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HEADER HYDROLASE 04-JUL-12 4B0P
TITLE CRYSTAL STRUCTURE OF SOMAN-AGED HUMAN BUTYRYLCHOLINESTERASE IN
TITLE 2 COMPLEX WITH METHYL 2-(PENTAFLUOROBENZYLOXYIMINO) PYRIDINIUM
CAVEAT 4B0P NAG A 2181 C1 HAS INCORRECT CHIRALITY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHOLINESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 29-557;
COMPND 5 SYNONYM: BUTYRYLCHOLINESTERASE, ACYLCHOLINE ACYLHYDROLASE,
COMPND 6 BUTYRYLCHOLINE ESTERASE, CHOLINE ESTERASE II,
COMPND 7 PSEUDOCHOLINESTERASE;
COMPND 8 EC: 3.1.1.8;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: CHO-K1;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGS
KEYWDS HYDROLASE, AGING
EXPDTA X-RAY DIFFRACTION
AUTHOR M.WANDHAMMER,M.DE KONING,M.VAN GROL,D.NOORT,M.GOELDNER,F.NACHON
REVDAT 1 29-AUG-12 4B0P 0
JRNL AUTH M.WANDHAMMER,M.DE KONING,M.VAN GROL,M.LOIODICE,L.SAUREL,
JRNL AUTH 2 D.NOORT,M.GOELDNER,F.NACHON
JRNL TITL A STEP TOWARD THE REACTIVATION OF AGED CHOLINESTERASES -
JRNL TITL 2 CRYSTAL STRUCTURE OF LIGANDS BINDING TO AGED HUMAN
JRNL TITL 3 BUTYRYLCHOLINESTERASE
JRNL REF CHEM.BIOL.INTERACT 2012
JRNL REFN ESSN 1872-7786
JRNL DOI 10.1016/J.CBI.2012.08.005
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT 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) : 2.500
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.878
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.36
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.70
REMARK 3 NUMBER OF REFLECTIONS : 27798
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.1663
REMARK 3 R VALUE (WORKING SET) : 0.1644
REMARK 3 FREE R VALUE : 0.2120
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.0
REMARK 3 FREE R VALUE TEST SET COUNT : 1112
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 30.8808 - 4.9939 0.95 3392 141 0.1684 0.2111
REMARK 3 2 4.9939 - 3.9664 0.98 3345 139 0.1283 0.1378
REMARK 3 3 3.9664 - 3.4658 0.99 3324 139 0.1471 0.2062
REMARK 3 4 3.4658 - 3.1493 1.00 3353 140 0.1753 0.2610
REMARK 3 5 3.1493 - 2.9237 1.00 3331 139 0.1930 0.2779
REMARK 3 6 2.9237 - 2.7515 1.00 3322 138 0.1994 0.2422
REMARK 3 7 2.7515 - 2.6137 1.00 3313 138 0.2071 0.2914
REMARK 3 8 2.6137 - 2.5000 0.99 3306 138 0.1969 0.2461
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 : 0.354
REMARK 3 B_SOL : 58.980
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.25
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.85
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 45.80
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 : 0.006 4535
REMARK 3 ANGLE : 1.259 6175
REMARK 3 CHIRALITY : 0.091 671
REMARK 3 PLANARITY : 0.005 782
REMARK 3 DIHEDRAL : 21.089 1684
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND (RESID 3 THROUGH 242)
REMARK 3 ORIGIN FOR THE GROUP (A): 29.6377 17.6955 37.8462
REMARK 3 T TENSOR
REMARK 3 T11: 0.3115 T22: 0.3797
REMARK 3 T33: 0.2918 T12: -0.0748
REMARK 3 T13: -0.0363 T23: -0.0817
REMARK 3 L TENSOR
REMARK 3 L11: 1.9780 L22: 1.8861
REMARK 3 L33: 2.3284 L12: 0.2613
REMARK 3 L13: 0.3384 L23: 0.3588
REMARK 3 S TENSOR
REMARK 3 S11: 0.1645 S12: -0.4942 S13: 0.1018
REMARK 3 S21: 0.4672 S22: -0.0819 S23: -0.0560
REMARK 3 S31: -0.1036 S32: 0.0094 S33: -0.0681
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND (RESID 243 THROUGH 322)
REMARK 3 ORIGIN FOR THE GROUP (A): 40.8139 3.2360 33.1803
REMARK 3 T TENSOR
REMARK 3 T11: 0.3971 T22: 0.4499
REMARK 3 T33: 0.4974 T12: 0.0071
REMARK 3 T13: -0.1547 T23: -0.0578
REMARK 3 L TENSOR
REMARK 3 L11: 3.7067 L22: 1.8618
REMARK 3 L33: 3.0680 L12: 0.0063
REMARK 3 L13: 1.3526 L23: -0.3177
REMARK 3 S TENSOR
REMARK 3 S11: 0.1511 S12: -0.2532 S13: -0.3263
REMARK 3 S21: 0.4397 S22: -0.0796 S23: -0.5735
REMARK 3 S31: 0.3436 S32: 0.6100 S33: -0.1093
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN A AND (RESID 323 THROUGH 529)
REMARK 3 ORIGIN FOR THE GROUP (A): 32.4078 19.0139 12.2258
REMARK 3 T TENSOR
REMARK 3 T11: 0.3271 T22: 0.2907
REMARK 3 T33: 0.2484 T12: -0.0466
REMARK 3 T13: -0.0545 T23: -0.0457
REMARK 3 L TENSOR
REMARK 3 L11: 3.1868 L22: 2.3365
REMARK 3 L33: 2.2759 L12: -0.2495
REMARK 3 L13: -0.5045 L23: 0.9473
REMARK 3 S TENSOR
REMARK 3 S11: 0.0195 S12: 0.2242 S13: 0.1411
REMARK 3 S21: -0.3737 S22: 0.1141 S23: -0.0932
REMARK 3 S31: -0.2717 S32: 0.1716 S33: -0.1257
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN A AND (RESID 1178 THROUGH 1178)
REMARK 3 ORIGIN FOR THE GROUP (A): 26.0479 29.6894 32.4666
REMARK 3 T TENSOR
REMARK 3 T11: 0.1944 T22: 0.1275
REMARK 3 T33: 0.2615 T12: -0.1003
REMARK 3 T13: 0.0236 T23: 0.0388
REMARK 3 L TENSOR
REMARK 3 L11: 8.6804 L22: 1.2667
REMARK 3 L33: 4.4780 L12: 2.1396
REMARK 3 L13: 5.7230 L23: 0.6878
REMARK 3 S TENSOR
REMARK 3 S11: 0.0461 S12: 0.3860 S13: -0.3821
REMARK 3 S21: -0.0075 S22: 0.4091 S23: -0.0882
REMARK 3 S31: 0.1327 S32: 0.3411 S33: -0.4192
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 4B0P COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-JUN-12.
REMARK 100 THE PDBE ID CODE IS EBI-52875.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-SEP-11
REMARK 200 TEMPERATURE (KELVIN) : 77
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 : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00407
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD (QUANTUM Q315R)
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27807
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.50
REMARK 200 RESOLUTION RANGE LOW (A) : 30.88
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 3.2
REMARK 200 R MERGE (I) : 0.01
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 21.40
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.60
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.2
REMARK 200 DATA REDUNDANCY IN SHELL : 3.2
REMARK 200 R MERGE FOR SHELL (I) : 0.06
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.58
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 1P0I
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.16
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.1 M AMMONIUM SULFATE, 0.1 M
REMARK 280 MES BUFFER PH 6.5
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 77.11500
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 77.11500
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 66.93000
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 77.11500
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 77.11500
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 66.93000
REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 77.11500
REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 77.11500
REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 66.93000
REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 77.11500
REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 77.11500
REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 66.93000
REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 77.11500
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 77.11500
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 66.93000
REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 77.11500
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 77.11500
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 66.93000
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 77.11500
REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 77.11500
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 66.93000
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 77.11500
REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 77.11500
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 66.93000
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: 9020 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41880 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -104.3 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 BIOMT1 2 0.000000 -1.000000 0.000000 77.11500
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 77.11500
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 66.93000
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 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 TYR A 237 CZ
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 NH1 ARG A 14 OD1 ASN A 57 2.20
REMARK 500 NH1 ARG A 240 OE2 GLU A 257 2.12
REMARK 500 ND2 ASN A 256 C2 NAG A 2188 2.18
REMARK 500 NZ LYS A 262 O HOH A 3098 2.19
REMARK 500 O HOH A 3071 O HOH A 3123 2.10
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 43 -4.12 75.06
REMARK 500 LYS A 51 141.91 88.46
REMARK 500 ASP A 54 166.56 63.39
REMARK 500 ASN A 106 56.65 -155.05
REMARK 500 ALA A 162 79.25 -158.03
REMARK 500 GLU A 257 -33.69 -39.52
REMARK 500 ASP A 297 -73.43 -132.41
REMARK 500 TRP A 376 151.81 -47.70
REMARK 500 VAL A 377 60.79 -118.80
REMARK 500 ASP A 378 46.56 -99.71
REMARK 500 GLN A 380 73.80 -115.61
REMARK 500 PHE A 398 -57.81 -134.10
REMARK 500 ASN A 485 58.78 -105.93
REMARK 500 ASN A 486 34.71 35.59
REMARK 500 THR A 496 -72.45 -68.54
REMARK 500 GLU A 506 -107.16 -96.34
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 NA A2190 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 443 OE1
REMARK 620 2 HOH A3145 O 77.6
REMARK 620 3 HOH A3187 O 111.2 117.6
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A1171 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SBG A 198 O2
REMARK 620 2 HOH A3021 O 86.9
REMARK 620 3 HOH A3064 O 144.4 74.6
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLY A1178
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A1170
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A1171
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MF5 A1179
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A2190
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A2191
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A2193
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A2194
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A2195
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A2197
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A2198
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NAG A2179 BOUND TO ASN A 57
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NAG A2180 BOUND TO ASN A 106
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO
REMARK 800 ASN A 241 RESIDUES 2181 TO 2183
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NAG A2188 BOUND TO ASN A 256
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO
REMARK 800 ASN A 341 RESIDUES 2184 TO 2186
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NAG A2187 BOUND TO ASN A 485
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1EHO RELATED DB: PDB
REMARK 900 MODEL OF (-)-COCAINE-BOUND BCHE COMPLEX.
REMARK 900 RELATED ID: 1EHQ RELATED DB: PDB
REMARK 900 MODEL OF (+)-COCAINE-BOUND BCHE COMPLEX
REMARK 900 RELATED ID: 1KCJ RELATED DB: PDB
REMARK 900 MODEL OF (-)-COCAINE-BOUND (-)-COCAINE HYDROLASE COMPLEX
REMARK 900 RELATED ID: 1P0I RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN BUTYRYL CHOLINESTERASE
REMARK 900 RELATED ID: 1P0M RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN BUTYRYL CHOLINESTERASE
REMARK 900 INCOMPLEX WITH A CHOLINE MOLECULE
REMARK 900 RELATED ID: 1P0P RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF SOMAN-AGED HUMAN
REMARK 900 BUTYRYLCHOLINESTERASE IN COMPLEX WITH THE SUBSTRATE
REMARK 900 ANALOGBUTYRYLTHIOCHOLINE
REMARK 900 RELATED ID: 1P0Q RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF SOMAN-AGED HUMAN BUTYRYL
REMARK 900 CHOLINESTERASE
REMARK 900 RELATED ID: 1XLU RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF DI-ISOPROPYL-PHOSPHORO-FLUORIDATE (
REMARK 900 DFP)INHIBITED BUTYRYLCHOLINESTERASE AFTER AGING
REMARK 900 RELATED ID: 1XLV RELATED DB: PDB
REMARK 900 ETHYLPHOSPHORYLATED BUTYRYLCHOLINESTERASE (AGED) OBTAINEDBY
REMARK 900 REACTION WITH ECHOTHIOPHATE
REMARK 900 RELATED ID: 1XLW RELATED DB: PDB
REMARK 900 DIETHYLPHOSPHORYLATED BUTYRYLCHOLINESTERASE (NONAGED)OBTAINED
REMARK 900 BY REACTION WITH ECHOTHIOPHATE
REMARK 900 RELATED ID: 2J4C RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX WITH
REMARK 900 10MM HGCL2
REMARK 900 RELATED ID: 2WID RELATED DB: PDB
REMARK 900 AGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY
REMARK 900 TABUN ANALOGUE TA1
REMARK 900 RELATED ID: 2WIF RELATED DB: PDB
REMARK 900 AGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY
REMARK 900 TABUN ANALOGUE TA1
REMARK 900 RELATED ID: 2WIG RELATED DB: PDB
REMARK 900 NONAGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY
REMARK 900 TABUN ANALOGUE TA4
REMARK 900 RELATED ID: 2WIJ RELATED DB: PDB
REMARK 900 NONAGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY
REMARK 900 TABUN ANALOGUE TA5
REMARK 900 RELATED ID: 2WIK RELATED DB: PDB
REMARK 900 NONAGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY
REMARK 900 TABUN ANALOGUE TA6
REMARK 900 RELATED ID: 2WIL RELATED DB: PDB
REMARK 900 AGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY
REMARK 900 TABUN ANALOGUE TA5
REMARK 900 RELATED ID: 2WSL RELATED DB: PDB
REMARK 900 AGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY
REMARK 900 TABUN ANALOGUE TA4
REMARK 900 RELATED ID: 2XMB RELATED DB: PDB
REMARK 900 G117H MUTANT OF HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX
REMARK 900 WITH SULFATE
REMARK 900 RELATED ID: 2XMC RELATED DB: PDB
REMARK 900 G117H MUTANT OF HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX
REMARK 900 WITH FLUORIDE ANION
REMARK 900 RELATED ID: 2XMD RELATED DB: PDB
REMARK 900 G117H MUTANT OF HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX
REMARK 900 WITH ECHOTHIOPHATE
REMARK 900 RELATED ID: 2XMG RELATED DB: PDB
REMARK 900 G117H MUTANT OF HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX
REMARK 900 WITH VX
REMARK 900 RELATED ID: 2XQF RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED
REMARK 900 BY RACEMIC VX
REMARK 900 RELATED ID: 2XQG RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED
REMARK 900 BY RACEMIC VR
REMARK 900 RELATED ID: 2XQI RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED
REMARK 900 BY RACEMIC CVX
REMARK 900 RELATED ID: 2XQJ RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED
REMARK 900 BY PURE ENANTIOMER VX-(R)
REMARK 900 RELATED ID: 2XQK RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED
REMARK 900 BY PURE ENANTIOMER VX-(S)
REMARK 900 RELATED ID: 2Y1K RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY CBDP
REMARK 900 (12H SOAK): PHOSPHOSERINE ADDUCT
REMARK 900 RELATED ID: 4AQD RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF FULLY GLYCOSYLATED HUMAN
REMARK 900 BUTYRYLCHOLINESTERASE
REMARK 900 RELATED ID: 4AXB RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF SOMAN-AGED HUMAN
REMARK 900 BUTYRYLCHOLINESTERASE IN COMPLEX WITH 2-PAM
REMARK 900 RELATED ID: 4B0O RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF SOMAN-AGED HUMAN
REMARK 900 BUTYRYLCHOLINESTERASE IN COMPLEX WITH BENZYL PYRIDINIUM-4
REMARK 900 -METHYLTRICHLOROACETIMIDATE
DBREF 4B0P A 1 529 UNP P06276 CHLE_HUMAN 29 557
SEQADV 4B0P GLN A 17 UNP P06276 ASN 45 CONFLICT
SEQADV 4B0P GLN A 384 UNP P06276 ASN 412 CONFLICT
SEQADV 4B0P GLN A 455 UNP P06276 ASN 483 CONFLICT
SEQADV 4B0P GLN A 481 UNP P06276 ASN 509 CONFLICT
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 SBG 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 GLN 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 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
MODRES 4B0P SBG A 198 SER MODIFIED SERINE
HET SBG A 198 10
HET GLY A1178 5
HET NA A1170 1
HET K A1171 1
HET MF5 A1179 22
HET NAG A2179 14
HET NAG A2180 14
HET NAG A2181 14
HET NAG A2182 14
HET FUL A2183 10
HET NAG A2184 14
HET NAG A2185 14
HET FUL A2186 10
HET NAG A2187 14
HET NAG A2188 14
HET NA A2190 1
HET CA A2191 1
HET CA A2192 1
HET CL A2193 1
HET CL A2194 1
HET CL A2195 1
HET CL A2196 1
HET CA A2197 1
HET CA A2198 1
HETNAM SBG O-[(S)-HYDROXY(METHYL)PHOSPHORYL]-L-SERINE
HETNAM GLY GLYCINE
HETNAM NA SODIUM ION
HETNAM K POTASSIUM ION
HETNAM MF5 1-(1-METHYLPYRIDIN-1-IUM-2-YL)-N-[[2,3,4,5,6-PENTAKIS(FLUORANYL)
HETNAM 2 MF5 PHENYL]METHOXY]METHANIMINE
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM FUL BETA-L-FUCOSE
HETNAM CA CALCIUM ION
HETNAM CL CHLORIDE ION
HETSYN MF5 METHYL2-(PENTAFLUOROBENZYLOXYIMINO)PYRIDINIUM
HETSYN FUL 6-DEOXY-BETA-L-GALACTOSE
FORMUL 1 SBG C4 H10 N O5 P
FORMUL 2 GLY C2 H5 N O2
FORMUL 3 NA 2(NA 1+)
FORMUL 4 K K 1+
FORMUL 5 MF5 C14 H10 F5 N2 O 1+
FORMUL 6 NAG 8(C8 H15 N O6)
FORMUL 7 FUL 2(C6 H12 O5)
FORMUL 8 CA 4(CA 2+)
FORMUL 9 CL 4(CL 1-)
FORMUL 10 HOH *188(H2 O)
HELIX 1 1 LEU A 38 ARG A 42 5 5
HELIX 2 2 PHE A 76 MET A 81 1 6
HELIX 3 3 LEU A 125 ASP A 129 5 5
HELIX 4 4 GLY A 130 ARG A 138 1 9
HELIX 5 5 VAL A 148 LEU A 154 1 7
HELIX 6 6 ASN A 165 ILE A 182 1 18
HELIX 7 7 ALA A 183 PHE A 185 5 3
HELIX 8 8 ALA A 199 SER A 210 1 12
HELIX 9 9 PRO A 211 HIS A 214 5 4
HELIX 10 10 SER A 235 THR A 250 1 16
HELIX 11 11 ASN A 256 ASN A 266 1 11
HELIX 12 12 ASP A 268 ALA A 277 1 10
HELIX 13 13 PHE A 278 VAL A 280 5 3
HELIX 14 14 MET A 302 LEU A 309 1 8
HELIX 15 15 GLY A 326 VAL A 331 1 6
HELIX 16 16 THR A 346 PHE A 358 1 13
HELIX 17 17 SER A 362 THR A 374 1 13
HELIX 18 18 GLU A 383 PHE A 398 1 16
HELIX 19 19 PHE A 398 GLU A 411 1 14
HELIX 20 20 PRO A 431 GLY A 435 5 5
HELIX 21 21 GLU A 441 PHE A 446 1 6
HELIX 22 22 GLY A 447 GLU A 451 5 5
HELIX 23 23 GLU A 451 GLN A 455 5 5
HELIX 24 24 THR A 457 GLY A 478 1 22
HELIX 25 25 ARG A 515 PHE A 525 1 11
HELIX 26 26 PHE A 526 VAL A 529 5 4
SHEET 1 AA 3 ILE A 5 THR A 8 0
SHEET 2 AA 3 GLY A 11 ARG A 14 -1 O GLY A 11 N THR A 8
SHEET 3 AA 3 TRP A 56 ASN A 57 1 O TRP A 56 N ARG A 14
SHEET 1 AB11 MET A 16 VAL A 20 0
SHEET 2 AB11 GLY A 23 PRO A 32 -1 O GLY A 23 N VAL A 20
SHEET 3 AB11 TYR A 94 PRO A 100 -1 O LEU A 95 N ILE A 31
SHEET 4 AB11 ILE A 140 MET A 144 -1 O VAL A 141 N TRP A 98
SHEET 5 AB11 ALA A 107 ILE A 113 1 O THR A 108 N ILE A 140
SHEET 6 AB11 GLY A 187 GLY A 196 1 N ASN A 188 O ALA A 107
SHEET 7 AB11 ARG A 219 GLN A 223 1 O ARG A 219 N LEU A 194
SHEET 8 AB11 ILE A 317 ASN A 322 1 O LEU A 318 N LEU A 222
SHEET 9 AB11 ALA A 416 PHE A 421 1 O PHE A 417 N VAL A 319
SHEET 10 AB11 LYS A 499 LEU A 503 1 O LEU A 501 N TYR A 420
SHEET 11 AB11 ARG A 509 THR A 512 -1 O ARG A 509 N THR A 502
SHEET 1 AC 2 SER A 64 CYS A 65 0
SHEET 2 AC 2 LEU A 88 SER A 89 1 N SER A 89 O SER A 64
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 2.05
LINK ND2 ASN A 57 C1 NAG A2179 1555 1555 1.46
LINK ND2 ASN A 106 C1 NAG A2180 1555 1555 1.46
LINK O2 SBG A 198 K K A1171 1555 1555 3.29
LINK N SBG A 198 C GLU A 197 1555 1555 1.33
LINK C SBG A 198 N ALA A 199 1555 1555 1.33
LINK ND2 ASN A 241 C1 NAG A2181 1555 1555 1.46
LINK ND2 ASN A 256 C1 NAG A2188 1555 1555 1.44
LINK ND2 ASN A 341 C1 NAG A2184 1555 1555 1.44
LINK ND2 ASN A 485 C1 NAG A2187 1555 1555 1.45
LINK K K A1171 O HOH A3021 1555 1555 2.84
LINK K K A1171 O HOH A3064 1555 1555 2.86
LINK O6 NAG A2181 C1 FUL A2183 1555 1555 1.44
LINK O4 NAG A2181 C1 NAG A2182 1555 1555 1.46
LINK O6 NAG A2184 C1 FUL A2186 1555 1555 1.44
LINK O4 NAG A2184 C1 NAG A2185 1555 1555 1.44
LINK NA NA A2190 O HOH A3187 1555 1555 2.66
LINK NA NA A2190 O HOH A3145 1555 1555 2.50
LINK NA NA A2190 OE1 GLU A 443 1555 1555 2.97
LINK CA CA A2197 SG CYS A 66 1555 1555 2.72
CISPEP 1 ALA A 101 PRO A 102 0 -2.80
CISPEP 2 VAL A 377 ASP A 378 0 -19.12
SITE 1 AC1 5 LEU A 18 TYR A 61 TRP A 98 ASP A 129
SITE 2 AC1 5 LYS A 131
SITE 1 AC2 2 GLU A 80 ASN A 83
SITE 1 AC3 3 SBG A 198 HOH A3021 HOH A3064
SITE 1 AC4 11 ASP A 70 TRP A 82 GLY A 116 GLU A 197
SITE 2 AC4 11 PRO A 285 ALA A 328 PHE A 329 TYR A 332
SITE 3 AC4 11 HIS A 438 GLY A 439 HOH A3041
SITE 1 AC5 4 MET A 81 GLU A 443 HOH A3145 HOH A3187
SITE 1 AC6 1 TYR A 420
SITE 1 AC7 2 ARG A 242 VAL A 288
SITE 1 AC8 1 ARG A 347
SITE 1 AC9 2 THR A 512 LYS A 513
SITE 1 BC1 2 CYS A 66 GLN A 270
SITE 1 BC2 1 PHE A 217
SITE 1 BC3 2 ARG A 14 ASN A 57
SITE 1 BC4 4 ASN A 106 ASN A 188 LYS A 190 HOH A3184
SITE 1 BC5 6 TYR A 237 ASN A 241 ASN A 245 LEU A 249
SITE 2 BC5 6 PHE A 278 PRO A 281
SITE 1 BC6 1 ASN A 256
SITE 1 BC7 7 PRO A 335 GLY A 336 PHE A 337 SER A 338
SITE 2 BC7 7 ASN A 341 ASN A 342 HOH A3185
SITE 1 BC8 4 ARG A 465 GLU A 482 ASN A 485 HOH A3186
CRYST1 154.230 154.230 133.860 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 0.006484 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006484 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007470 0.00000
TER 4238 VAL A 529
MASTER 562 0 24 26 16 0 22 6 4595 1 192 41
END |