z+1/2
REMARK 290 12555 Y+1/2,-X+1/2,Z+1/2
REMARK 290 13555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 14555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 15555 Y+1/2,X+1/2,-Z+1/2
REMARK 290 16555 -Y+1/2,-X+1/2,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 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 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 77.43000
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 77.43000
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 66.11500
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 77.43000
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 77.43000
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 66.11500
REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 77.43000
REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 77.43000
REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 66.11500
REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 77.43000
REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 77.43000
REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 66.11500
REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 77.43000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 77.43000
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 66.11500
REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 77.43000
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 77.43000
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 66.11500
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 77.43000
REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 77.43000
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 66.11500
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 77.43000
REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 77.43000
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 66.11500
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3870 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21050 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 2.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 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 VAL A 377
REMARK 465 ASP A 378
REMARK 465 ASP A 379
REMARK 465 GLN A 380
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 43 -4.79 71.49
REMARK 500 ASP A 54 -154.25 -100.90
REMARK 500 ASN A 106 56.02 -158.20
REMARK 500 PHE A 153 11.67 -141.94
REMARK 500 ALA A 162 73.51 -152.13
REMARK 500 SER A 198 -124.94 60.03
REMARK 500 ASP A 297 -78.46 -128.01
REMARK 500 ASP A 375 77.57 -104.21
REMARK 500 PHE A 398 -59.52 -137.64
REMARK 500 ASN A 485 46.32 -109.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 945 DISTANCE = 5.92 ANGSTROMS
DBREF 6EP4 A 1 529 UNP P06276 CHLE_HUMAN 29 557
SEQADV 6EP4 GLN A 17 UNP P06276 ASN 45 ENGINEERED MUTATION
SEQADV 6EP4 GLN A 455 UNP P06276 ASN 483 ENGINEERED MUTATION
SEQADV 6EP4 GLN A 481 UNP P06276 ASN 509 ENGINEERED MUTATION
SEQADV 6EP4 GLN A 486 UNP P06276 ASN 514 ENGINEERED MUTATION
SEQRES 1 A 529 GLU ASP ASP ILE ILE ILE ALA THR LYS ASN GLY LYS VAL
SEQRES 2 A 529 ARG GLY MET GLN 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 GLN
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 GLN
SEQRES 38 A 529 GLU THR GLN ASN GLN 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
HET NAG B 1 14
HET NAG B 2 14
HET FUL B 3 10
HET NAG C 1 14
HET NAG C 2 14
HET FUL C 3 10
HET DME A 601 18
HET NAG A 602 14
HET NAG A 603 14
HET NAG A 607 14
HET NAG A 611 14
HET SO4 A 612 5
HET CL A 613 1
HET CL A 614 1
HET CL A 615 1
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM FUL BETA-L-FUCOPYRANOSE
HETNAM DME DECAMETHONIUM ION
HETNAM SO4 SULFATE ION
HETNAM CL CHLORIDE ION
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN FUL BETA-L-FUCOSE; 6-DEOXY-BETA-L-GALACTOPYRANOSE; L-
HETSYN 2 FUL FUCOSE; FUCOSE; 6-DEOXY-BETA-L-GALACTOSE
FORMUL 2 NAG 8(C8 H15 N O6)
FORMUL 2 FUL 2(C6 H12 O5)
FORMUL 4 DME C16 H38 N2 2+
FORMUL 9 SO4 O4 S 2-
FORMUL 10 CL 3(CL 1-)
FORMUL 13 HOH *245(H2 O)
HELIX 1 AA1 LEU A 38 ARG A 42 5 5
HELIX 2 AA2 PHE A 76 MET A 81 1 6
HELIX 3 AA3 LEU A 125 ASP A 129 5 5
HELIX 4 AA4 GLY A 130 ARG A 138 1 9
HELIX 5 AA5 GLY A 149 LEU A 154 1 6
HELIX 6 AA6 ASN A 165 ILE A 182 1 18
HELIX 7 AA7 ALA A 183 PHE A 185 5 3
HELIX 8 AA8 SER A 198 SER A 210 1 13
HELIX 9 AA9 SER A 210 SER A 215 1 6
HELIX 10 AB1 SER A 235 THR A 250 1 16
HELIX 11 AB2 ASN A 256 ARG A 265 1 10
HELIX 12 AB3 ASP A 268 ALA A 277 1 10
HELIX 13 AB4 MET A 302 LEU A 309 1 8
HELIX 14 AB5 GLY A 326 GLY A 333 5 8
HELIX 15 AB6 THR A 346 PHE A 358 1 13
HELIX 16 AB7 SER A 362 TYR A 373 1 12
HELIX 17 AB8 GLU A 383 PHE A 398 1 16
HELIX 18 AB9 PHE A 398 GLU A 411 1 14
HELIX 19 AC1 PRO A 431 GLY A 435 5 5
HELIX 20 AC2 GLU A 441 PHE A 446 1 6
HELIX 21 AC3 GLY A 447 GLN A 455 5 9
HELIX 22 AC4 THR A 457 GLY A 478 1 22
HELIX 23 AC5 ARG A 515 PHE A 525 1 11
HELIX 24 AC6 PHE A 526 VAL A 529 5 4
SHEET 1 AA1 3 ILE A 5 THR A 8 0
SHEET 2 AA1 3 GLY A 11 ARG A 14 -1 O VAL A 13 N ILE A 6
SHEET 3 AA1 3 ILE A 55 ASN A 57 1 O TRP A 56 N ARG A 14
SHEET 1 AA211 MET A 16 VAL A 20 0
SHEET 2 AA211 GLY A 23 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 ILE A 140
SHEET 6 AA211 GLY A 187 GLU A 197 1 O ASN A 188 N ALA A 107
SHEET 7 AA211 ARG A 219 GLN A 223 1 O GLN A 223 N GLY A 196
SHEET 8 AA211 ILE A 317 ASN A 322 1 O LEU A 318 N LEU A 222
SHEET 9 AA211 ALA A 416 PHE A 421 1 O PHE A 417 N VAL A 319
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
SSBOND 1 CYS A 65 CYS A 92 1555 1555 2.04
SSBOND 2 CYS A 252 CYS A 263 1555 1555 2.04
SSBOND 3 CYS A 400 CYS A 519 1555 1555 2.04
LINK ND2 ASN A 57 C1 NAG A 602 1555 1555 1.44
LINK ND2 ASN A 106 C1 NAG A 603 1555 1555 1.44
LINK ND2 ASN A 241 C1 NAG B 1 1555 1555 1.44
LINK ND2 ASN A 256 C1 NAG A 607 1555 1555 1.44
LINK ND2 ASN A 341 C1 NAG C 1 1555 1555 1.44
LINK ND2 ASN A 485 C1 NAG A 611 1555 1555 1.44
LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.44
LINK O6 NAG B 1 C1 FUL B 3 1555 1555 1.44
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.44
LINK O6 NAG C 1 C1 FUL C 3 1555 1555 1.44
CISPEP 1 ALA A 101 PRO A 102 0 -0.10
CRYST1 154.860 154.860 132.230 90.00 90.00 90.00 I 4 2 2 16
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 0.006457 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006457 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007563 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
