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HEADER HYDROLASE 08-NOV-20 7AWH
TITLE CRYSTAL STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX WITH TERT-
TITLE 2 BUTYL 3-(((2-((1-(BENZENESULFONYL)-1H-INDOL-4-YL)OXY)ETHYL)AMINO)
TITLE 3 METHYL)PIPERIDINE-1-CARBOXYLATE
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;
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: CRICETULUS GRISEUS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 10029
KEYWDS BUTYRYLCHOLINESTERASE, INHIBITOR COMPLEX, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR X.BRAZZOLOTTO,T.WICHUR,A.WIECKOWSKA
REVDAT 1 29-SEP-21 7AWH 0
JRNL AUTH X.BRAZZOLOTTO,T.WICHUR,A.WIECKOWSKA
JRNL TITL CRYSTAL STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX
JRNL TITL 2 WITH (2-((1-(BENZENESULFONYL)-1H-INDOL-4-YL)OXY)ETHYL)
JRNL TITL 3 (BENZYL)AMINE
JRNL REF TO BE PUBLISHED
JRNL REFN
JRNL DOI 10.1016/J.EJMECH.2021.113792
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.19RC4_4035
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) : 48.85
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 34389
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.193
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.222
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1032
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 48.8500 - 4.4000 1.00 4984 155 0.1705 0.1961
REMARK 3 2 4.4000 - 3.4900 1.00 4796 148 0.1644 0.1886
REMARK 3 3 3.4900 - 3.0500 1.00 4761 147 0.1992 0.2300
REMARK 3 4 3.0500 - 2.7700 1.00 4719 146 0.2178 0.2562
REMARK 3 5 2.7700 - 2.5700 1.00 4709 146 0.2519 0.3155
REMARK 3 6 2.5700 - 2.4200 1.00 4700 145 0.2972 0.3077
REMARK 3 7 2.4200 - 2.3000 1.00 4688 145 0.3341 0.3891
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) : 0.342
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.296
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 60.77
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 68.99
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 : 0.009 4615
REMARK 3 ANGLE : 0.966 6278
REMARK 3 CHIRALITY : 0.055 689
REMARK 3 PLANARITY : 0.008 786
REMARK 3 DIHEDRAL : 13.860 687
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 4 THROUGH 235 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.8956 28.4565 27.3523
REMARK 3 T TENSOR
REMARK 3 T11: 0.5998 T22: 0.5541
REMARK 3 T33: 0.5558 T12: -0.0208
REMARK 3 T13: 0.0244 T23: 0.0365
REMARK 3 L TENSOR
REMARK 3 L11: 0.2278 L22: 0.4825
REMARK 3 L33: 1.0096 L12: 0.2444
REMARK 3 L13: -0.2701 L23: -0.1454
REMARK 3 S TENSOR
REMARK 3 S11: -0.0426 S12: 0.0669 S13: 0.0799
REMARK 3 S21: -0.1717 S22: 0.0961 S23: -0.0331
REMARK 3 S31: 0.0287 S32: 0.0315 S33: 0.0000
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 236 THROUGH 316 )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.4166 42.2852 31.8506
REMARK 3 T TENSOR
REMARK 3 T11: 0.6303 T22: 0.5948
REMARK 3 T33: 0.7090 T12: 0.0086
REMARK 3 T13: -0.0718 T23: 0.0784
REMARK 3 L TENSOR
REMARK 3 L11: 0.2432 L22: 0.0093
REMARK 3 L33: 0.4141 L12: -0.0985
REMARK 3 L13: -0.0744 L23: 0.0695
REMARK 3 S TENSOR
REMARK 3 S11: -0.0821 S12: 0.0467 S13: 0.1412
REMARK 3 S21: -0.0267 S22: 0.1125 S23: 0.0910
REMARK 3 S31: -0.1012 S32: -0.1863 S33: 0.0000
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 317 THROUGH 529 )
REMARK 3 ORIGIN FOR THE GROUP (A): 19.4303 31.8733 52.8111
REMARK 3 T TENSOR
REMARK 3 T11: 0.5144 T22: 0.5630
REMARK 3 T33: 0.5642 T12: -0.0152
REMARK 3 T13: 0.0141 T23: 0.0248
REMARK 3 L TENSOR
REMARK 3 L11: 0.2923 L22: 0.6717
REMARK 3 L33: 0.9350 L12: -0.0813
REMARK 3 L13: -0.4438 L23: 0.1582
REMARK 3 S TENSOR
REMARK 3 S11: 0.0282 S12: -0.1808 S13: 0.0389
REMARK 3 S21: 0.0591 S22: 0.0379 S23: -0.0001
REMARK 3 S31: -0.0546 S32: 0.0939 S33: 0.0001
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 7AWH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-NOV-20.
REMARK 100 THE DEPOSITION ID IS D_1292112201.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-JUL-20
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SOLEIL
REMARK 200 BEAMLINE : PROXIMA 1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.978564918041
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34407
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 48.850
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 26.70
REMARK 200 R MERGE (I) : 0.12690
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 19.1600
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 (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 27.90
REMARK 200 R MERGE FOR SHELL (I) : 2.50300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.420
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: 1P0I
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.35
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 295K
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 77.23500
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 77.23500
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 63.71000
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 77.23500
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 77.23500
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 63.71000
REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 77.23500
REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 77.23500
REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 63.71000
REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 77.23500
REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 77.23500
REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 63.71000
REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 77.23500
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 77.23500
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 63.71000
REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 77.23500
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 77.23500
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 63.71000
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 77.23500
REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 77.23500
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 63.71000
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 77.23500
REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 77.23500
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 63.71000
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 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 798 LIES ON A SPECIAL POSITION.
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 ASP A 3
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 -8.50 78.33
REMARK 500 ALA A 58 68.03 -107.33
REMARK 500 GLN A 67 148.96 -171.22
REMARK 500 LYS A 103 126.57 -33.84
REMARK 500 ASN A 106 59.40 -145.94
REMARK 500 ALA A 162 70.95 -162.53
REMARK 500 SER A 198 -125.82 63.63
REMARK 500 SER A 287 70.86 41.05
REMARK 500 ASP A 297 -72.27 -131.40
REMARK 500 ASP A 324 60.75 -116.13
REMARK 500 PHE A 398 -60.33 -134.25
REMARK 500 PRO A 480 49.37 -85.59
REMARK 500 ASN A 485 50.51 -110.19
REMARK 500 GLN A 486 48.69 36.42
REMARK 500 GLU A 506 -82.22 -79.41
REMARK 500
REMARK 500 REMARK: NULL
DBREF 7AWH A 1 529 UNP P06276 CHLE_HUMAN 29 557
SEQADV 7AWH GLN A 17 UNP P06276 ASN 45 ENGINEERED MUTATION
SEQADV 7AWH GLN A 455 UNP P06276 ASN 483 ENGINEERED MUTATION
SEQADV 7AWH GLN A 481 UNP P06276 ASN 509 ENGINEERED MUTATION
SEQADV 7AWH 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 FUC B 2 10
HET NAG C 1 14
HET NAG C 2 14
HET FUC C 3 10
HET NAG D 1 14
HET NAG D 2 14
HET FUC D 3 10
HET NAG A 601 14
HET NAG A 602 14
HET NAG A 603 14
HET MES A 604 12
HET SO4 A 605 5
HET SO4 A 606 5
HET SO4 A 607 5
HET GOL A 608 6
HET S8K A 609 36
HET GOL A 610 6
HET GOL A 611 6
HET SO4 A 612 5
HET NA A 613 1
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM FUC ALPHA-L-FUCOPYRANOSE
HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETNAM S8K ~{TERT}-BUTYL (3~{S})-3-[[2-[1-(PHENYLSULFONYL)INDOL-4-
HETNAM 2 S8K YL]OXYETHYLAMINO]METHYL]PIPERIDINE-1-CARBOXYLATE
HETNAM NA SODIUM 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 FUC ALPHA-L-FUCOSE; 6-DEOXY-ALPHA-L-GALACTOPYRANOSE; L-
HETSYN 2 FUC FUCOSE; FUCOSE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 NAG 8(C8 H15 N O6)
FORMUL 2 FUC 3(C6 H12 O5)
FORMUL 8 MES C6 H13 N O4 S
FORMUL 9 SO4 4(O4 S 2-)
FORMUL 12 GOL 3(C3 H8 O3)
FORMUL 13 S8K C27 H35 N3 O5 S
FORMUL 17 NA NA 1+
FORMUL 18 HOH *98(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 VAL A 148 LEU A 154 1 7
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 PRO A 211 PHE A 217 5 7
HELIX 10 AB1 SER A 235 THR A 250 1 16
HELIX 11 AB2 ASN A 256 ASN A 266 1 11
HELIX 12 AB3 ASP A 268 ALA A 277 1 10
HELIX 13 AB4 PHE A 278 VAL A 280 5 3
HELIX 14 AB5 MET A 302 LEU A 309 1 8
HELIX 15 AB6 GLY A 326 GLY A 333 5 8
HELIX 16 AB7 THR A 346 PHE A 358 1 13
HELIX 17 AB8 SER A 362 THR A 374 1 13
HELIX 18 AB9 GLU A 383 PHE A 398 1 16
HELIX 19 AC1 PHE A 398 TRP A 412 1 15
HELIX 20 AC2 PRO A 431 GLY A 435 5 5
HELIX 21 AC3 GLU A 441 GLY A 447 1 7
HELIX 22 AC4 LEU A 448 GLN A 455 5 8
HELIX 23 AC5 THR A 457 GLY A 478 1 22
HELIX 24 AC6 ARG A 515 PHE A 525 1 11
HELIX 25 AC7 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 GLY A 11 N THR A 8
SHEET 3 AA1 3 ILE A 55 ASN A 57 1 O TRP A 56 N LYS A 12
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 ALA A 101 -1 O VAL A 97 N PHE A 28
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 THR A 193 N VAL A 109
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
SHEET 1 AA3 2 SER A 64 CYS A 65 0
SHEET 2 AA3 2 LEU A 88 SER A 89 1 O SER A 89 N SER A 64
SSBOND 1 CYS A 65 CYS A 92 1555 1555 2.05
SSBOND 2 CYS A 252 CYS A 263 1555 1555 2.05
SSBOND 3 CYS A 400 CYS A 519 1555 1555 2.06
LINK ND2 ASN A 57 C1 NAG B 1 1555 1555 1.46
LINK ND2 ASN A 106 C1 NAG A 601 1555 1555 1.46
LINK ND2 ASN A 241 C1 NAG D 1 1555 1555 1.45
LINK ND2 ASN A 256 C1 NAG A 602 1555 1555 1.45
LINK ND2 ASN A 341 C1 NAG C 1 1555 1555 1.45
LINK ND2 ASN A 485 C1 NAG A 603 1555 1555 1.44
LINK O6 NAG B 1 C1 FUC B 2 1555 1555 1.43
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.44
LINK O6 NAG C 1 C1 FUC C 3 1555 1555 1.45
LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.46
LINK O6 NAG D 1 C1 FUC D 3 1555 1555 1.45
CISPEP 1 ALA A 101 PRO A 102 0 5.35
CRYST1 154.470 154.470 127.420 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 0.006474 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006474 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007848 0.00000
TER 4264 VAL A 529
MASTER 336 0 21 25 16 0 0 6 4522 1 240 41
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