| content |
HEADER HYDROLASE 25-JAN-10 3LII
TITLE RECOMBINANT HUMAN ACETYLCHOLINESTERASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 35-574;
COMPND 5 SYNONYM: ACHE;
COMPND 6 EC: 3.1.1.7;
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: ACHE;
SOURCE 6 EXPRESSION_SYSTEM: DROSOPHILA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7215
KEYWDS RECOMBINANT HUMAN ACETYLCHOLINESTERASE, ALTERNATIVE
KEYWDS 2 SPLICING, BLOOD GROUP ANTIGEN, CELL JUNCTION, CELL
KEYWDS 3 MEMBRANE, DISULFIDE BOND, GLYCOPROTEIN, GPI-ANCHOR,
KEYWDS 4 HYDROLASE, LIPOPROTEIN, MEMBRANE, NEUROTRANSMITTER
KEYWDS 5 DEGRADATION, NUCLEUS, POLYMORPHISM, SECRETED, SERINE
KEYWDS 6 ESTERASE, SYNAPSE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.DVIR,T.ROSENBERRY,M.HAREL,I.SILMAN,J.SUSSMAN
REVDAT 1 16-MAR-10 3LII 0
JRNL AUTH H.DVIR,T.ROSENBERRY,M.HAREL,I.SILMAN,J.SUSSMAN
JRNL TITL ACETYLCHOLINESTERASE: FROM 3D STRUCTURE TO FUNCTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 3.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.05
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 45505
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.179
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.220
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2470
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.28
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3233
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK 3 BIN R VALUE (WORKING SET) : 0.3030
REMARK 3 BIN FREE R VALUE SET COUNT : 167
REMARK 3 BIN FREE R VALUE : 0.3760
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8293
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 101
REMARK 3 SOLVENT ATOMS : 54
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 76.54
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -4.18000
REMARK 3 B22 (A**2) : -4.18000
REMARK 3 B33 (A**2) : 6.27000
REMARK 3 B12 (A**2) : -2.09000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.488
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.308
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.231
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.813
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.950
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.921
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8646 ; 0.024 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11832 ; 2.368 ; 1.969
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1061 ; 8.531 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 393 ;35.726 ;22.621
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1221 ;23.478 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 75 ;24.406 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1265 ; 0.148 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6807 ; 0.012 ; 0.022
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 5320 ; 1.070 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8562 ; 2.101 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3326 ; 2.774 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3270 ; 4.924 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 3LII COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-JAN-10.
REMARK 100 THE RCSB ID CODE IS RCSB057319.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-NOV-00
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.8
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) : 0.93
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47979
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.200
REMARK 200 RESOLUTION RANGE LOW (A) : 31.100
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 5.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08300
REMARK 200 FOR THE DATA SET : 15.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.31
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.47500
REMARK 200 FOR SHELL : 3.500
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: PDB ENTRY 1B41
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 80.31
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 6.25
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.4M LITHIUM SULFATE, 0.1M HEPES,
REMARK 280 PH 6.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 38.42333
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 76.84667
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 57.63500
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 96.05833
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 19.21167
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: 7170 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 39500 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -299.0 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 4
REMARK 465 PRO A 259
REMARK 465 GLY A 260
REMARK 465 GLY A 261
REMARK 465 THR A 262
REMARK 465 GLY A 263
REMARK 465 GLU B 4
REMARK 465 PRO B 259
REMARK 465 GLY B 260
REMARK 465 GLY B 261
REMARK 465 THR B 262
REMARK 465 GLY B 263
REMARK 465 GLY B 264
REMARK 465 ARG B 493
REMARK 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 NH2 ARG B 417 O HOH B 649 1.91
REMARK 500 NH1 ARG B 417 O HOH B 649 2.02
REMARK 500 NH1 ARG A 224 O ALA A 484 2.09
REMARK 500 O ARG B 46 NH1 ARG B 274 2.17
REMARK 500 ND2 ASN B 350 O5 NAG B 1003 2.18
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 GLU A 51 CG GLU A 51 CD 0.096
REMARK 500 CYS A 529 CB CYS A 529 SG 0.176
REMARK 500 GLU B 81 CG GLU B 81 CD 0.092
REMARK 500 TRP B 286 CB TRP B 286 CG -0.109
REMARK 500 GLU B 376 CB GLU B 376 CG 0.192
REMARK 500 GLU B 376 CG GLU B 376 CD 0.169
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 ARG A 152 NE - CZ - NH1 ANGL. DEV. = -4.1 DEGREES
REMARK 500 ASP A 193 CB - CG - OD1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 CYS A 257 CA - CB - SG ANGL. DEV. = 9.0 DEGREES
REMARK 500 PRO A 290 C - N - CA ANGL. DEV. = 9.3 DEGREES
REMARK 500 LEU A 386 CA - CB - CG ANGL. DEV. = -15.6 DEGREES
REMARK 500 LYS A 470 CD - CE - NZ ANGL. DEV. = -14.0 DEGREES
REMARK 500 ARG A 475 NE - CZ - NH1 ANGL. DEV. = -4.2 DEGREES
REMARK 500 LEU B 92 CB - CG - CD1 ANGL. DEV. = -11.1 DEGREES
REMARK 500 LEU B 130 CB - CG - CD1 ANGL. DEV. = -11.8 DEGREES
REMARK 500 MET B 149 CG - SD - CE ANGL. DEV. = 10.2 DEGREES
REMARK 500 ARG B 152 NE - CZ - NH1 ANGL. DEV. = -3.5 DEGREES
REMARK 500 VAL B 370 N - CA - C ANGL. DEV. = -17.2 DEGREES
REMARK 500 ARG B 417 NE - CZ - NH1 ANGL. DEV. = 4.0 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 ALA A 6 6.09 43.61
REMARK 500 PRO A 25 -46.55 -28.13
REMARK 500 PHE A 47 -7.40 78.28
REMARK 500 ASP A 61 99.51 -52.88
REMARK 500 ALA A 62 35.78 -98.06
REMARK 500 GLN A 66 -171.57 -69.90
REMARK 500 CYS A 96 -10.40 -146.28
REMARK 500 LEU A 97 78.86 -69.33
REMARK 500 ARG A 107 112.56 -38.98
REMARK 500 PRO A 111 80.15 -65.84
REMARK 500 GLU A 142 3.27 -154.30
REMARK 500 GLU A 185 3.14 -61.76
REMARK 500 ASN A 186 -15.99 -154.16
REMARK 500 ALA A 188 -64.41 -17.23
REMARK 500 ALA A 189 5.77 -64.96
REMARK 500 THR A 195 -148.57 -90.51
REMARK 500 SER A 196 78.83 5.35
REMARK 500 SER A 203 -117.09 35.29
REMARK 500 MET A 241 -41.78 -29.81
REMARK 500 CYS A 257 145.52 115.65
REMARK 500 ASN A 265 -150.56 -80.73
REMARK 500 ASP A 266 -90.55 52.18
REMARK 500 THR A 267 -45.39 -24.48
REMARK 500 ASP A 306 -81.44 -89.87
REMARK 500 SER A 309 -37.22 -36.69
REMARK 500 ASN A 317 -76.06 -51.71
REMARK 500 TYR A 341 36.05 -95.38
REMARK 500 ASN A 350 -149.36 -102.94
REMARK 500 SER A 352 46.48 27.93
REMARK 500 GLN A 369 81.91 43.11
REMARK 500 ASP A 404 -72.64 -46.97
REMARK 500 VAL A 407 -80.54 -114.76
REMARK 500 ASN A 464 73.22 -63.65
REMARK 500 ASP A 488 125.08 -174.96
REMARK 500 ASP A 494 66.73 170.32
REMARK 500 THR A 504 126.99 -171.15
REMARK 500 ASP A 514 -158.91 -151.30
REMARK 500 ARG A 525 59.54 38.18
REMARK 500 ALA B 6 -59.17 49.51
REMARK 500 ARG B 13 -7.89 -51.69
REMARK 500 PRO B 25 -8.40 -37.97
REMARK 500 PHE B 47 -0.94 85.03
REMARK 500 ALA B 62 40.33 -144.38
REMARK 500 TYR B 72 143.82 -37.05
REMARK 500 THR B 75 30.74 -81.63
REMARK 500 GLU B 81 -76.22 -46.89
REMARK 500 GLU B 91 137.69 -33.72
REMARK 500 ARG B 107 125.17 -38.13
REMARK 500 TYR B 133 49.25 -97.89
REMARK 500 ARG B 136 -68.85 -20.08
REMARK 500
REMARK 500 THIS ENTRY HAS 89 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 TYR A 503 THR A 504 -149.13
REMARK 500 LEU B 22 LYS B 23 -146.90
REMARK 500 ASN B 490 GLU B 491 -147.25
REMARK 500 GLU B 491 PRO B 492 -146.20
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 VAL A 114 24.8 L L OUTSIDE RANGE
REMARK 500 ASN A 350 24.4 L L OUTSIDE RANGE
REMARK 500 GLN A 369 21.3 L L OUTSIDE RANGE
REMARK 500 ASP B 74 24.6 L L OUTSIDE RANGE
REMARK 500 PHE B 158 24.6 L L OUTSIDE RANGE
REMARK 500 GLN B 369 21.2 L L OUTSIDE RANGE
REMARK 500 VAL B 370 46.1 L L OUTSIDE RANGE
REMARK 500 ASN B 490 23.7 L L OUTSIDE RANGE
REMARK 500 GLU B 491 24.9 L L OUTSIDE RANGE
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 NAG A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1005
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1010
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1012
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1011
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1013
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1014
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1015
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1016
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1017
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 1004
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1F8U RELATED DB: PDB
REMARK 900 MUTANT E202Q OF HUMAN ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 1B41 RELATED DB: PDB
REMARK 900 RECOMBINANT NATIVE HUMAN ACETYLCHOLINESTERASE COMPLEXED
REMARK 900 WITH SNAKE-VENOM TOXIN FASCICULIN-II
DBREF 3LII A 4 543 UNP P22303 ACES_HUMAN 35 574
DBREF 3LII B 4 543 UNP P22303 ACES_HUMAN 35 574
SEQRES 1 A 540 GLU ASP ALA GLU LEU LEU VAL THR VAL ARG GLY GLY ARG
SEQRES 2 A 540 LEU ARG GLY ILE ARG LEU LYS THR PRO GLY GLY PRO VAL
SEQRES 3 A 540 SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO MET
SEQRES 4 A 540 GLY PRO ARG ARG PHE LEU PRO PRO GLU PRO LYS GLN PRO
SEQRES 5 A 540 TRP SER GLY VAL VAL ASP ALA THR THR PHE GLN SER VAL
SEQRES 6 A 540 CYS TYR GLN TYR VAL ASP THR LEU TYR PRO GLY PHE GLU
SEQRES 7 A 540 GLY THR GLU MET TRP ASN PRO ASN ARG GLU LEU SER GLU
SEQRES 8 A 540 ASP CYS LEU TYR LEU ASN VAL TRP THR PRO TYR PRO ARG
SEQRES 9 A 540 PRO THR SER PRO THR PRO VAL LEU VAL TRP ILE TYR GLY
SEQRES 10 A 540 GLY GLY PHE TYR SER GLY ALA SER SER LEU ASP VAL TYR
SEQRES 11 A 540 ASP GLY ARG PHE LEU VAL GLN ALA GLU ARG THR VAL LEU
SEQRES 12 A 540 VAL SER MET ASN TYR ARG VAL GLY ALA PHE GLY PHE LEU
SEQRES 13 A 540 ALA LEU PRO GLY SER ARG GLU ALA PRO GLY ASN VAL GLY
SEQRES 14 A 540 LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP VAL GLN GLU
SEQRES 15 A 540 ASN VAL ALA ALA PHE GLY GLY ASP PRO THR SER VAL THR
SEQRES 16 A 540 LEU PHE GLY GLU SER ALA GLY ALA ALA SER VAL GLY MET
SEQRES 17 A 540 HIS LEU LEU SER PRO PRO SER ARG GLY LEU PHE HIS ARG
SEQRES 18 A 540 ALA VAL LEU GLN SER GLY ALA PRO ASN GLY PRO TRP ALA
SEQRES 19 A 540 THR VAL GLY MET GLY GLU ALA ARG ARG ARG ALA THR GLN
SEQRES 20 A 540 LEU ALA HIS LEU VAL GLY CYS PRO PRO GLY GLY THR GLY
SEQRES 21 A 540 GLY ASN ASP THR GLU LEU VAL ALA CYS LEU ARG THR ARG
SEQRES 22 A 540 PRO ALA GLN VAL LEU VAL ASN HIS GLU TRP HIS VAL LEU
SEQRES 23 A 540 PRO GLN GLU SER VAL PHE ARG PHE SER PHE VAL PRO VAL
SEQRES 24 A 540 VAL ASP GLY ASP PHE LEU SER ASP THR PRO GLU ALA LEU
SEQRES 25 A 540 ILE ASN ALA GLY ASP PHE HIS GLY LEU GLN VAL LEU VAL
SEQRES 26 A 540 GLY VAL VAL LYS ASP GLU GLY SER TYR PHE LEU VAL TYR
SEQRES 27 A 540 GLY ALA PRO GLY PHE SER LYS ASP ASN GLU SER LEU ILE
SEQRES 28 A 540 SER ARG ALA GLU PHE LEU ALA GLY VAL ARG VAL GLY VAL
SEQRES 29 A 540 PRO GLN VAL SER ASP LEU ALA ALA GLU ALA VAL VAL LEU
SEQRES 30 A 540 HIS TYR THR ASP TRP LEU HIS PRO GLU ASP PRO ALA ARG
SEQRES 31 A 540 LEU ARG GLU ALA LEU SER ASP VAL VAL GLY ASP HIS ASN
SEQRES 32 A 540 VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY ARG LEU ALA
SEQRES 33 A 540 ALA GLN GLY ALA ARG VAL TYR ALA TYR VAL PHE GLU HIS
SEQRES 34 A 540 ARG ALA SER THR LEU SER TRP PRO LEU TRP MET GLY VAL
SEQRES 35 A 540 PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE GLY ILE PRO
SEQRES 36 A 540 LEU ASP PRO SER ARG ASN TYR THR ALA GLU GLU LYS ILE
SEQRES 37 A 540 PHE ALA GLN ARG LEU MET ARG TYR TRP ALA ASN PHE ALA
SEQRES 38 A 540 ARG THR GLY ASP PRO ASN GLU PRO ARG ASP PRO LYS ALA
SEQRES 39 A 540 PRO GLN TRP PRO PRO TYR THR ALA GLY ALA GLN GLN TYR
SEQRES 40 A 540 VAL SER LEU ASP LEU ARG PRO LEU GLU VAL ARG ARG GLY
SEQRES 41 A 540 LEU ARG ALA GLN ALA CYS ALA PHE TRP ASN ARG PHE LEU
SEQRES 42 A 540 PRO LYS LEU LEU SER ALA THR
SEQRES 1 B 540 GLU ASP ALA GLU LEU LEU VAL THR VAL ARG GLY GLY ARG
SEQRES 2 B 540 LEU ARG GLY ILE ARG LEU LYS THR PRO GLY GLY PRO VAL
SEQRES 3 B 540 SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO MET
SEQRES 4 B 540 GLY PRO ARG ARG PHE LEU PRO PRO GLU PRO LYS GLN PRO
SEQRES 5 B 540 TRP SER GLY VAL VAL ASP ALA THR THR PHE GLN SER VAL
SEQRES 6 B 540 CYS TYR GLN TYR VAL ASP THR LEU TYR PRO GLY PHE GLU
SEQRES 7 B 540 GLY THR GLU MET TRP ASN PRO ASN ARG GLU LEU SER GLU
SEQRES 8 B 540 ASP CYS LEU TYR LEU ASN VAL TRP THR PRO TYR PRO ARG
SEQRES 9 B 540 PRO THR SER PRO THR PRO VAL LEU VAL TRP ILE TYR GLY
SEQRES 10 B 540 GLY GLY PHE TYR SER GLY ALA SER SER LEU ASP VAL TYR
SEQRES 11 B 540 ASP GLY ARG PHE LEU VAL GLN ALA GLU ARG THR VAL LEU
SEQRES 12 B 540 VAL SER MET ASN TYR ARG VAL GLY ALA PHE GLY PHE LEU
SEQRES 13 B 540 ALA LEU PRO GLY SER ARG GLU ALA PRO GLY ASN VAL GLY
SEQRES 14 B 540 LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP VAL GLN GLU
SEQRES 15 B 540 ASN VAL ALA ALA PHE GLY GLY ASP PRO THR SER VAL THR
SEQRES 16 B 540 LEU PHE GLY GLU SER ALA GLY ALA ALA SER VAL GLY MET
SEQRES 17 B 540 HIS LEU LEU SER PRO PRO SER ARG GLY LEU PHE HIS ARG
SEQRES 18 B 540 ALA VAL LEU GLN SER GLY ALA PRO ASN GLY PRO TRP ALA
SEQRES 19 B 540 THR VAL GLY MET GLY GLU ALA ARG ARG ARG ALA THR GLN
SEQRES 20 B 540 LEU ALA HIS LEU VAL GLY CYS PRO PRO GLY GLY THR GLY
SEQRES 21 B 540 GLY ASN ASP THR GLU LEU VAL ALA CYS LEU ARG THR ARG
SEQRES 22 B 540 PRO ALA GLN VAL LEU VAL ASN HIS GLU TRP HIS VAL LEU
SEQRES 23 B 540 PRO GLN GLU SER VAL PHE ARG PHE SER PHE VAL PRO VAL
SEQRES 24 B 540 VAL ASP GLY ASP PHE LEU SER ASP THR PRO GLU ALA LEU
SEQRES 25 B 540 ILE ASN ALA GLY ASP PHE HIS GLY LEU GLN VAL LEU VAL
SEQRES 26 B 540 GLY VAL VAL LYS ASP GLU GLY SER TYR PHE LEU VAL TYR
SEQRES 27 B 540 GLY ALA PRO GLY PHE SER LYS ASP ASN GLU SER LEU ILE
SEQRES 28 B 540 SER ARG ALA GLU PHE LEU ALA GLY VAL ARG VAL GLY VAL
SEQRES 29 B 540 PRO GLN VAL SER ASP LEU ALA ALA GLU ALA VAL VAL LEU
SEQRES 30 B 540 HIS TYR THR ASP TRP LEU HIS PRO GLU ASP PRO ALA ARG
SEQRES 31 B 540 LEU ARG GLU ALA LEU SER ASP VAL VAL GLY ASP HIS ASN
SEQRES 32 B 540 VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY ARG LEU ALA
SEQRES 33 B 540 ALA GLN GLY ALA ARG VAL TYR ALA TYR VAL PHE GLU HIS
SEQRES 34 B 540 ARG ALA SER THR LEU SER TRP PRO LEU TRP MET GLY VAL
SEQRES 35 B 540 PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE GLY ILE PRO
SEQRES 36 B 540 LEU ASP PRO SER ARG ASN TYR THR ALA GLU GLU LYS ILE
SEQRES 37 B 540 PHE ALA GLN ARG LEU MET ARG TYR TRP ALA ASN PHE ALA
SEQRES 38 B 540 ARG THR GLY ASP PRO ASN GLU PRO ARG ASP PRO LYS ALA
SEQRES 39 B 540 PRO GLN TRP PRO PRO TYR THR ALA GLY ALA GLN GLN TYR
SEQRES 40 B 540 VAL SER LEU ASP LEU ARG PRO LEU GLU VAL ARG ARG GLY
SEQRES 41 B 540 LEU ARG ALA GLN ALA CYS ALA PHE TRP ASN ARG PHE LEU
SEQRES 42 B 540 PRO LYS LEU LEU SER ALA THR
MODRES 3LII ASN A 350 ASN GLYCOSYLATION SITE
MODRES 3LII ASN B 350 ASN GLYCOSYLATION SITE
HET NAG A1001 14
HET NAG A1002 14
HET SO4 A1005 5
HET SO4 A1010 5
HET SO4 A1012 5
HET SO4 A1011 5
HET SO4 A1013 5
HET SO4 B1014 5
HET SO4 B1015 5
HET SO4 B1016 5
HET SO4 A1017 5
HET NAG B1003 14
HET NAG B1004 14
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM SO4 SULFATE ION
FORMUL 3 NAG 4(C8 H15 N O6)
FORMUL 4 SO4 9(O4 S 2-)
FORMUL 14 HOH *54(H2 O)
HELIX 1 1 MET A 42 ARG A 46 5 5
HELIX 2 2 PHE A 80 MET A 85 1 6
HELIX 3 3 LEU A 130 ASP A 134 5 5
HELIX 4 4 GLY A 135 ALA A 141 1 7
HELIX 5 5 GLY A 154 LEU A 159 1 6
HELIX 6 6 ASN A 170 ALA A 188 1 19
HELIX 7 7 ALA A 189 GLY A 191 5 3
HELIX 8 8 SER A 203 SER A 215 1 13
HELIX 9 9 SER A 215 GLY A 220 1 6
HELIX 10 10 MET A 241 VAL A 255 1 15
HELIX 11 11 ASP A 266 CYS A 272 1 7
HELIX 12 12 PRO A 277 GLU A 285 1 9
HELIX 13 13 TRP A 286 LEU A 289 5 4
HELIX 14 14 THR A 311 ALA A 318 1 8
HELIX 15 15 GLY A 335 VAL A 340 1 6
HELIX 16 16 SER A 355 VAL A 367 1 13
HELIX 17 17 SER A 371 THR A 383 1 13
HELIX 18 18 ASP A 390 VAL A 407 1 18
HELIX 19 19 VAL A 407 ALA A 420 1 14
HELIX 20 20 PRO A 440 GLY A 444 5 5
HELIX 21 21 GLU A 450 PHE A 455 1 6
HELIX 22 22 THR A 466 GLY A 487 1 22
HELIX 23 23 ARG A 525 ARG A 534 1 10
HELIX 24 24 ARG A 534 SER A 541 1 8
HELIX 25 25 MET B 42 ARG B 46 5 5
HELIX 26 26 PHE B 80 MET B 85 1 6
HELIX 27 27 LEU B 130 TYR B 133 5 4
HELIX 28 28 ASP B 134 ARG B 143 1 10
HELIX 29 29 VAL B 153 LEU B 159 1 7
HELIX 30 30 ASN B 170 ALA B 188 1 19
HELIX 31 31 SER B 203 SER B 215 1 13
HELIX 32 32 SER B 215 GLY B 220 1 6
HELIX 33 33 MET B 241 LEU B 254 1 14
HELIX 34 34 ASP B 266 THR B 275 1 10
HELIX 35 35 PRO B 277 GLU B 285 1 9
HELIX 36 36 TRP B 286 VAL B 288 5 3
HELIX 37 37 THR B 311 ALA B 318 1 8
HELIX 38 38 GLY B 335 LEU B 339 5 5
HELIX 39 39 SER B 355 VAL B 367 1 13
HELIX 40 40 SER B 371 THR B 383 1 13
HELIX 41 41 ASP B 390 VAL B 407 1 18
HELIX 42 42 VAL B 407 ALA B 420 1 14
HELIX 43 43 PRO B 440 GLY B 444 5 5
HELIX 44 44 GLU B 450 PHE B 455 1 6
HELIX 45 45 GLY B 456 ASP B 460 5 5
HELIX 46 46 GLU B 468 GLY B 487 1 20
HELIX 47 47 ARG B 525 ARG B 534 1 10
HELIX 48 48 ARG B 534 SER B 541 1 8
SHEET 1 A 3 LEU A 9 VAL A 12 0
SHEET 2 A 3 GLY A 15 ARG A 18 -1 O GLY A 15 N VAL A 12
SHEET 3 A 3 VAL A 59 ASP A 61 1 O VAL A 60 N ARG A 16
SHEET 1 B 9 ILE A 20 THR A 24 0
SHEET 2 B 9 GLY A 27 PRO A 36 -1 O ALA A 31 N ILE A 20
SHEET 3 B 9 TYR A 98 PRO A 104 -1 O VAL A 101 N PHE A 32
SHEET 4 B 9 VAL A 145 MET A 149 -1 O SER A 148 N ASN A 100
SHEET 5 B 9 VAL A 114 ILE A 118 1 N LEU A 115 O VAL A 145
SHEET 6 B 9 VAL A 197 GLU A 202 1 O THR A 198 N VAL A 114
SHEET 7 B 9 ARG A 224 GLN A 228 1 O VAL A 226 N LEU A 199
SHEET 8 B 9 GLN A 325 VAL A 331 1 O LEU A 327 N ALA A 225
SHEET 9 B 9 ARG A 424 PHE A 430 1 O PHE A 430 N VAL A 330
SHEET 1 C 2 VAL A 68 CYS A 69 0
SHEET 2 C 2 LEU A 92 SER A 93 1 O SER A 93 N VAL A 68
SHEET 1 D 2 VAL A 239 GLY A 240 0
SHEET 2 D 2 VAL A 302 VAL A 303 1 O VAL A 303 N VAL A 239
SHEET 1 E 2 GLN A 509 SER A 512 0
SHEET 2 E 2 GLU A 519 ARG A 522 -1 O ARG A 521 N TYR A 510
SHEET 1 F 3 LEU B 9 VAL B 12 0
SHEET 2 F 3 GLY B 15 ARG B 18 -1 O GLY B 15 N VAL B 12
SHEET 3 F 3 VAL B 59 ASP B 61 1 O VAL B 60 N ARG B 18
SHEET 1 G11 ILE B 20 THR B 24 0
SHEET 2 G11 GLY B 27 PRO B 36 -1 O VAL B 29 N LEU B 22
SHEET 3 G11 TYR B 98 PRO B 104 -1 O VAL B 101 N PHE B 32
SHEET 4 G11 VAL B 145 MET B 149 -1 O SER B 148 N ASN B 100
SHEET 5 G11 THR B 112 ILE B 118 1 N TRP B 117 O VAL B 147
SHEET 6 G11 GLY B 192 GLU B 202 1 O THR B 198 N VAL B 114
SHEET 7 G11 ARG B 224 GLN B 228 1 O VAL B 226 N LEU B 199
SHEET 8 G11 GLN B 325 VAL B 331 1 O LEU B 327 N LEU B 227
SHEET 9 G11 ARG B 424 PHE B 430 1 O TYR B 426 N VAL B 326
SHEET 10 G11 GLN B 509 LEU B 513 1 O VAL B 511 N VAL B 429
SHEET 11 G11 VAL B 520 ARG B 522 -1 O ARG B 521 N TYR B 510
SHEET 1 H 2 VAL B 68 CYS B 69 0
SHEET 2 H 2 LEU B 92 SER B 93 1 O SER B 93 N VAL B 68
SHEET 1 I 2 VAL B 239 GLY B 240 0
SHEET 2 I 2 VAL B 302 VAL B 303 1 O VAL B 303 N VAL B 239
SSBOND 1 CYS A 69 CYS A 96 1555 1555 2.08
SSBOND 2 CYS A 409 CYS A 529 1555 1555 2.11
SSBOND 3 CYS B 69 CYS B 96 1555 1555 2.11
SSBOND 4 CYS B 409 CYS B 529 1555 1555 2.10
LINK ND2 ASN A 350 C1 NAG A1001 1555 1555 1.45
LINK ND2 ASN B 350 C1 NAG B1003 1555 1555 1.45
LINK O4 NAG A1001 C1 NAG A1002 1555 1555 1.48
LINK O4 NAG B1003 C1 NAG B1004 1555 1555 1.49
CISPEP 1 CYS A 257 PRO A 258 0 6.15
CISPEP 2 TYR B 105 PRO B 106 0 -2.71
CISPEP 3 CYS B 257 PRO B 258 0 8.04
SITE 1 AC1 3 GLY A 345 ASN A 350 NAG A1002
SITE 1 AC2 2 GLY A 345 NAG A1001
SITE 1 AC3 4 ARG A 525 ALA A 526 GLN A 527 ALA A 528
SITE 1 AC4 3 GLN A 413 ARG A 417 HOH A 608
SITE 1 AC5 4 TRP A 86 GLY A 121 SER A 203 HIS A 447
SITE 1 AC6 4 THR A 504 GLY A 506 ALA A 507 HOH A 601
SITE 1 AC7 4 GLY A 240 MET A 241 GLY A 242 HOH A 624
SITE 1 AC8 3 ARG B 356 LEU B 360 TRP B 385
SITE 1 AC9 3 THR B 504 GLY B 506 ALA B 507
SITE 1 BC1 5 ARG B 525 ALA B 526 GLN B 527 ALA B 528
SITE 2 BC1 5 HOH B 616
SITE 1 BC2 3 ARG A 356 LEU A 360 ARG B 534
SITE 1 BC3 2 ASN B 350 NAG B1004
SITE 1 BC4 1 NAG B1003
CRYST1 210.900 210.900 115.270 90.00 90.00 120.00 P 61 12
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.004742 0.002738 0.000000 0.00000
SCALE2 0.000000 0.005475 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008675 0.00000
TER 4155 THR A 543
TER 8295 THR B 543
MASTER 501 0 13 48 36 0 14 6 8448 2 111 84
END |