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HEADER HYDROLASE/TOXIN 21-JAN-02 1KU6
TITLE FASCICULIN 2-MOUSE ACETYLCHOLINESTERASE COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ACHE;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: FASCICULIN 2;
COMPND 8 CHAIN: B;
COMPND 9 SYNONYM: FAS-II
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGAN: BRAIN;
SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 7 EXPRESSION_SYSTEM_CELL_LINE: HEK293;
SOURCE 8 EXPRESSION_SYSTEM_ORGAN: KIDNEY;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: LAMBDA-ZAP AND LAMBDA-FIX CDNA;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: DENDROASPIS ANGUSTICEPS;
SOURCE 12 ORGANISM_COMMON: EASTERN GREEN MAMBA;
SOURCE 13 SECRETION: VENOM
KEYWDS HYDROLASE, SERINE ESTERASE, SYNAPSE, VENOM, TOXIN
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.BOURNE,W.BURMEISTER,P.TAYLOR,P.MARCHOT
REVDAT 1 23-DEC-03 1KU6 0
JRNL AUTH Y.BOURNE,W.BURMEISTER,P.TAYLOR,P.MARCHOT
JRNL TITL ACETYLCHOLINESTERASE INHIBITION BY FASCICULIN
JRNL TITL 2 REVISITED
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.66
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 3747291.810
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 84.4
REMARK 3 NUMBER OF REFLECTIONS : 27361
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 SET) : 0.226
REMARK 3 FREE R VALUE : 0.273
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.900
REMARK 3 FREE R VALUE TEST SET COUNT : 803
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.010
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.66
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 51.40
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2617
REMARK 3 BIN R VALUE (WORKING SET) : 0.3230
REMARK 3 BIN FREE R VALUE : 0.3630
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 2.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 77
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.041
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4616
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 18
REMARK 3 SOLVENT ATOMS : 190
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 19.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 55.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 19.95000
REMARK 3 B22 (A**2) : 19.95000
REMARK 3 B33 (A**2) : -39.90000
REMARK 3 B12 (A**2) : 4.30000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.35
REMARK 3 ESD FROM SIGMAA (A) : 0.43
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.43
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.46
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.011
REMARK 3 BOND ANGLES (DEGREES) : 1.80
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.90
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.35
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.300 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.220 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.880 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.850 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.28
REMARK 3 BSOL : 37.60
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : EDO.PAR
REMARK 3 PARAMETER FILE 4 : CARBOHYDRATE.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER_REP.TOP
REMARK 3 TOPOLOGY FILE 3 : EDO.TOP
REMARK 3 TOPOLOGY FILE 4 : CARBOHYDRATE.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1KU6 COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-FEB-2002.
REMARK 100 THE RCSB ID CODE IS RCSB015349.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-OCT-1998
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-EH3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.947
REMARK 200 MONOCHROMATOR : MIRROR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : FILM
REMARK 200 DETECTOR MANUFACTURER : LARGE IMAGE PLATE SCANNER
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27485
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 84.5
REMARK 200 DATA REDUNDANCY : 5.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07400
REMARK 200 FOR THE DATA SET : 8.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG 2K, 50 MM NAAC, PH 6.5,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,2/3+Z
REMARK 290 3555 -X+Y,-X,1/3+Z
REMARK 290 4555 -X,-Y,1/2+Z
REMARK 290 5555 Y,-X+Y,1/6+Z
REMARK 290 6555 X-Y,X,5/6+Z
REMARK 290 7555 Y,X,2/3-Z
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,1/3-Z
REMARK 290 10555 -Y,-X,1/6-Z
REMARK 290 11555 -X+Y,Y,1/2-Z
REMARK 290 12555 X,X-Y,5/6-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 -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 365.74667
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 182.87333
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 274.31000
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 91.43667
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 457.18333
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 365.74667
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 182.87333
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 91.43667
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 274.31000
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 457.18333
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 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 GLY A 2
REMARK 465 PRO A 259
REMARK 465 GLY A 260
REMARK 465 GLY A 261
REMARK 465 ALA A 262
REMARK 465 ALA A 542
REMARK 465 THR A 543
REMARK 465 ASP A 544
REMARK 465 THR A 545
REMARK 465 LEU A 546
REMARK 465 ASP A 547
REMARK 465 GLU A 548
REMARK 465 ALA A 549
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 ARG A 3 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 165 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 493 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 496 CG CD CE NZ
REMARK 470 LYS B 51 CG CD CE NZ
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 O HOH 732 O HOH 732 8675 1.82
REMARK 500 O HOH 738 O HOH 738 10665 1.83
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),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 PRO A 28 CB PRO A 28 CG 0.066
REMARK 500 MET A 195 SD MET A 195 CE 0.099
REMARK 500 PRO A 258 CB PRO A 258 CG 0.071
REMARK 500 MET A 398 SD MET A 398 CE -0.084
REMARK 500 PRO A 498 CB PRO A 498 CG 0.125
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: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 VAL A 145 N - CA - C ANGL. DEV. =-12.1 DEGREES
REMARK 500 PHE A 158 N - CA - C ANGL. DEV. = 11.9 DEGREES
REMARK 500 LEU A 161 N - CA - C ANGL. DEV. =-12.3 DEGREES
REMARK 500 LEU A 327 N - CA - C ANGL. DEV. =-10.1 DEGREES
REMARK 500 ASP A 384 N - CA - C ANGL. DEV. =-10.7 DEGREES
REMARK 500 ASN A 490 N - CA - C ANGL. DEV. = 16.3 DEGREES
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 M RES CSSEQI PSI PHI
REMARK 500 ARG A 493 -100.44 -172.05
REMARK 525
REMARK 525 SOLVENT
REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED
REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE
REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL
REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH 874 DISTANCE = 5.36 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1MAH RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 REFERENCE: RACHINSKY ET AL. (1990) NEURON, 5:317-327.
REMARK 999 THE ENZYME CONTAINS THE ALTERNATIVE SPLICE OF EXON 5, AND
REMARK 999 IS TRUNCATED AT CODON POSITION 549.
REMARK 999
REMARK 999 IN CHAIN B, RESIDUE 47 IS ASN IN FASCICULIN II.
DBREF 1KU6 A 1 549 SWS P21836 ACES_MOUSE 32 580
DBREF 1KU6 B 1 61 SWS P01403 TXF7_DENAN 1 61
SEQADV 1KU6 ASN B 47 SWS P01403 TYR 47 SEE REMARK 999
SEQRES 1 A 549 GLU GLY ARG GLU ASP PRO GLN LEU LEU VAL ARG VAL ARG
SEQRES 2 A 549 GLY GLY GLN LEU ARG GLY ILE ARG LEU LYS ALA PRO GLY
SEQRES 3 A 549 GLY PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU
SEQRES 4 A 549 PRO PRO VAL GLY SER ARG ARG PHE MET PRO PRO GLU PRO
SEQRES 5 A 549 LYS ARG PRO TRP SER GLY VAL LEU ASP ALA THR THR PHE
SEQRES 6 A 549 GLN ASN VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO
SEQRES 7 A 549 GLY PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU
SEQRES 8 A 549 LEU SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO
SEQRES 9 A 549 TYR PRO ARG PRO ALA SER PRO THR PRO VAL LEU ILE TRP
SEQRES 10 A 549 ILE TYR GLY GLY GLY PHE TYR SER GLY ALA ALA SER LEU
SEQRES 11 A 549 ASP VAL TYR ASP GLY ARG PHE LEU ALA GLN VAL GLU GLY
SEQRES 12 A 549 ALA VAL LEU VAL SER MET ASN TYR ARG VAL GLY THR PHE
SEQRES 13 A 549 GLY PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY
SEQRES 14 A 549 ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP
SEQRES 15 A 549 VAL GLN GLU ASN ILE ALA ALA PHE GLY GLY ASP PRO MET
SEQRES 16 A 549 SER VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER
SEQRES 17 A 549 VAL GLY MET HIS ILE LEU SER LEU PRO SER ARG SER LEU
SEQRES 18 A 549 PHE HIS ARG ALA VAL LEU GLN SER GLY THR PRO ASN GLY
SEQRES 19 A 549 PRO TRP ALA THR VAL SER ALA GLY GLU ALA ARG ARG ARG
SEQRES 20 A 549 ALA THR LEU LEU ALA ARG LEU VAL GLY CYS PRO PRO GLY
SEQRES 21 A 549 GLY ALA GLY GLY ASN ASP THR GLU LEU ILE ALA CYS LEU
SEQRES 22 A 549 ARG THR ARG PRO ALA GLN ASP LEU VAL ASP HIS GLU TRP
SEQRES 23 A 549 HIS VAL LEU PRO GLN GLU SER ILE PHE ARG PHE SER PHE
SEQRES 24 A 549 VAL PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO
SEQRES 25 A 549 GLU ALA LEU ILE ASN THR GLY ASP PHE GLN ASP LEU GLN
SEQRES 26 A 549 VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE
SEQRES 27 A 549 LEU VAL TYR GLY VAL PRO GLY PHE SER LYS ASP ASN GLU
SEQRES 28 A 549 SER LEU ILE SER ARG ALA GLN PHE LEU ALA GLY VAL ARG
SEQRES 29 A 549 ILE GLY VAL PRO GLN ALA SER ASP LEU ALA ALA GLU ALA
SEQRES 30 A 549 VAL VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP
SEQRES 31 A 549 PRO THR HIS LEU ARG ASP ALA MET SER ALA VAL VAL GLY
SEQRES 32 A 549 ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY
SEQRES 33 A 549 ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR ILE
SEQRES 34 A 549 PHE GLU HIS ARG ALA SER THR LEU THR TRP PRO LEU TRP
SEQRES 35 A 549 MET GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE
SEQRES 36 A 549 GLY LEU PRO LEU ASP PRO SER LEU ASN TYR THR THR GLU
SEQRES 37 A 549 GLU ARG ILE PHE ALA GLN ARG LEU MET LYS TYR TRP THR
SEQRES 38 A 549 ASN PHE ALA ARG THR GLY ASP PRO ASN ASP PRO ARG ASP
SEQRES 39 A 549 SER LYS SER PRO GLN TRP PRO PRO TYR THR THR ALA ALA
SEQRES 40 A 549 GLN GLN TYR VAL SER LEU ASN LEU LYS PRO LEU GLU VAL
SEQRES 41 A 549 ARG ARG GLY LEU ARG ALA GLN THR CYS ALA PHE TRP ASN
SEQRES 42 A 549 ARG PHE LEU PRO LYS LEU LEU SER ALA THR ASP THR LEU
SEQRES 43 A 549 ASP GLU ALA
SEQRES 1 B 61 THR MET CYS TYR SER HIS THR THR THR SER ARG ALA ILE
SEQRES 2 B 61 LEU THR ASN CYS GLY GLU ASN SER CYS TYR ARG LYS SER
SEQRES 3 B 61 ARG ARG HIS PRO PRO LYS MET VAL LEU GLY ARG GLY CYS
SEQRES 4 B 61 GLY CYS PRO PRO GLY ASP ASP ASN LEU GLU VAL LYS CYS
SEQRES 5 B 61 CYS THR SER PRO ASP LYS CYS ASN TYR
MODRES 1KU6 ASN A 350 ASN GLYCOSYLATION SITE
HET NAG A1509 14
HET EDO 701 4
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM EDO 1,2-ETHANEDIOL
HETSYN NAG NAG
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 NAG C8 H15 N1 O6
FORMUL 4 EDO C2 H6 O2
FORMUL 5 HOH *190(H2 O1)
HELIX 1 1 VAL 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 GLY A 143 1 9
HELIX 5 5 VAL A 153 LEU A 159 1 7
HELIX 6 6 ASN A 170 ALA A 188 1 19
HELIX 7 7 SER A 203 SER A 215 1 13
HELIX 8 8 SER A 215 SER A 220 1 6
HELIX 9 9 ALA A 241 VAL A 255 1 15
HELIX 10 10 ASN A 265 ARG A 274 1 10
HELIX 11 11 PRO A 277 TRP A 286 1 10
HELIX 12 12 THR A 311 GLY A 319 1 9
HELIX 13 13 GLY A 335 GLY A 342 5 8
HELIX 14 14 SER A 355 VAL A 367 1 13
HELIX 15 15 SER A 371 THR A 383 1 13
HELIX 16 16 ASP A 390 VAL A 407 1 18
HELIX 17 17 VAL A 407 ALA A 420 1 14
HELIX 18 18 PRO A 440 GLY A 444 5 5
HELIX 19 19 GLU A 450 GLY A 456 1 7
HELIX 20 20 LEU A 457 ASP A 460 5 4
HELIX 21 21 THR A 466 GLY A 487 1 22
HELIX 22 22 ARG A 525 ARG A 534 1 10
SHEET 1 A 3 LEU A 9 ARG A 11 0
SHEET 2 A 3 GLN A 16 ARG A 18 -1 O LEU A 17 N VAL A 10
SHEET 3 A 3 VAL A 59 ASP A 61 1 O LEU A 60 N GLN A 16
SHEET 1 B11 ILE A 20 LYS A 23 0
SHEET 2 B11 PRO A 28 PRO A 36 -1 O ALA A 31 N ILE A 20
SHEET 3 B11 TYR A 98 PRO A 104 -1 O VAL A 101 N PHE A 32
SHEET 4 B11 VAL A 145 MET A 149 -1 O SER A 148 N ASN A 100
SHEET 5 B11 THR A 112 ILE A 118 1 N TRP A 117 O VAL A 147
SHEET 6 B11 GLY A 192 GLU A 202 1 O ASP A 193 N THR A 112
SHEET 7 B11 ARG A 224 GLN A 228 1 O GLN A 228 N GLY A 201
SHEET 8 B11 GLN A 325 VAL A 331 1 O LEU A 327 N LEU A 227
SHEET 9 B11 ARG A 424 PHE A 430 1 O TYR A 426 N VAL A 328
SHEET 10 B11 GLN A 509 LEU A 513 1 O LEU A 513 N ILE A 429
SHEET 11 B11 VAL A 520 ARG A 522 -1 O ARG A 521 N TYR A 510
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 SER 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 MET B 2 SER B 5 0
SHEET 2 E 2 ILE B 13 ASN B 16 -1 O THR B 15 N CYS B 3
SHEET 1 F 3 VAL B 34 CYS B 39 0
SHEET 2 F 3 CYS B 22 ARG B 27 -1 N LYS B 25 O GLY B 36
SHEET 3 F 3 LEU B 48 CYS B 53 -1 O GLU B 49 N SER B 26
SSBOND 1 CYS A 69 CYS A 96
SSBOND 2 CYS A 257 CYS A 272
SSBOND 3 CYS A 409 CYS A 529
SSBOND 4 CYS B 3 CYS B 22
SSBOND 5 CYS B 17 CYS B 39
SSBOND 6 CYS B 41 CYS B 52
SSBOND 7 CYS B 53 CYS B 59
LINK ND2 ASN A 350 C1 NAG A1509
CISPEP 1 TYR A 105 PRO A 106 0 0.18
CISPEP 2 CYS A 257 PRO A 258 0 0.25
CISPEP 3 PRO B 30 PRO B 31 0 -0.09
CISPEP 4 SER B 55 PRO B 56 0 -0.17
CRYST1 73.800 73.800 548.620 90.00 90.00 120.00 P 65 2 2 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 0.013550 0.007823 0.000000 0.00000
SCALE2 0.000000 0.015646 0.000000 0.00000
SCALE3 0.000000 0.000000 0.001823 0.00000
TER 4157 SER A 541
TER 4618 TYR B 61
MASTER 371 0 2 22 23 0 0 6 4824 2 33 48
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