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HEADER HYDROLASE 24-OCT-17 6ESY
TITLE HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX WITH THIOFLAVINE T
CAVEAT 6ESY FUC A 604 HAS WRONG CHIRALITY AT ATOM C1 FUC A 611 HAS WRONG
CAVEAT 2 6ESY CHIRALITY AT ATOM C1 FUC B 610 HAS WRONG CHIRALITY AT ATOM
CAVEAT 3 6ESY C1
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;
COMPND 8 MUTATION: 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_TAXID: 7227;
SOURCE 8 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 6ESY 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. 2.80 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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.35
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 33659
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.209
REMARK 3 R VALUE (WORKING SET) : 0.206
REMARK 3 FREE R VALUE : 0.262
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.860
REMARK 3 FREE R VALUE TEST SET COUNT : 1635
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 39.3535 - 6.4020 0.98 2849 153 0.1940 0.2132
REMARK 3 2 6.4020 - 5.0849 0.99 2750 137 0.1938 0.2968
REMARK 3 3 5.0849 - 4.4431 0.99 2690 136 0.1616 0.2174
REMARK 3 4 4.4431 - 4.0373 0.99 2687 133 0.1657 0.2388
REMARK 3 5 4.0373 - 3.7482 0.99 2632 155 0.1779 0.2344
REMARK 3 6 3.7482 - 3.5274 0.99 2671 152 0.2051 0.2659
REMARK 3 7 3.5274 - 3.3508 1.00 2680 126 0.2413 0.2712
REMARK 3 8 3.3508 - 3.2050 1.00 2659 138 0.2518 0.3564
REMARK 3 9 3.2050 - 3.0817 0.99 2672 114 0.2720 0.3056
REMARK 3 10 3.0817 - 2.9754 0.98 2605 126 0.2935 0.3563
REMARK 3 11 2.9754 - 2.8824 0.98 2609 145 0.3308 0.4305
REMARK 3 12 2.8824 - 2.8000 0.94 2520 120 0.3829 0.3988
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) : 0.480
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.280
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 75.25
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 : 0.007 9009
REMARK 3 ANGLE : 1.594 12302
REMARK 3 CHIRALITY : 0.060 1352
REMARK 3 PLANARITY : 0.009 1562
REMARK 3 DIHEDRAL : 6.069 6151
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): -5.0992 -5.3663 -15.6308
REMARK 3 T TENSOR
REMARK 3 T11: 0.5123 T22: 0.4412
REMARK 3 T33: 0.3537 T12: -0.0294
REMARK 3 T13: -0.0415 T23: 0.0467
REMARK 3 L TENSOR
REMARK 3 L11: 2.6318 L22: 2.1152
REMARK 3 L33: 2.4432 L12: 0.0365
REMARK 3 L13: -0.7366 L23: -0.0403
REMARK 3 S TENSOR
REMARK 3 S11: 0.0272 S12: -0.4398 S13: -0.2099
REMARK 3 S21: 0.1539 S22: 0.0280 S23: 0.0268
REMARK 3 S31: 0.2129 S32: 0.0930 S33: -0.0702
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'B'
REMARK 3 ORIGIN FOR THE GROUP (A): 25.5259 -9.9433 -70.6543
REMARK 3 T TENSOR
REMARK 3 T11: 0.3997 T22: 0.4077
REMARK 3 T33: 0.4586 T12: -0.0025
REMARK 3 T13: -0.0428 T23: -0.0429
REMARK 3 L TENSOR
REMARK 3 L11: 1.9972 L22: 3.2041
REMARK 3 L33: 3.3307 L12: -0.1626
REMARK 3 L13: -0.6249 L23: -0.0221
REMARK 3 S TENSOR
REMARK 3 S11: 0.1460 S12: -0.0804 S13: 0.1769
REMARK 3 S21: 0.0706 S22: -0.0584 S23: -0.1689
REMARK 3 S31: -0.3357 S32: 0.2945 S33: -0.0917
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 6ESY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 25-OCT-17.
REMARK 100 THE DEPOSITION ID IS D_1200007207.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-APR-15
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 : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97242
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 : 33783
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 39.350
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 200 DATA REDUNDANCY : 4.600
REMARK 200 R MERGE (I) : 0.07808
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.0900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : 1.07300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.010
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 (%): 55.41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.76
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 37.13500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 114.46000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.62500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 114.46000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 37.13500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.62500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6540 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41640 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 43.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLU A 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 GLU A 259 CG CD OE1 OE2
REMARK 470 LYS A 262 CG CD CE NZ
REMARK 470 GLN A 380 CG CD OE1 NE2
REMARK 470 ARG A 453 CG CD NE CZ NH1 NH2
REMARK 470 SER B 53 OG
REMARK 470 ASP B 54 CG OD1 OD2
REMARK 470 THR B 483 OG1 CG2
REMARK 470 GLN B 484 CG CD OE1 NE2
REMARK 470 ASN B 485 CG OD1 ND2
REMARK 470 ASN B 486 CG OD1 ND2
REMARK 470 SER B 487 OG
REMARK 470 THR B 488 OG1 CG2
REMARK 470 SER B 489 OG
REMARK 470 GLU B 506 CG CD OE1 OE2
REMARK 470 SER B 507 OG
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 GLU A 506 CD OE1 OE2
REMARK 480 ILE B 4 O CG1 CG2 CD1
REMARK 480 LYS B 51 CB CG CD CE NZ
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 ND2 ASN B 256 O5 NAG B 603 1.95
REMARK 500 NH2 ARG A 381 OE1 GLU A 383 1.97
REMARK 500 ND2 ASN B 106 C2 NAG B 602 2.06
REMARK 500 O ARG B 40 NZ LYS B 44 2.15
REMARK 500 ND2 ASN B 57 C2 NAG B 601 2.15
REMARK 500 ND2 ASN A 481 O5 NAG A 608 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 CB PRO A 157 NH2 ARG B 453 3544 2.13
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 ASN B 455 CB ASN B 455 CG 0.177
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASN B 106 CB - CA - C ANGL. DEV. = -15.2 DEGREES
REMARK 500 ASN B 106 N - CA - CB ANGL. DEV. = 13.8 DEGREES
REMARK 500 LEU B 236 CB - CG - CD1 ANGL. DEV. = -11.7 DEGREES
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 -13.30 73.37
REMARK 500 THR A 50 -87.95 -108.87
REMARK 500 ASP A 54 -132.64 58.95
REMARK 500 CYS A 92 4.70 -154.68
REMARK 500 ASN A 106 61.07 -154.60
REMARK 500 PHE A 118 11.60 56.38
REMARK 500 PHE A 153 26.83 -143.61
REMARK 500 ALA A 162 76.79 -159.89
REMARK 500 SER A 198 -122.06 61.02
REMARK 500 CYS A 252 44.14 -150.73
REMARK 500 ASP A 297 -70.04 -111.17
REMARK 500 GLU A 383 0.81 -64.07
REMARK 500 PHE A 398 -60.35 -131.30
REMARK 500 GLU A 506 -71.66 -66.64
REMARK 500 LYS A 513 73.10 50.80
REMARK 500 PHE B 43 -1.60 75.86
REMARK 500 ASP B 54 -169.92 -76.02
REMARK 500 ALA B 58 59.74 -102.48
REMARK 500 ASN B 106 55.32 -141.05
REMARK 500 PHE B 118 9.51 59.43
REMARK 500 ALA B 162 68.37 -157.91
REMARK 500 SER B 198 -118.39 55.54
REMARK 500 THR B 218 -73.10 -105.58
REMARK 500 TYR B 282 52.30 -106.36
REMARK 500 ASP B 297 -70.55 -131.54
REMARK 500 ASP B 301 -158.48 -170.27
REMARK 500 ILE B 305 -80.48 -47.87
REMARK 500 LEU B 306 -36.97 -39.84
REMARK 500 TYR B 332 49.87 -108.44
REMARK 500 SER B 343 37.52 70.70
REMARK 500 PHE B 398 -59.77 -132.99
REMARK 500 TRP B 412 31.11 -87.94
REMARK 500 PRO B 480 53.59 -63.21
REMARK 500 GLN B 484 55.46 -112.43
REMARK 500 ASN B 485 -121.38 52.07
REMARK 500 PRO B 491 -165.79 -78.15
REMARK 500 LYS B 513 79.87 50.91
REMARK 500 PRO B 527 6.27 -68.18
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 TFX A 612
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TFX A 613
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 614
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TFX B 611
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TFX B 612
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 613
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
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: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 602 through FUC A 604 bound to ASN A 57
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 605 through NAG A 606 bound to ASN A 106
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 607 bound
REMARK 800 to ASN A 341
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 608 through NAG A 609 bound to ASN A 481
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 610 through FUC A 611 bound to ASN A 486
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 601 bound
REMARK 800 to ASN B 57
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 602 bound
REMARK 800 to ASN B 106
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B
REMARK 800 608 through FUC B 610 bound to ASN B 241
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 800 603 through NAG B 604 bound to ASN B 256
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 605 bound
REMARK 800 to ASN B 341
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 606 bound
REMARK 800 to ASN B 455
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 607 bound
REMARK 800 to ASN B 481
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6EP4 RELATED DB: PDB
REMARK 900 HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX WITH DECAMETHONIUM. CONTAINS
REMARK 900 THE SAME PROTEIN COMPLEXED WITH DIFFERENT LIGANDS
REMARK 900 RELATED ID: 6EQP RELATED DB: PDB
REMARK 900 HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX WITH ETHOPROPAZINE. CONTAINS
REMARK 900 THE SAME PROTEIN COMPLEXED WITH DIFFERENT LIGANDS
REMARK 900 RELATED ID: 6EQQ RELATED DB: PDB
REMARK 900 HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX WITH HUPRINE 19. CONTAINS
REMARK 900 THE SAME PROTEIN COMPLEXED WITH DIFFERENT LIGANDS
REMARK 900 RELATED ID: 6ESJ RELATED DB: PDB
REMARK 900 HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX WITH PROPIDIUM. CONTAINS THE
REMARK 900 SAME PROTEIN COMPLEXED WITH DIFFERENT LIGANDS
DBREF 6ESY A 1 529 UNP P06276 CHLE_HUMAN 29 557
DBREF 6ESY 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 FUC A 604 10
HET NAG A 605 14
HET NAG A 606 14
HET NAG A 607 14
HET NAG A 608 14
HET NAG A 609 14
HET NAG A 610 14
HET FUC A 611 10
HET TFX A 612 20
HET TFX A 613 20
HET CL A 614 1
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 FUC B 610 10
HET TFX B 611 20
HET TFX B 612 20
HET CL B 613 1
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM FUC ALPHA-L-FUCOSE
HETNAM TFX 2-[4-(DIMETHYLAMINO)PHENYL]-3,6-DIMETHYL-1,3-
HETNAM 2 TFX BENZOTHIAZOL-3-IUM
HETNAM CL CHLORIDE ION
HETSYN TFX THIOFLAVIN T
FORMUL 3 NAG 18(C8 H15 N O6)
FORMUL 4 FUC 3(C6 H12 O5)
FORMUL 9 TFX 4(C17 H19 N2 S 1+)
FORMUL 11 CL 2(CL 1-)
FORMUL 22 HOH *41(H2 O)
HELIX 1 AA1 PHE A 76 MET A 81 1 6
HELIX 2 AA2 LEU A 125 ASP A 129 5 5
HELIX 3 AA3 GLY A 130 GLU A 137 1 8
HELIX 4 AA4 GLY A 149 LEU A 154 1 6
HELIX 5 AA5 ASN A 165 ILE A 182 1 18
HELIX 6 AA6 SER A 198 LEU A 208 1 11
HELIX 7 AA7 SER A 210 HIS A 214 5 5
HELIX 8 AA8 SER A 235 THR A 250 1 16
HELIX 9 AA9 ASN A 256 ARG A 265 1 10
HELIX 10 AB1 ASP A 268 LEU A 274 1 7
HELIX 11 AB2 ASN A 275 VAL A 279 5 5
HELIX 12 AB3 MET A 302 LEU A 309 1 8
HELIX 13 AB4 GLY A 326 GLY A 333 5 8
HELIX 14 AB5 THR A 346 PHE A 358 1 13
HELIX 15 AB6 SER A 362 TYR A 373 1 12
HELIX 16 AB7 GLU A 383 PHE A 398 1 16
HELIX 17 AB8 PHE A 398 GLU A 411 1 14
HELIX 18 AB9 PRO A 431 GLY A 435 5 5
HELIX 19 AC1 GLU A 441 PHE A 446 1 6
HELIX 20 AC2 GLY A 447 ASN A 455 5 9
HELIX 21 AC3 THR A 457 GLY A 478 1 22
HELIX 22 AC4 ARG A 515 PHE A 525 1 11
HELIX 23 AC5 PHE A 526 VAL A 529 5 4
HELIX 24 AC6 LEU B 38 ARG B 42 5 5
HELIX 25 AC7 PHE B 76 MET B 81 1 6
HELIX 26 AC8 LEU B 125 ASP B 129 5 5
HELIX 27 AC9 GLY B 130 GLU B 137 1 8
HELIX 28 AD1 GLY B 149 LEU B 154 1 6
HELIX 29 AD2 ASN B 165 ILE B 182 1 18
HELIX 30 AD3 ALA B 183 PHE B 185 5 3
HELIX 31 AD4 SER B 198 LEU B 208 1 11
HELIX 32 AD5 SER B 210 HIS B 214 5 5
HELIX 33 AD6 SER B 235 THR B 250 1 16
HELIX 34 AD7 ASN B 256 LYS B 267 1 12
HELIX 35 AD8 ASP B 268 LEU B 274 1 7
HELIX 36 AD9 ASN B 275 VAL B 279 5 5
HELIX 37 AE1 MET B 302 GLY B 310 1 9
HELIX 38 AE2 GLY B 326 VAL B 331 1 6
HELIX 39 AE3 THR B 346 PHE B 358 1 13
HELIX 40 AE4 SER B 362 TYR B 373 1 12
HELIX 41 AE5 GLU B 383 PHE B 398 1 16
HELIX 42 AE6 PHE B 398 TRP B 412 1 15
HELIX 43 AE7 PRO B 431 GLY B 435 5 5
HELIX 44 AE8 GLU B 441 PHE B 446 1 6
HELIX 45 AE9 GLY B 447 GLU B 451 5 5
HELIX 46 AF1 THR B 457 GLY B 478 1 22
HELIX 47 AF2 ARG B 515 PHE B 525 1 11
HELIX 48 AF3 PHE B 526 VAL B 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 GLY A 11 N THR A 8
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 GLY A 23 N VAL A 20
SHEET 3 AA211 TYR A 94 PRO A 100 -1 O LEU A 95 N ILE A 31
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 ARG A 219 N LEU A 194
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 421 N VAL A 321
SHEET 10 AA211 LYS A 499 LEU A 503 1 O LEU A 501 N TYR A 420
SHEET 11 AA211 ILE A 510 THR A 512 -1 O MET A 511 N TYR A 500
SHEET 1 AA3 3 ILE B 5 ALA B 7 0
SHEET 2 AA3 3 LYS B 12 ARG B 14 -1 O VAL B 13 N ILE B 6
SHEET 3 AA3 3 ILE B 55 ASN B 57 1 O TRP B 56 N LYS B 12
SHEET 1 AA411 MET B 16 VAL B 20 0
SHEET 2 AA411 GLY B 23 PRO B 32 -1 O VAL B 25 N LEU B 18
SHEET 3 AA411 TYR B 94 ALA B 101 -1 O VAL B 97 N PHE B 28
SHEET 4 AA411 ILE B 140 MET B 144 -1 O VAL B 141 N TRP B 98
SHEET 5 AA411 ALA B 107 ILE B 113 1 N TRP B 112 O VAL B 142
SHEET 6 AA411 GLY B 187 GLU B 197 1 O ASN B 188 N ALA B 107
SHEET 7 AA411 ARG B 219 GLN B 223 1 O ILE B 221 N LEU B 194
SHEET 8 AA411 ILE B 317 ASN B 322 1 O LEU B 318 N LEU B 222
SHEET 9 AA411 ALA B 416 PHE B 421 1 O PHE B 417 N VAL B 319
SHEET 10 AA411 LYS B 499 LEU B 503 1 O LEU B 501 N PHE B 418
SHEET 11 AA411 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 2.10
SSBOND 3 CYS A 400 CYS A 519 1555 1555 2.03
SSBOND 4 CYS B 65 CYS B 92 1555 1555 2.03
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 1.45
LINK ND2 ASN A 57 C1 NAG A 602 1555 1555 1.44
LINK ND2 ASN A 106 C1 NAG A 605 1555 1555 1.44
LINK ND2 ASN A 341 C1 NAG A 607 1555 1555 1.44
LINK ND2 ASN A 481 C1 NAG A 608 1555 1555 1.44
LINK ND2 ASN A 486 C1 NAG A 610 1555 1555 1.46
LINK ND2 ASN B 57 C1 NAG B 601 1555 1555 1.40
LINK ND2 ASN B 106 C1 NAG B 602 1555 1555 1.23
LINK ND2 ASN B 241 C1 NAG B 608 1555 1555 1.45
LINK ND2 ASN B 256 C1 NAG B 603 1555 1555 1.44
LINK ND2 ASN B 341 C1 NAG B 605 1555 1555 1.43
LINK ND2 ASN B 455 C1 NAG B 606 1555 1555 1.49
LINK ND2 ASN B 481 C1 NAG B 607 1555 1555 1.44
LINK O4 NAG A 602 C1 NAG A 603 1555 1555 1.45
LINK O6 NAG A 602 C1 FUC A 604 1555 1555 1.45
LINK O4 NAG A 605 C1 NAG A 606 1555 1555 1.45
LINK O4 NAG A 608 C1 NAG A 609 1555 1555 1.44
LINK O6 NAG A 610 C1 FUC A 611 1555 1555 1.45
LINK O4 NAG B 603 C1 NAG B 604 1555 1555 1.44
LINK O4 NAG B 608 C1 NAG B 609 1555 1555 1.44
LINK O6 NAG B 608 C1 FUC B 610 1555 1555 1.44
CISPEP 1 ALA A 101 PRO A 102 0 3.96
CISPEP 2 ALA B 101 PRO B 102 0 3.12
SITE 1 AC1 6 GLY A 117 THR A 120 SER A 198 TRP A 231
SITE 2 AC1 6 LEU A 286 TFX A 613
SITE 1 AC2 6 TRP A 82 PRO A 285 PHE A 329 TYR A 332
SITE 2 AC2 6 HIS A 438 TFX A 612
SITE 1 AC3 1 LYS A 476
SITE 1 AC4 5 GLY B 117 THR B 120 SER B 198 LEU B 286
SITE 2 AC4 5 TFX B 612
SITE 1 AC5 4 PRO B 285 PHE B 329 TYR B 332 TFX B 611
SITE 1 AC6 1 TRP B 433
SITE 1 AC7 2 ASN A 17 THR A 24
SITE 1 AC8 4 ARG A 14 ILE A 55 ASN A 57 LYS B 12
SITE 1 AC9 2 ASN A 106 ASN A 188
SITE 1 AD1 2 SER A 338 ASN A 341
SITE 1 AD2 7 ASN A 473 ASN A 481 GLU A 482 CYS B 66
SITE 2 AD2 7 ASP B 87 LEU B 88 GLN B 270
SITE 1 AD3 2 ASN A 486 GLY B 75
SITE 1 AD4 2 ARG B 14 ASN B 57
SITE 1 AD5 2 ASN B 106 ASN B 188
SITE 1 AD6 7 TYR B 237 ASN B 241 ASN B 245 LEU B 249
SITE 2 AD6 7 PHE B 278 TYR B 282 GLN B 380
SITE 1 AD7 3 ASN B 256 GLU B 259 GLU B 411
SITE 1 AD8 2 SER B 338 ASN B 341
SITE 1 AD9 2 TYR A 237 ASN B 455
SITE 1 AE1 3 TYR B 477 ASN B 481 THR B 483
CRYST1 74.270 79.250 228.920 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 0.013464 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012618 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004368 0.00000
TER 4205 VAL A 529
TER 8372 VAL B 529
MASTER 509 0 27 48 28 0 24 6 8752 2 387 82
END |